Author: "A. Pinton" / Topic: biology - Searchworks@Jio Institute Digital Library Search Results

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583 results on '"A. Pinton"'

1. Dihydropyrimidinone-derived selenoesters efficacy and safety in an in vivo model of Aβ aggregation

Author: Rômulo Farias Santos Canto, Caroline Brandão Quines, Juliano B. Azeredo, Flávia Suelen de Oliveira Pereira, Cristiane Lucchese, Simone Pinton, Flavio A. R. Barbosa, Daiana Silva Ávila, and Antonio L. Braga
Subjects: Antioxidant, Amyloid beta, Aché, Oviposition, Transgene, medicine.medical_treatment, Pyrimidinones, Pharmacology, Toxicology, chemistry.chemical_compound, In vivo, Organoselenium Compounds, medicine, Animals, Caenorhabditis elegans, Amyloid beta-Peptides, Organisms, Genetically Modified, biology, General Neuroscience, biology.organism_classification, Acetylcholinesterase, language.human_language, Disease Models, Animal, Neuroprotective Agents, Levamisole, chemistry, Toxicity, biology.protein, language
Abstract: In a previous in vitro study, dihydropyrimidinone-derived selenoesteres demonstrated antioxidant properties, metal chelators and inhibitory acetylcholinesterase (AChE) activity, making these compounds promising candidates for Alzheimer’s Disease (AD) treatment. However, these effects have yet to be demonstrated in an in vivo animal model; therefore, this study aimed to evaluate the safety and efficacy of eight selenoester compounds in a Caenorhabditis elegans model using transgenic strains for amyloid-beta peptide (Aβ) aggregation. The L1 stage worms were acutely exposed (30 min) to the compounds at concentrations ranging from 5 to 200 μM and after 48 h the maintenance temperature was increased to 25 ° C for Aβ expression and aggregation. After 48 h, several parameters related to phenotypic manifestations of Aβ toxicity and mechanistic elucidation were analyzed. At the concentrations tested no significant toxicity of the compounds was found. The selenoester compound FA90 significantly reduced the rate of paralyzed worms and increased the number of swimming movements compared to the untreated worms. In addition, FA90 and FA130 improved egg-laying induced by levamisole and positively modulated HSP-6 and HSP-4 expression, thereby increasing reticular and mitochondrial protein folding response in C. elegans, which could attenuate Aβ aggregation in early exposure. Therefore, our initial screening using an alternative model demonstrated that FA90, among the eight selenoesters evaluated, was the most promising compound for AD evaluation screening in more complex animals.
Published: 2022

2. Beyond Residence Time: Quantifying Factors that Drive the Spatially Explicit Filtration Services of an Abundant Native Oyster Population

Author: Raymond E. Grizzle, Matthew Gray, Nicole Dix, P. Marcum, Daniele Pinton, Alberto Canestrelli, and David L. Kimbro
Subjects: 0106 biological sciences, Oyster, Watershed, 010504 meteorology & atmospheric sciences, Population, Aquatic Science, Spatial distribution, 01 natural sciences, Ecosystem services, biology.animal, 14. Life underwater, education, Reef, Ecology, Evolution, Behavior and Systematics, 0105 earth and related environmental sciences, geography, education.field_of_study, geography.geographical_feature_category, Ecology, biology, 010604 marine biology & hydrobiology, Estuary, biology.organism_classification, Oceanography, Crassostrea, Environmental science
Abstract: The Guana-Tolomato-Matanzas (GTM) system is a well-flushed estuary in Northeastern Florida, USA, and characterized as having an extraordinarily high abundance of oysters that resembles the populations described by Euro-American settlers. Historically, dense populations of oysters, such as those found in GTM, are believed to play an important role in water filtration; however, most research teams seeking to simulate this role have not had access to such robust populations to parametrize their models. To quantify the filtration service (FS) of Eastern oysters (Crassostrea virginica) in GTM at several spatial scales (i.e., reef, watershed, estuary), we implemented a model that solves for the hydrodynamics and depletion of particulate matter passing over model oyster populations, the latter of which were derived from detailed bay-wide surveys. The model results suggested that oyster reefs populating the GTM play an important role in water quality by filtering ~60% of the estuary’s volume within its residence time. Our approach teases apart the role of reef size, residence time, particle concentration, and other physical factors on the generation of FS at different spatial scales. Downstream effects were found to be very important for estuary FS, which depend on the spatial distribution of the reefs in the GTM and local and estuarine-scale hydrodynamics. Therefore, the difference between “realized” FS and the “potential” FS of a given reef may be substantial when considering the complex hydrodynamic and connectivity among populations at several scales. Our model results provide clear and actionable information for management of these oyster populations and conservation of their ecosystem services.
Published: 2021

3. Co-nanoencapsulated meloxicam and curcumin improves cognitive impairment induced by amyloid-beta through modulation of cyclooxygenase-2 in mice

Author: Renata Bem dos Santos, Anne Suély Pinto Savall, Simone Pinton, Cristiane Luchese, Edina da Luz Abreu, Caroline Brandão Quines, Marina Costa Monteiro Guedes, Maria Eduarda Ziani Gutierrez, Kelly Ayumi Nakama, Sandra Elisa Haas, and Daiana Silva Ávila
Subjects: 0301 basic medicine, Amyloid beta, Inflammation, Pharmacology, Neuroprotection, lcsh:RC346-429, memory, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Developmental Neuroscience, Downregulation and upregulation, alzheimer’s disease, curcumin, cyclooxygenase-2, lipid core nanocapsules, meloxicam, rats, inflammation, Medicine, lcsh:Neurology. Diseases of the nervous system, biology, business.industry, Alzheimer's disease, Pathophysiology, Meloxicam, 030104 developmental biology, chemistry, Curcumin, biology.protein, Cyclooxygenase, medicine.symptom, business, 030217 neurology & neurosurgery, medicine.drug, Research Article
Abstract: Alzheimer's disease (AD) is a progressive brain disorder and complex mechanisms are involved in the physiopathology of AD. However, there is data suggesting that inflammation plays a role in its development and progression. Indeed, some non-steroidal anti-inflammatory drugs, such as meloxicam, which act by inhibiting cyclooxygenase-2 (COX-2) have been used as neuroprotective agents in different neurodegenerative disease models. The purpose of this study was to investigate the effects of co-nanoencapsulated curcumin and meloxicam in lipid core nanocapsules (LCN) on cognitive impairment induced by amyloid-beta peptide injection in mice. LCN were prepared by the nanoprecipitation method. Male Swiss mice received a single intracerebroventricular injection of amyloid-beta peptide aggregates (fragment 25-35, 3 nmol/3 μL) or vehicle and were subsequently treated with curcumin-loaded LCN (10 mg/kg) or meloxicam-loaded LCN (5 mg/kg) or meloxicam + curcumin-co-loaded LCN (5 and 10 mg/kg, respectively). Treatments were given on alternate days for 12 days (i.e., six doses, once every 48 hours, by intragastric gavage). Our data showed that amyloid-beta peptide infusion caused long-term memory deficits in the inhibitory avoidance and object recognition tests in mice. In the inhibitory avoidance test, both meloxicam and curcumin formulations (oil or co-loaded LCN) improved amyloid-beta-induced memory impairment in mice. However, only meloxicam and curcumin-co-loaded LCN attenuated non-aversive memory impairment in the object recognition test. Moreover, the beneficial effects of meloxicam and curcumin-co-loaded LCN could be explained by the anti-inflammatory properties of these drugs through cortical COX-2 downregulation. Our study suggests that the neuroprotective potential of meloxicam and curcumin co-nanoencapsulation is associated with cortical COX-2 modulation. This study was approved by the Committee on Care and Use of Experimental Animal Resources, the Federal University of Pampa, Brazil (approval No. 02-2015) on April 16, 2015.
Published: 2021

4. Translational readthrough ofGLAnonsense mutations suggests dominant-negative effects exerted by the interaction of wild-type and missense variants

Author: Francesco Bernardi, Mattia Ferrarese, Mirko Pinotti, Saverio Marchi, Silvia Lombardi, Paolo Pinton, Alessio Branchini, Lombardi, S, Ferrarese, M, Marchi, S, Pinton, P, Pinotti, M, Bernardi, F, and Branchini, A
Subjects: Nonsense mutations, fabry disease, lysosomal disorders, translational readthrough, Nonsense mutation, Socio-culturale, Biology, 03 medical and health sciences, 0302 clinical medicine, Missense mutation, Molecular Biology, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, lysosomal disorder, Translational readthrough, Wild type, RNA, Cell Biology, Molecular biology, Phenotype, Amino acid, Enzyme, chemistry, 030220 oncology & carcinogenesis
Abstract: Nonsense mutations are relatively frequent in the rare X-linked lysosomal α-galactosidase A (α-Gal) deficiency (Fabry disease; FD), but have been poorly investigated. Here, we evaluated the responsiveness of a wide panel (n = 14) of GLA premature termination codons (PTCs) to the RNA-based approach of drug-induced readthrough through expression of recombinant α-Gal (rGal) nonsense and missense variants. We identified four high-responders to the readthrough-inducing aminoglycoside G418 in terms of full-length protein (C56X/W209X, ≥10% of wild-type rGal) and/or activity (Q119X/W209X/Q321X, ~5-7%), resulting in normal (Q119X/Q321X) or reduced (C56X, 0.27 ± 0.11; W209X, 0.35 ± 0.1) specific activity. To provide mechanistic insights we investigated the predicted amino acid substitutions mediated by readthrough (W209C/R, C56W/R), which resulted in correct lysosomal localization and appreciable protein/activity levels for the W209C/R variants. Differently, the C56W/R variants, albeit appreciably produced and localized into lysosomes, were inactive, thus indicating detrimental effects of substitutions at this position. Noticeably, when co-expressed with the functional W209C or W209R variants, the wild-type rGal displayed a reduced specific activity (0.5 ± 0.2 and 0.6 ± 0.2, respectively) that, considering the dimeric features of the α-Gal enzyme, suggested dominant-negative effects of missense variants through their interaction with the wild-type. Overall, we provide a novel mechanism through which amino acids inserted during readthrough might impact on the functional protein output. Our findings may also have implications for the interpretation of pathological phenotypes in heterozygous FD females, and for other human disorders involving dimeric or oligomeric proteins.
Published: 2019

5. Baricitinib restrains the immune dysregulation in patients with severe COVID-19

Author: Veronica Batani, Manuela Iezzi, Daniela Righetti, Stefano Ugel, Simone Caligola, Enrico Polati, Pier Giuseppe Pelicci, Walter Mosaner, Claudio Lunardi, Katia Donadello, Francesco De Sanctis, Alessandra Fiore, Varvara Petrova, Simonetta Friso, Federica Facciotti, Lorena Torroni, Andrea Claudio Comel, Paolo Bazzoni, Laura Pinton, Francesca Pizzolo, Mariaelisa Rampudda, Francesca Hofer, Elisa Tinazzi, Rosalinda Trovato, Vincenzo Bronte, Antonio Vella, Stefania Canè, Oliviero Olivieri, Chiara Musiu, and Roza Maria Barouni
Subjects: Male, 0301 basic medicine, Myeloid, T-Lymphocytes, medicine.medical_treatment, medicine.disease_cause, Severity of Illness Index, 03 medical and health sciences, 0302 clinical medicine, Immune system, Fraction of inspired oxygen, Oxygen therapy, medicine, Humans, Longitudinal Studies, B cell, Aged, Aged, 80 and over, B-Lymphocytes, Sulfonamides, biology, SARS-CoV-2, business.industry, COVID-19, Off-Label Use, General Medicine, Middle Aged, Immune dysregulation, COVID-19 Drug Treatment, 030104 developmental biology, medicine.anatomical_structure, Cytokine, Purines, 030220 oncology & carcinogenesis, Immunology, Commentary, biology.protein, Azetidines, Cytokines, Pyrazoles, Female, Antibody, business
Abstract: BACKGROUNDPatients with coronavirus disease 2019 (COVID-19) develop pneumonia generally associated with lymphopenia and a severe inflammatory response due to uncontrolled cytokine release. These mediators are transcriptionally regulated by the JAK/STAT signaling pathways, which can be disabled by small molecules.METHODSWe treated a group of patients (n = 20) with baricitinib according to an off-label use of the drug. The study was designed as an observational, longitudinal trial and approved by the local ethics committee. The patients were treated with 4 mg baricitinib twice daily for 2 days, followed by 4 mg per day for the remaining 7 days. Changes in the immune phenotype and expression of phosphorylated STAT3 (p-STAT3) in blood cells were evaluated and correlated with serum-derived cytokine levels and antibodies against severe acute respiratory syndrome-coronavirus 2 (anti-SARS-CoV-2). In a single treated patient, we also evaluated the alteration of myeloid cell functional activity.RESULTSWe provide evidence that patients treated with baricitinib had a marked reduction in serum levels of IL-6, IL-1β, and TNF-α, a rapid recovery of circulating T and B cell frequencies, and increased antibody production against the SARS-CoV-2 spike protein, all of which were clinically associated with a reduction in the need for oxygen therapy and a progressive increase in the P/F (PaO2, oxygen partial pressure/FiO2, fraction of inspired oxygen) ratio.CONCLUSIONThese data suggest that baricitinib prevented the progression to a severe, extreme form of the viral disease by modulating the patients' immune landscape and that these changes were associated with a safer, more favorable clinical outcome for patients with COVID-19 pneumonia.TRIAL REGISTRATIONClinicalTrials.gov NCT04438629.FUNDINGThis work was supported by the Fondazione Cariverona (ENACT Project) and the Fondazione TIM.
Published: 2020

6. PLCγ1 suppression promotes the adaptation of KRAS-mutant lung adenocarcinomas to hypoxia

Author: Tina M. Schnöder, Stefan Freigang, Georgia Konstantinidou, Ralph A. Schmid, Sabina Berezowska, Alessandro Rimessi, Paolo Pinton, Johanna Baumgartner, Chiara Pozzato, Florian H. Heidel, Maria Saliakoura, Matteo Rossi Sebastiano, Lukas Bubendorf, and Spasenija Savic Prince
Subjects: Male, Lung Neoplasms, lipid droplets, Mitochondrion, RAS transformed cells, medicine.disease_cause, Transgenic, stress, Mice, 0302 clinical medicine, Mice, Inbred NOD, 610 Medicine & health, induction, fatty acid oxidation, 0303 health sciences, growth factor, Adaptation, Physiological, Cell biology, Mitochondria, 030220 oncology & carcinogenesis, Adenocarcinoma, Female, KRAS, medicine.symptom, cancer calcium, Signal Transduction, Cell Survival, Physiological, Socio-culturale, Adenocarcinoma of Lung, Mice, Transgenic, Biology, Article, Proto-Oncogene Proteins p21(ras), 03 medical and health sciences, stress, phospholipase C gamma, RAS transformed cells, fatty acid oxidation, lipid droplets, growth factor, cancer calcium, activation, induction, medicine, Animals, Humans, Adaptation, 030304 developmental biology, Cell Proliferation, Tumor hypoxia, Cell growth, Phospholipase C gamma, Cell Biology, Hypoxia (medical), medicine.disease, Apoptosis, A549 Cells, Cancer cell, Mutation, Inbred NOD, 570 Life sciences, biology, Tumor Hypoxia, activation, Lipid Peroxidation, Energy Metabolism
Abstract: Mutant KRAS modulates the metabolic plasticity of cancer cells to confer a growth advantage during hypoxia, but the molecular underpinnings are largely unknown. Using a lipidomic screen, we found that PLCγ1 is suppressed during hypoxia in KRAS-mutant human lung adenocarcinoma cancer cell lines. Suppression of PLCγ1 in hypoxia promotes a less oxidative cancer cell metabolism state, reduces the formation of mitochondrial reactive oxygen species and switches tumour bioenergetics towards glycolysis by impairing Ca2+ entry into the mitochondria. This event prevents lipid peroxidation, antagonizes apoptosis and increases cancer cell proliferation. Accordingly, loss of function of Plcg1 in a mouse model of KrasG12D-driven lung adenocarcinoma increased the expression of glycolytic genes, boosted tumour growth and reduced survival. In patients with KRAS-mutant lung adenocarcinomas, low PLCγ1 expression correlates with increased expression of hypoxia markers and predicts poor patient survival. Thus, our work reveals a mechanism of cancer cell adaptation to hypoxia with potential therapeutic value.
Published: 2020

7. Asbestos induces mesothelial cell transformation via HMGB1-driven autophagy

Author: Keisuke Goto, Simone Patergnani, Mauro Tognon, Carlotta Giorgi, Ronghui Xu, Flavia Novelli, Harvey I. Pass, Angela Bononi, Sandra Pastorino, Mika Tanji, Giovanni Gaudino, Michele Carbone, Jiaming Xue, Natascia Caroccia, A. Umran Dogan, Haining Yang, Joelle S. Suarez, Paolo Pinton, and Tak W. Mak
Subjects: Cell death, Adult, Male, Mesothelioma, Programmed cell death, ATG5, Socio-culturale, chemical and pharmacologic phenomena, HMGB1, medicine.disease_cause, Asbestos, Autophagy, Malignant transformation, Mice, Occupational Exposure, medicine, LS4_6, Animals, Humans, HMGB1 Protein, Cells, Cultured, Aged, Mice, Knockout, Multidisciplinary, biology, Chemistry, Epithelial Cells, Biological Sciences, Middle Aged, Cell Transformation, Neoplastic, biology.protein, Cancer research, Carcinogenesis, Mesothelial Cell
Abstract: Asbestos causes malignant transformation of primary human mesothelial cells (HM), leading to mesothelioma. The mechanisms of asbestos carcinogenesis remain enigmatic, as exposure to asbestos induces HM death. However, some asbestos-exposed HM escape cell death, accumulate DNA damage, and may become transformed. We previously demonstrated that, upon asbestos exposure, HM and reactive macrophages releases the high mobility group box 1 (HMGB1) protein that becomes detectable in the tissues near asbestos deposits where HMGB1 triggers chronic inflammation. HMGB1 is also detectable in the sera of asbestos-exposed individuals and mice. Searching for additional biomarkers, we found higher levels of the autophagy marker ATG5 in sera from asbestos-exposed individuals compared to unexposed controls. As we investigated the mechanisms underlying this finding, we discovered that the release of HMGB1 upon asbestos exposure promoted autophagy, allowing a higher fraction of HM to survive asbestos exposure. HMGB1 silencing inhibited autophagy and increased asbestos-induced HM death, thereby decreasing asbestos-induced HM transformation. We demonstrate that autophagy was induced by the cytoplasmic and extracellular fractions of HMGB1 via the engagement of the RAGE receptor and Beclin 1 pathway, while nuclear HMGB1 did not participate in this process. We validated our findings in a novel unique mesothelial conditional HMGB1-knockout (HMGB1-cKO) mouse model. Compared to HMGB1 wild-type mice, mesothelial cells from HMGB1-cKO mice showed significantly reduced autophagy and increased cell death. Autophagy inhibitors chloroquine and desmethylclomipramine increased cell death and reduced asbestos-driven foci formation. In summary, HMGB1 released upon asbestos exposure induces autophagy, promoting HM survival and malignant transformation.
Published: 2020

8. A new algorithm for estimating ground elevation and vegetation characteristics in coastal salt marshes from high‐resolution UAV‐based LiDAR point clouds

Author: Andrew Ortega, Daniele Pinton, Alberto Canestrelli, Benjamin E. Wilkinson, and Peter Ifju
Subjects: geography, Vegetation height, geography.geographical_feature_category, biology, Geography, Planning and Development, Elevation, Point cloud, High resolution, Spartina alterniflora, biology.organism_classification, Atmospheric sciences, Lidar, Salt marsh, Earth and Planetary Sciences (miscellaneous), medicine, Environmental science, medicine.symptom, Vegetation (pathology), Earth-Surface Processes
Published: 2020

9. Nodulating white lupins take advantage of the reciprocal interplay between N and P nutritional responses

Author: Mauro Commisso, Nicola Tomasi, Anita Zamboni, Sara Buoso, Alessandro Franco, Laura Zanin, Zeno Varanini, Roberto Pinton, and Flavia Guzzo
Subjects: nutrient interactions, Physiology, chemistry.chemical_element, Plant Science, Biology, root exudates, Plant Roots, nitrogen, Nutrient, Symbiosis, Nitrogen Fixation, Genetics, Cluster root, Bradyrhizobium, saponin, Legume, Phosphorus, food and beverages, Cell Biology, General Medicine, leguminous, Lupinus, Bioavailability, White (mutation), chemistry, Agronomy, Nutrient deficiency, nodules
Abstract: The low bioavailability of nutrients, especially nitrogen (N) and phosphorus (P), is one of the most limiting factors for crop production. In this study, under N- and P-free nutrient solution (-N-P), nodulating white lupin plants developed some nodules and analogous cluster root structures characterized by different morphological, physiological, and molecular responses than those observed upon single nutrient deficiency (strong acidification of external media, a better nutritional status than -N+P and +N-P plants). The multi-elemental analysis highlighted that the concentrations of nutrients in white lupin plants were mainly affected by P availability. Gene-expression analyses provided evidence of interconnections between N and P nutritional pathways that are active to promote N and P balance in plants. The root exudome was mainly characterized by N availability in nutrient solution, and, in particular, the absence of N and P in the nutrient solution triggered a high release of phenolic compounds, nucleosides monophosphate and saponines by roots. These morphological, physiological, and molecular responses result from a close interplay between N and P nutritional pathways. They contribute to the good development of nodulating white lupin plants when grown on N- and P-free media. This study provides evidence that limited N and P availability in the nutrient solution can promote white lupin-Bradyrhizobium symbiosis, which is favourable for the sustainability of legume production.
Published: 2022

10. Analysis of Polycerate Mutants Reveals the Evolutionary Co-option of HOXD1 for Horn Patterning in Bovidae

Author: Daniele Bigi, Fiona Menzi, Slim Ben Jemaa, Marie-Christine Deloche, Aurélien Capitan, Johannes A. Lenstra, Marina Naval-Sanchez, Ivica Medugorac, Nathalie Hirter, Gwenola Tosser-Klopp, Diane Esquerre, Coralie M. Reich, Julia M. Paris, Rose-Marie Arbogast, Amandine Blin, Abdelhak Boukadiri, Aurélie Hintermann, Julie Rivière, Denis Duboule, Raphaël Cornette, Cécile Donnadieu, Marie-Dominique Wandhammer, Gjoko Bunevski, Louisa Gidney, Michael Stache, Isabelle Palhiere, Renate Schafberg, James Kijas, Claude Guintard, Joséphine Lesur, Jozsef Zakany, Rachel Rupp, Noelle E. Cockett, John Hedges, Ashleigh Haruda, Philippe Bardou, Olivier Putelat, Tracy Hadfield, Alain Pinton, Ockert Greyvenstein, Aurélie Allais-Bonnet, Este Van Marle-Koster, Eric Pailhoux, Coralie Danchin-Burge, David G. Riley, Cécile Grohs, Benjamin J. Hayes, Cord Drögemüller, Allice, Biologie de la Reproduction, Environnement, Epigénétique & Développement (BREED), Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-École nationale vétérinaire d'Alfort (ENVA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), Institut de Systématique, Evolution, Biodiversité (ISYEB ), Muséum national d'Histoire naturelle (MNHN)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université des Antilles (UA), Génétique Physiologie et Systèmes d'Elevage (GenPhySE ), Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-École nationale supérieure agronomique de Toulouse [ENSAT]-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), École nationale supérieure agronomique de Toulouse [ENSAT]-Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Martin-Luther-University Halle-Wittenberg, Génétique Animale et Biologie Intégrative (GABI), Université Paris-Saclay-AgroParisTech-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), University of Geneva [Switzerland], University of Bologna, Ludwig Maximilian University [Munich] (LMU), Archéologie d'Alsace, Archéologie et histoire ancienne : Méditerranée - Europe (ARCHIMEDE), Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Ministère de la Culture et de la Communication (MCC)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Texas A&M University [College Station], Utah State University (USU), Université de Carthage - University of Carthage, Ss. Cyril and Methodius University in Skopje, University of Bern, Manx Text, Manx Loaghtan Sheep Breeders (MLSBG), Utrecht University [Utrecht], Rent a Peasant, Archéozoologie, archéobotanique : sociétés, pratiques et environnements (AASPE), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Musée Zoologique de Strasbourg, Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), Acquisition et Analyse de Données pour l'Histoire naturelle (2AD), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Génome et Transcriptome - Plateforme Génomique ( GeT-PlaGe), Plateforme Génome & Transcriptome (GET), Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut de l'élevage (IDELE), Agriculture Victoria (AgriBio), Tshwane University of Technology [Pretoria] (TUT), Queensland Alliance for Agriculture and Food Innovation (QAAFI), University of Queensland [Brisbane], CSIRO Agriculture and Food (CSIRO), Ecole Polytechnique Fédérale de Lausanne (EPFL), Collège de France (CdF (institution)), Allais-Bonnet, Aurélie, Hintermann, Aurélie, Deloche, Marie-Christine, Cornette, Raphaël, Bardou, Philippe, Naval-Sanchez, Marina, Pinton, Alain, Haruda, Ashleigh, Grohs, Cécile, Zakany, Jozsef, Bigi, Daniele, Medugorac, Ivica, Putelat, Olivier, Greyvenstein, Ockert, Hadfield, Tracy, Jemaa, Slim Ben, Bunevski, Gjoko, Menzi, Fiona, Hirter, Nathalie, Paris, Julia M, Hedges, John, Palhiere, Isabelle, Rupp, Rachel, Lenstra, Johannes A, Gidney, Louisa, Lesur, Joséphine, Schafberg, Renate, Stache, Michael, Wandhammer, Marie-Dominique, Arbogast, Rose-Marie, Guintard, Claude, Blin, Amandine, Boukadiri, Abdelhak, Rivière, Julie, Esquerré, Diane, Donnadieu, Cécile, Danchin-Burge, Coralie, Reich, Coralie M, Riley, David G, Marle-Koster, Este van, Cockett, Noelle, Hayes, Benjamin J, Drögemüller, Cord, Kijas, Jame, Pailhoux, Eric, Tosser-Klopp, Gwenola, Duboule, Deni, Capitan, Aurélien, École nationale vétérinaire d'Alfort (ENVA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Ministère de la Culture et de la Communication (MCC)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Muséum national d'Histoire naturelle (MNHN), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), École nationale vétérinaire - Alfort (ENVA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-École nationale supérieure agronomique de Toulouse [ENSAT], Université de Genève = University of Geneva (UNIGE), University of Bologna/Università di Bologna, Ss. Cyril and Methodius University in Skopje (UKIM), École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), and Collège de France - Chaire internationale Évolution des génomes et développement
Subjects: 0106 biological sciences, Male, co-option, translocation, AcademicSubjects/SCI01180, regulatory mutation, 01 natural sciences, Hox genes, Hox gene, genes, 610 Medicine & health, Bilateria, time, Horns, 0303 health sciences, biology, Ecology, 630 Agriculture, Goats, [SDV.BDD.EO] Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Gene Expression Regulation, Developmental, alignment, Morphogenetic field, Biological Evolution, [SDV.BDD.MOR] Life Sciences [q-bio]/Development Biology/Morphogenesis, 590 Animals (Zoology), Haploinsufficiency, transcription, Biometry, Evolution, growth, Locus (genetics), Mice, Transgenic, [SDV.GEN.GA] Life Sciences [q-bio]/Genetics/Animal genetics, 010603 evolutionary biology, 03 medical and health sciences, goat and sheep genomics, Behavior and Systematics, framework, Genetics, Animals, Allele, Gene, Molecular Biology, Discoveries, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, Homeodomain Proteins, locus, Sheep, Horn (anatomy), AcademicSubjects/SCI01130, [SDV.BDD.MOR]Life Sciences [q-bio]/Development Biology/Morphogenesis, sequence, biology.organism_classification, [SDV.GEN.GA]Life Sciences [q-bio]/Genetics/Animal genetics, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Evolutionary biology, Mutation, genome-wide association, 570 Life sciences, goat and sheep genomic
Abstract: In the course of evolution, pecorans (i.e., higher ruminants) developed a remarkable diversity of osseous cranial appendages, collectively referred to as “headgear,” which likely share the same origin and genetic basis. However, the nature and function of the genetic determinants underlying their number and position remain elusive. Jacob and other rare populations of sheep and goats are characterized by polyceraty, the presence of more than two horns. Here, we characterize distinct POLYCERATE alleles in each species, both associated with defective HOXD1 function. We show that haploinsufficiency at this locus results in the splitting of horn bud primordia, likely following the abnormal extension of an initial morphogenetic field. These results highlight the key role played by this gene in headgear patterning and illustrate the evolutionary co-option of a gene involved in the early development of bilateria to properly fix the position and number of these distinctive organs of Bovidae.
Published: 2021

11. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author: Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan, Backues, Steven, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter, Barmada, Sami, Barreiro, Esther, Barreto, George, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav, Basagoudanavar, Suresh, Bassham, Diane, Bast, Robert, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne, Baumgarner, Bradley, Bayry, Jagadeesh, Beale, Rupert, Beau, Isabelle, Beaumatin, Florian, Bechara, Luiz, Beck, George, Beers, Michael, Begun, Jakob, Behrends, Christian, Behrens, Georg, Bei, Roberto, Bejarano, Eloy, Bel, Shai, Behl, Christian, Belaid, Amine, Belgareh-Touzé, Naïma, Bellarosa, Cristina, Belleudi, Francesca, Belló Pérez, Melissa, Bello-Morales, Raquel, Beltran, Jackeline Soares de Oliveira, Beltran, Sebastián, Benbrook, Doris Mangiaracina, Bendorius, Mykolas, Benitez, Bruno, Benito-Cuesta, Irene, Bensalem, Julien, Berchtold, Martin, Berezowska, Sabina, Bergamaschi, Daniele, Bergami, Matteo, Bergmann, Andreas, Berliocchi, Laura, Berlioz-Torrent, Clarisse, Bernard, Amélie, Berthoux, Lionel, Besirli, Cagri, Besteiro, Sebastien, Betin, Virginie, Beyaert, Rudi, Bezbradica, Jelena, Bhaskar, Kiran, Bhatia-Kissova, Ingrid, Bhattacharya, Resham, Bhattacharya, Sujoy, Bhattacharyya, Shalmoli, Bhuiyan, Md Shenuarin, Bhutia, Sujit Kumar, Bi, Lanrong, Bi, Xiaolin, Biden, Trevor, Bijian, Krikor, Billes, Viktor, Binart, Nadine, Bincoletto, Claudia, Birgisdottir, Asa, Bjorkoy, Geir, Blanco, Gonzalo, Blas-Garcia, Ana, Blasiak, Janusz, Blomgran, Robert, Blomgren, Klas, Blum, Janice, Boada-Romero, Emilio, Boban, Mirta, Boesze-Battaglia, Kathleen, Boeuf, Philippe, Boland, Barry, Bomont, Pascale, Bonaldo, Paolo, Bonam, Srinivasa Reddy, Bonfili, Laura, Bonifacino, Juan, Boone, Brian, Bootman, Martin, Bordi, Matteo, Borner, Christoph, Bornhauser, Beat, Borthakur, Gautam, Bosch, Jürgen, Bose, Santanu, botana, luis, Botas, Juan, Boulanger, Chantal, Boulton, Michael, Bourdenx, Mathieu, Bourgeois, Benjamin, Bourke, Nollaig, Bousquet, Guilhem, Boya, Patricia, Bozhkov, Peter, Bozi, Luiz, Bozkurt, Tolga, Brackney, Doug, Brandts, Christian, Braun, Ralf, Braus, Gerhard, Bravo-Sagua, Roberto, Bravo-San Pedro, José, Brest, Patrick, Bringer, Marie-Agnès, Briones-Herrera, Alfredo, Broaddus, V Courtney, Brodersen, Peter, Brodsky, Jeffrey, Brody, Steven, Bronson, Paola, Bronstein, Jeff, Brown, Carolyn, Brown, Rhoderick, Brum, Patricia, Brumell, John, Brunetti-Pierri, Nicola, Bruno, Daniele, Bryson-Richardson, Robert, Bucci, Cecilia, Buchrieser, Carmen, Bueno, Marta, Buitrago-Molina, Laura Elisa, Buraschi, Simone, Buch, Shilpa, Buchan, J Ross, Buckingham, Erin, Budak, Hikmet, Budini, Mauricio, Bultynck, Geert, Burada, Florin, Burgoyne, Joseph, Burón, M Isabel, Bustos, Victor, Büttner, Sabrina, Butturini, Elena, Byrd, Aaron, Cabas, Isabel, Cabrera-Benitez, Sandra, Cadwell, Ken, Cai, Jingjing, Cai, Lu, Cai, Qian, Cairó, Montserrat, Calbet, Jose, Caldwell, Guy, Caldwell, Kim, Call, Jarrod, Calvani, Riccardo, Calvo, Ana, Calvo-Rubio Barrera, Miguel, Camara, Niels OS, Camonis, Jacques, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Edward, Campbell-Valois, François-Xavier, Campello, Silvia, Campesi, Ilaria, Campos, Juliane, Camuzard, Olivier, Cancino, Jorge, Candido de Almeida, Danilo, Canesi, Laura, Caniggia, Isabella, Canonico, Barbara, Cantí, Carles, Cao, Bin, Caraglia, Michele, Caramés, Beatriz, Carchman, Evie, Cardenal-Muñoz, Elena, Cardenas, Cesar, Cardenas, Luis, Cardoso, Sandra, Carew, Jennifer, Carle, Georges, Carleton, Gillian, Carloni, Silvia, Carmona-Gutierrez, Didac, Carneiro, Leticia, Carnevali, Oliana, Carosi, Julian, Carra, Serena, Carrier, Alice, Carrier, Lucie, Carroll, Bernadette, Carter, A Brent, Carvalho, Andreia Neves, Casanova, Magali, Casas, Caty, Casas, Josefina, Cassioli, Chiara, Castillo, Eliseo, Castillo, Karen, Castillo-Lluva, Sonia, Castoldi, Francesca, Castori, Marco, Castro, Ariel, Castro-Caldas, Margarida, Castro-Hernandez, Javier, Castro-Obregon, Susana, Catz, Sergio, Cavadas, Claudia, Cavaliere, Federica, Cavallini, Gabriella, Cavinato, Maria, Cayuela, Maria, Cebollada Rica, Paula, Cecarini, Valentina, Cecconi, Francesco, Cechowska-Pasko, Marzanna, Cenci, Simone, Ceperuelo-Mallafré, Victòria, Cerqueira, João, Cerutti, Janete, Cervia, Davide, Cetintas, Vildan Bozok, Cetrullo, Silvia, Chae, Han-Jung, Chagin, Andrei, Chai, Chee-Yin, Chakrabarti, Gopal, Chakrabarti, Oishee, Chakraborty, Tapas, Chakraborty, Trinad, Chami, mounia, Chamilos, Georgios, Chan, David, Chan, Edmond, Chan, Edward, Chan, H.Y. Edwin, Chan, Helen, Chan, Hung, Chan, Matthew, Chan, Yau Sang, Chandra, Partha, Chang, Chih-Peng, Chang, Chunmei, Chang, Hao-Chun, Chang, Kai, Chao, Jie, Chapman, Tracey, Charlet-Berguerand, Nicolas, Chatterjee, Samrat, Chaube, Shail, Chaudhary, Anu, Chauhan, Santosh, Chaum, Edward, Checler, Frédéric, Cheetham, Michael, Chen, Chang-Shi, Chen, Guang-Chao, Chen, Jian-Fu, Chen, Liam, Chen, Leilei, Chen, Lin, Chen, Mingliang, Chen, Mu-Kuan, Chen, Ning, Chen, Quan, Chen, Ruey-Hwa, Chen, Shi, Chen, Wei, Chen, Weiqiang, Chen, Xin-Ming, Chen, Xiong-Wen, Chen, Xu, Chen, Yan, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Zhefan Stephen, Chen, Zhi, Chen, Zhi-Hua, Chen, Zhijian, Chen, Zhixiang, Cheng, Hanhua, Cheng, Jun, Cheng, Shi-Yuan, Cheng, Wei, Cheng, Xiaodong, Cheng, Xiu-Tang, Cheng, Yiyun, Cheng, Zhiyong, Chen, Zhong, Cheong, Heesun, Cheong, Jit Kong, Chernyak, Boris, Cherry, Sara, Cheung, Chi Fai Randy, Cheung, Chun Hei Antonio, Cheung, King-Ho, Chevet, Eric, Chi, Richard, Chiang, Alan Kwok Shing, Chiaradonna, Ferdinando, Chiarelli, Roberto, Chiariello, Mario, Chica, Nathalia, Chiocca, Susanna, Chiong, Mario, Chiou, Shih-Hwa, Chiramel, Abhilash, Chiurchiù, Valerio, Cho, Dong-Hyung, Choe, Seong-Kyu, Choi, Augustine, Choi, Mary, Choudhury, Kamalika Roy, Chow, Norman, Chu, Charleen, Chua, Jason, Chua, John Jia En, Chung, Hyewon, Chung, Kin Pan, Chung, Seockhoon, Chung, So-Hyang, Chung, Yuen-Li, Cianfanelli, Valentina, Ciechomska, Iwona, Cifuentes, Mariana, Cinque, Laura, Cirak, Sebahattin, Cirone, Mara, Clague, Michael, Clarke, Robert, Clementi, Emilio, Coccia, Eliana, Codogno, Patrice, Cohen, Ehud, Cohen, Mickael, Colasanti, Tania, Colasuonno, Fiorella, Colbert, Robert, Colell, Anna, Čolić, Miodrag, Coll, Nuria, Collins, Mark, Colombo, María, Colón-Ramos, Daniel, Combaret, Lydie, Comincini, Sergio, Cominetti, Márcia, Consiglio, Antonella, Conte, Andrea, Conti, Fabrizio, Contu, Viorica Raluca, Cookson, Mark, Coombs, Kevin, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corkery, Dale, Cordes, Nils, Cortese, Katia, Costa, Maria do Carmo, Costantino, Sarah, Costelli, Paola, Coto-Montes, Ana, Crack, Peter, Crespo, Jose, Criollo, Alfredo, Crippa, Valeria, Cristofani, Riccardo, Csizmadia, Tamas, Cuadrado, Antonio, Cui, Bing, Cui, Jun, Cui, Yixian, Cui, Yong, Culetto, Emmanuel, Cumino, Andrea, Cybulsky, Andrey, Czaja, Mark, Czuczwar, Stanislaw, D'Adamo, Stefania, D'Amelio, Marcello, D'Arcangelo, Daniela, D'Lugos, Andrew, D'Orazi, Gabriella, da Silva, James, Dafsari, Hormos Salimi, Dagda, Ruben, Dagdas, Yasin, Daglia, Maria, Dai, Xiaoxia, Dai, Yun, Dai, Yuyuan, Dal Col, Jessica, Dalhaimer, Paul, Dalla Valle, Luisa, Dallenga, Tobias, Dalmasso, Guillaume, Damme, Markus, Dando, Ilaria, Dantuma, Nico, Darling, April, Das, Hiranmoy, Dasarathy, Srinivasan, Dasari, Santosh, Dash, Srikanta, Daumke, Oliver, Dauphinee, Adrian, Davies, Jeffrey, Dávila, Valeria, Davis, Roger, Davis, Tanja, Dayalan Naidu, Sharadha, De Amicis, Francesca, De Bosscher, Karolien, De Felice, Francesca, De Franceschi, Lucia, De Leonibus, Chiara, de Mattos Barbosa, Mayara, De Meyer, Guido, De Milito, Angelo, De Nunzio, Cosimo, De Palma, Clara, De Santi, Mauro, De Virgilio, Claudio, De Zio, Daniela, Debnath, Jayanta, DeBosch, Brian, Decuypere, Jean-Paul, Deehan, Mark, Deflorian, Gianluca, DeGregori, James, Dehay, Benjamin, Del Rio, Gabriel, Delaney, Joe, Delbridge, Lea, Delorme-Axford, Elizabeth, Delpino, M Victoria, Demarchi, Francesca, Dembitz, Vilma, Demers, Nicholas, Deng, Hongbin, Deng, Zhiqiang, Dengjel, Joern, Dent, Paul, Denton, Donna, DePamphilis, Melvin, Der, Channing, Deretic, Vojo, Descoteaux, Albert, Devis, Laura, Devkota, Sushil, Devuyst, Olivier, Dewson, Grant, Dharmasivam, Mahendiran, Dhiman, Rohan, di Bernardo, Diego, Di Cristina, Manlio, Di Domenico, Fabio, Di Fazio, Pietro, Di Fonzo, Alessio, Di Guardo, Giovanni, Di Guglielmo, Gianni, Di Leo, Luca, Di Malta, Chiara, Di Nardo, Alessia, Di Rienzo, Martina, Di Sano, Federica, Diallinas, George, Diao, Jiajie, Diaz-Araya, Guillermo, Díaz-Laviada, Inés, Dickinson, Jared, Diederich, Marc, Dieudé, Mélanie, Dikic, Ivan, Ding, Shiping, Ding, Wen-Xing, Dini, Luciana, Dinić, Jelena, Dinic, Miroslav, Dinkova-Kostova, Albena, Dionne, Marc, Distler, Jörg, Diwan, Abhinav, Dixon, Ian, Djavaheri-Mergny, Mojgan, Dobrinski, Ina, Dobrovinskaya, Oxana, Dobrowolski, Radek, Dobson, Renwick, Đokić, Jelena, Dokmeci Emre, Serap, Donadelli, Massimo, Dong, Bo, Dong, Xiaonan, Dong, Zhiwu, Dorn Ii, Gerald, Dotsch, Volker, Dou, Huan, Dou, Juan, Dowaidar, Moataz, Dridi, Sami, Drucker, Liat, Du, Ailian, Du, Caigan, Du, Guangwei, Du, Hai-Ning, Du, Li-Lin, du Toit, André, Duan, Shao-Bin, Duan, Xiaoqiong, Duarte, Sónia, Dubrovska, Anna, Dunlop, Elaine, Dupont, Nicolas, Durán, Raúl, Dwarakanath, Bilikere, Dyshlovoy, Sergey, Ebrahimi-Fakhari, Darius, Eckhart, Leopold, Edelstein, Charles, Efferth, Thomas, Eftekharpour, Eftekhar, Eichinger, Ludwig, Eid, Nabil, Eisenberg, Tobias, Eissa, N Tony, Eissa, Sanaa, Ejarque, Miriam, El Andaloussi, Abdeljabar, El-Hage, Nazira, El-Naggar, Shahenda, Eleuteri, Anna Maria, El-Shafey, Eman, Elgendy, Mohamed, Eliopoulos, Aristides, Elizalde, María, Elks, Philip, Elsasser, Hans-Peter, Elsherbiny, Eslam, Emerling, Brooke, Emre, N., Eng, Christina, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelsen, Agnete, Enserink, Jorrit, Escalante, Ricardo, Esclatine, Audrey, Escobar-Henriques, Mafalda, Eskelinen, Eeva-Liisa, Espert, Lucile, Eusebio, Makandjou-Ola, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Facchiano, Francesco, Fadeel, Bengt, Fader, Claudio, Faesen, Alex, Fairlie, W Douglas, Falcó, Alberto, Falkenburger, Bjorn, Fan, Daping, Fan, Jie, Fan, Yanbo, Fang, Evandro, Fang, Yanshan, Fang, Yognqi, Fanto, Manolis, Farfel-Becker, Tamar, Faure, Mathias, Fazeli, Gholamreza, Fedele, Anthony, Feldman, Arthur, Feng, Du, Feng, Jiachun, Feng, Lifeng, Feng, Yibin, Feng, Yuchen, Feng, Wei, Fenz Araujo, Thais, Ferguson, Thomas, Fernández, Álvaro, Fernandez-Checa, Jose, Fernández-Veledo, Sonia, Fernie, Alisdair, Ferrante, Anthony, Ferraresi, Alessandra, Ferrari, Merari, Ferreira, Julio, Ferro-Novick, Susan, Figueras, Antonio, Filadi, Riccardo, Filigheddu, Nicoletta, Filippi-Chiela, Eduardo, Filomeni, Giuseppe, Fimia, Gian Maria, Fineschi, Vittorio, Finetti, Francesca, Finkbeiner, Steven, Fisher, Edward, Fisher, Paul, Flamigni, Flavio, Fliesler, Steven, Flo, Trude, Florance, Ida, Florey, Oliver, Florio, Tullio, Fodor, Erika, Follo, Carlo, Fon, Edward, Forlino, Antonella, Fornai, Francesco, Fortini, Paola, Fracassi, Anna, Fraldi, Alessandro, Franco, Brunella, Franco, Rodrigo, Franconi, Flavia, Frankel, Lisa, Friedman, Scott, Fröhlich, Leopold, Frühbeck, Gema, Fuentes, Jose, Fujiki, Yukio, Fujita, Naonobu, Fujiwara, Yuuki, Fukuda, Mitsunori, Fulda, Simone, Furic, Luc, Furuya, Norihiko, Fusco, Carmela, Gack, Michaela, Gaffke, Lidia, Galadari, Sehamuddin, Galasso, Alessia, Galindo, Maria, Gallolu Kankanamalage, 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Sylvie, Giustiniani, Julien, Gluschko, Alexander, Goder, Veit, Goginashvili, Alexander, Golab, Jakub, Goldstone, David, Golebiewska, Anna, Gomes, Luciana, Gomez, Rodrigo, Gómez-Sánchez, Rubén, Gomez-Puerto, Maria Catalina, Gomez-Sintes, Raquel, Gong, Qingqiu, Goni, Felix, González-Gallego, Javier, Gonzalez-Hernandez, Tomas, Gonzalez-Polo, Rosa, Gonzalez-Reyes, Jose, González-Rodríguez, Patricia, Goping, Ing Swie, Gorbatyuk, Marina, Gorbunov, Nikolai, Görgülü, Kıvanç, Gorojod, Roxana, Gorski, Sharon, Goruppi, Sandro, Gotor, Cecilia, Gottlieb, Roberta, Gozes, Illana, Gozuacik, Devrim, Graef, Martin, Gräler, Markus, Granatiero, Veronica, Grasso, Daniel, Gray, Joshua, Green, Douglas, Greenhough, Alexander, Gregory, Stephen, Griffin, Edward, Grinstaff, Mark, Gros, Frederic, Grose, Charles, Gross, Angelina, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Gu, Xueyan, Guan, Jun-Lin, Guardia, Carlos, Guda, Kishore, Guerra, Flora, Guerri, Consuelo, Guha, Prasun, Guillén, Carlos, Gujar, Shashi, 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Anna, Hernández, Agustín, Hernandez, Carlos, Hernandez-Diaz, Sergio, Hernandez-Gea, Virginia, Herpin, Amaury, Herreros, Judit, Hervás, Javier, Hesselson, Daniel, Hetz, Claudio, Heussler, Volker, Higuchi, Yujiro, Hilfiker, Sabine, Hill, Joseph, Hlavacek, William, Ho, Emmanuel, Ho, Idy, Ho, Philip Wing-Lok, Ho, Shu-Leong, Ho, Wan Yun, Hobbs, G Aaron, Hochstrasser, Mark, Hoet, Peter, Hofius, Daniel, Hofman, Paul, Höhn, Annika, Holmberg, Carina, Hombrebueno, Jose, Yi-Ren Hong, Chang-Won Hong, Hooper, Lora, Hoppe, Thorsten, Horos, Rastislav, Hoshida, Yujin, Hsin, I-Lun, Hsu, Hsin-Yun, Hu, Bing, Hu, Dong, Hu, Li-Fang, Hu, Ming Chang, Hu, Ronggui, Hu, Wei, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Jinlian, Hua, Yingqi, Huan, Chongmin, Huang, Canhua, Huang, Chuanshu, Huang, Chuanxin, Huang, Chunling, Huang, Haishan, Huang, Kun, Huang, Michael, Huang, Rui, Huang, Shan, Huang, Tianzhi, Huang, Xing, Huang, Yuxiang Jack, Huber, Tobias, Hubert, Virginie, Hubner, Christian, Hughes, Stephanie, 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Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gomez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Alvarez, E. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. Y., Antas, P., Antebi, A., Anton, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araujo, W. L., Araya, J., Arden, C., Arevalo, M. -A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A. R., Armstrong-James, D., Arnaune-Pelloquin, L., Aroca, A., Arroyo, D. S., Arsov, I., Artero, R., Asaro, D. M. L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A. G., Au, A. K., Auberger, P., Auner, H. W., Aurelian, L., Autelli, R., Avagliano, L., Avalos, Y., Aveic, S., Aveleira, C. A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M., Backer, J. M., Backues, S. K., Bae, D. -H., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, A., Baek, S. -H., Baek, S. H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C. T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banreti, A., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barila, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touze, N., Bellarosa, C., Belleudi, F., Bello Perez, M., Bello-Morales, R., Beltran, J. S. D. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. G., Besteiro, S., Betin, V. M., Beyaert, R., Bezbradica, J. S., Bhaskar, K., Bhatia-Kissova, I., Bhattacharya, R., Bhattacharya, S., Bhattacharyya, S., Bhuiyan, M. S., Bhutia, S. K., Bi, L., Bi, X., Biden, T. J., Bijian, K., Billes, V. A., Binart, N., Bincoletto, C., Birgisdottir, A. B., Bjorkoy, G., Blanco, G., Blas-Garcia, A., Blasiak, J., Blomgran, R., Blomgren, K., Blum, J. S., Boada-Romero, E., Boban, M., Boesze-Battaglia, K., Boeuf, P., Boland, B., Bomont, P., Bonaldo, P., Bonam, S. R., Bonfili, L., Bonifacino, J. S., Boone, B. A., Bootman, M. D., Bordi, M., Borner, C., Bornhauser, B. C., Borthakur, G., Bosch, J., Bose, S., Botana, L. M., Botas, J., Boulanger, C. M., Boulton, M. E., Bourdenx, M., Bourgeois, B., Bourke, N. M., Bousquet, G., Boya, P., Bozhkov, P. V., Bozi, L. H. M., Bozkurt, T. O., Brackney, D. E., Brandts, C. H., Braun, R. J., Braus, G. H., Bravo-Sagua, R., Bravo-San Pedro, J. M., Brest, P., Bringer, M. -A., Briones-Herrera, A., Broaddus, V. C., Brodersen, P., Brodsky, J. L., Brody, S. L., Bronson, P. G., Bronstein, J. M., Brown, C. N., Brown, R. E., Brum, P. C., Brumell, J. H., Brunetti-Pierri, N., Bruno, D., Bryson-Richardson, R. J., Bucci, C., Buchrieser, C., Bueno, M., Buitrago-Molina, L. E., Buraschi, S., Buch, S., Buchan, J. R., Buckingham, E. M., Budak, H., Budini, M., Bultynck, G., Burada, F., Burgoyne, J. R., Buron, M. I., Bustos, V., Buttner, S., Butturini, E., Byrd, A., Cabas, I., Cabrera-Benitez, S., Cadwell, K., Cai, J., Cai, L., Cai, Q., Cairo, M., Calbet, J. A., Caldwell, G. A., Caldwell, K. A., Call, J. A., Calvani, R., Calvo, A. C., Calvo-Rubio Barrera, M., Camara, N. O. S., Camonis, J. H., Camougrand, N., Campanella, M., Campbell, E. M., Campbell-Valois, F. -X., Campello, S., Campesi, I., Campos, J. C., Camuzard, O., Cancino, J., Candido de Almeida, D., Canesi, L., Caniggia, I., Canonico, B., Canti, C., Cao, B., Caraglia, M., Carames, B., Carchman, E. 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K., Chang, C. -P., Chang, C., Chang, H. -C., Chang, K., Chao, J., Chapman, T., Charlet-Berguerand, N., Chatterjee, S., Chaube, S. K., Chaudhary, A., Chauhan, S., Chaum, E., Checler, F., Cheetham, M. E., Chen, C. -S., Chen, G. -C., Chen, J. -F., Chen, L. L., Chen, L., Chen, M., Chen, M. -K., Chen, N., Chen, Q., Chen, R. -H., Chen, S., Chen, W., Chen, X. -M., Chen, X. -W., Chen, X., Chen, Y., Chen, Y. -G., Chen, Y. -J., Chen, Y. -Q., Chen, Z. S., Chen, Z., Chen, Z. -H., Chen, Z. J., Cheng, H., Cheng, J., Cheng, S. -Y., Cheng, W., Cheng, X., Cheng, X. -T., Cheng, Y., Cheng, Z., Cheong, H., Cheong, J. K., Chernyak, B. V., Cherry, S., Cheung, C. F. R., Cheung, C. H. A., Cheung, K. -H., Chevet, E., Chi, R. J., Chiang, A. K. S., Chiaradonna, F., Chiarelli, R., Chiariello, M., Chica, N., Chiocca, S., Chiong, M., Chiou, S. -H., Chiramel, A. I., Chiurchiu, V., Cho, D. -H., Choe, S. -K., Choi, A. M. K., Choi, M. E., Choudhury, K. R., Chow, N. S., Chu, C. T., Chua, J. P., Chua, J. J. E., Chung, H., Chung, K. P., Chung, S., Chung, S. -H., Chung, Y. -L., Cianfanelli, V., Ciechomska, I. A., Cifuentes, M., Cinque, L., Cirak, S., Cirone, M., Clague, M. J., Clarke, R., Clementi, E., Coccia, E. M., Codogno, P., Cohen, E., Cohen, M. M., Colasanti, T., Colasuonno, F., Colbert, R. A., Colell, A., Colic, M., Coll, N. S., Collins, M. O., Colombo, M. I., Colon-Ramos, D. A., Combaret, L., Comincini, S., Cominetti, M. R., Consiglio, A., Conte, A., Conti, F., Contu, V. R., Cookson, M. R., Coombs, K. M., Coppens, I., Corasaniti, M. T., Corkery, D. P., Cordes, N., Cortese, K., Costa, M. D. C., Costantino, S., Costelli, P., Coto-Montes, A., Crack, P. J., Crespo, J. L., Criollo, A., Crippa, V., Cristofani, R., Csizmadia, T., Cuadrado, A., Cui, B., Cui, J., Cui, Y., Culetto, E., Cumino, A. C., Cybulsky, A. V., Czaja, M. J., Czuczwar, S. J., D'Adamo, S., D'Amelio, M., D'Arcangelo, D., D'Lugos, A. C., D'Orazi, G., da Silva, J. A., Dafsari, H. S., Dagda, R. K., Dagdas, Y., Daglia, M., Dai, X., Dai, Y., Dal Col, J., Dalhaimer, P., Dalla Valle, L., Dallenga, T., Dalmasso, G., Damme, M., Dando, I., Dantuma, N. P., Darling, A. L., Das, H., Dasarathy, S., Dasari, S. K., Dash, S., Daumke, O., Dauphinee, A. N., Davies, J. S., Davila, V. A., Davis, R. J., Davis, T., Dayalan Naidu, S., De Amicis, F., De Bosscher, K., De Felice, F., De Franceschi, L., De Leonibus, C., de Mattos Barbosa, M. G., De Meyer, G. R. Y., De Milito, A., De Nunzio, C., De Palma, C., De Santi, M., De Virgilio, C., De Zio, D., Debnath, J., Debosch, B. J., Decuypere, J. -P., Deehan, M. A., Deflorian, G., Degregori, J., Dehay, B., Del Rio, G., Delaney, J. R., Delbridge, L. M. D., Delorme-Axford, E., Delpino, M. V., Demarchi, F., Dembitz, V., Demers, N. D., Deng, H., Deng, Z., Dengjel, J., Dent, P., Denton, D., Depamphilis, M. L., Der, C. J., Deretic, V., Descoteaux, A., Devis, L., Devkota, S., Devuyst, O., Dewson, G., Dharmasivam, M., Dhiman, R., di Bernardo, D., Di Cristina, M., Di Domenico, F., Di Fazio, P., Di Fonzo, A., Di Guardo, G., Di Guglielmo, G. M., Di Leo, L., Di Malta, C., Di Nardo, A., Di Rienzo, M., Di Sano, F., Diallinas, G., Diao, J., Diaz-Araya, G., Diaz-Laviada, I., Dickinson, J. M., Diederich, M., Dieude, M., Dikic, I., Ding, S., Ding, W. -X., Dini, L., Dinic, J., Dinic, M., Dinkova-Kostova, A. T., Dionne, M. S., Distler, J. H. W., Diwan, A., Dixon, I. M. C., Djavaheri-Mergny, M., Dobrinski, I., Dobrovinskaya, O., Dobrowolski, R., Dobson, R. C. J., Dokic, J., Dokmeci Emre, S., Donadelli, M., Dong, B., Dong, X., Dong, Z., Dorn II, G. W., Dotsch, V., Dou, H., Dou, J., Dowaidar, M., Dridi, S., Drucker, L., Du, A., Du, C., Du, G., Du, H. -N., Du, L. -L., du Toit, A., Duan, S. -B., Duan, X., Duarte, S. P., Dubrovska, A., Dunlop, E. A., Dupont, N., Duran, R. V., Dwarakanath, B. S., Dyshlovoy, S. A., Ebrahimi-Fakhari, D., Eckhart, L., Edelstein, C. L., Efferth, T., Eftekharpour, E., Eichinger, L., Eid, N., Eisenberg, T., Eissa, N. T., Eissa, S., Ejarque, M., El Andaloussi, A., El-Hage, N., El-Naggar, S., Eleuteri, A. M., El-Shafey, E. S., Elgendy, M., Eliopoulos, A. G., Elizalde, M. M., Elks, P. M., Elsasser, H. -P., Elsherbiny, E. S., Emerling, B. M., Emre, N. C. T., Eng, C. H., Engedal, N., Engelbrecht, A. -M., Engelsen, A. S. T., Enserink, J. M., Escalante, R., Esclatine, A., Escobar-Henriques, M., Eskelinen, E. -L., Espert, L., Eusebio, M. -O., Fabrias, G., Fabrizi, C., Facchiano, A., Facchiano, F., Fadeel, B., Fader, C., Faesen, A. C., Fairlie, W. D., Falco, A., Falkenburger, B. H., Fan, D., Fan, J., Fan, Y., Fang, E. F., Fang, Y., Fanto, M., Farfel-Becker, T., Faure, M., Fazeli, G., Fedele, A. O., Feldman, A. M., Feng, D., Feng, J., Feng, L., Feng, Y., Feng, W., Fenz Araujo, T., Ferguson, T. A., Fernandez, A. F., Fernandez-Checa, J. C., Fernandez-Veledo, S., Fernie, A. R., Ferrante, A. W., Ferraresi, A., Ferrari, M. F., Ferreira, J. C. B., Ferro-Novick, S., Figueras, A., Filadi, R., Filigheddu, N., Filippi-Chiela, E., Filomeni, G., Fimia, G. M., Fineschi, V., Finetti, F., Finkbeiner, S., Fisher, E. A., Fisher, P. B., Flamigni, F., Fliesler, S. J., Flo, T. H., Florance, I., Florey, O., Florio, T., Fodor, E., Follo, C., Fon, E. A., Forlino, A., Fornai, F., Fortini, P., Fracassi, A., Fraldi, A., Franco, B., Franco, R., Franconi, F., Frankel, L. B., Friedman, S. L., Frohlich, L. F., Fruhbeck, G., Fuentes, J. M., Fujiki, Y., Fujita, N., Fujiwara, Y., Fukuda, M., Fulda, S., Furic, L., Furuya, N., Fusco, C., Gack, M. U., Gaffke, L., Galadari, S., Galasso, A., Galindo, M. F., Gallolu Kankanamalage, S., Galluzzi, L., Galy, V., Gammoh, N., Gan, B., Ganley, I. G., Gao, F., Gao, H., Gao, M., Gao, P., Gao, S. -J., Gao, W., Gao, X., Garcera, A., Garcia, M. N., Garcia, V. E., Garcia-Del Portillo, F., Garcia-Escudero, V., Garcia-Garcia, A., Garcia-Macia, M., Garcia-Moreno, D., Garcia-Ruiz, C., Garcia-Sanz, P., Garg, A. D., Gargini, R., Garofalo, T., Garry, R. F., Gassen, N. C., Gatica, D., Ge, L., Ge, W., Geiss-Friedlander, R., Gelfi, C., Genschik, P., Gentle, I. E., Gerbino, V., Gerhardt, C., Germain, K., Germain, M., Gewirtz, D. A., Ghasemipour Afshar, E., Ghavami, S., Ghigo, A., Ghosh, M., Giamas, G., Giampietri, C., Giatromanolaki, A., Gibson, G. E., Gibson, S. B., Ginet, V., Giniger, E., Giorgi, C., Girao, H., Girardin, S. E., Giridharan, M., Giuliano, S., Giulivi, C., Giuriato, S., Giustiniani, J., Gluschko, A., Goder, V., Goginashvili, A., Golab, J., Goldstone, D. C., Golebiewska, A., Gomes, L. R., Gomez, R., Gomez-Sanchez, R., Gomez-Puerto, M. C., Gomez-Sintes, R., Gong, Q., Goni, F. M., Gonzalez-Gallego, J., Gonzalez-Hernandez, T., Gonzalez-Polo, R. A., Gonzalez-Reyes, J. A., Gonzalez-Rodriguez, P., Goping, I. S., Gorbatyuk, M. S., Gorbunov, N. V., Gorgulu, K., Gorojod, R. M., Gorski, S. M., Goruppi, S., Gotor, C., Gottlieb, R. A., Gozes, I., Gozuacik, D., Graef, M., Graler, M. H., Granatiero, V., Grasso, D., Gray, J. P., Green, D. R., Greenhough, A., Gregory, S. L., Griffin, E. F., Grinstaff, M. W., Gros, F., Grose, C., Gross, A. S., Gruber, F., Grumati, P., Grune, T., Gu, X., Guan, J. -L., Guardia, C. M., Guda, K., Guerra, F., Guerri, C., Guha, P., Guillen, C., Gujar, S., Gukovskaya, A., Gukovsky, I., Gunst, J., Gunther, A., Guntur, A. R., Guo, C., Guo, H., Guo, L. -W., Guo, M., Gupta, P., Gupta, S. K., Gupta, S., Gupta, V. B., Gupta, V., Gustafsson, A. B., Gutterman, D. D., H. B, R., Haapasalo, A., Haber, J. E., Hac, A., Hadano, S., Hafren, A. J., Haidar, M., Hall, B. S., Hallden, G., Hamacher-Brady, A., Hamann, A., Hamasaki, M., Han, W., Hansen, M., Hanson, P. I., Hao, Z., Harada, M., Harhaji-Trajkovic, L., Hariharan, N., Haroon, N., Harris, J., Hasegawa, T., Hasima Nagoor, N., Haspel, J. A., Haucke, V., Hawkins, W. D., Hay, B. A., Haynes, C. M., Hayrabedyan, S. B., Hays, T. S., He, C., He, Q., He, R. -R., He, Y. -W., He, Y. -Y., Heakal, Y., Heberle, A. M., Hejtmancik, J. F., Helgason, G. V., Henkel, V., Herb, M., Hergovich, A., Herman-Antosiewicz, A., Hernandez, A., Hernandez, C., Hernandez-Diaz, S., Hernandez-Gea, V., Herpin, A., Herreros, J., Hervas, J. H., Hesselson, D., Hetz, C., Heussler, V. T., Higuchi, Y., Hilfiker, S., Hill, J. A., Hlavacek, W. S., Ho, E. A., Ho, I. H. T., Ho, P. W. -L., Ho, S. -L., Ho, W. Y., Hobbs, G. A., Hochstrasser, M., Hoet, P. H. M., Hofius, D., Hofman, P., Hohn, A., Holmberg, C. I., Hombrebueno, J. R., Yi-Ren Hong, C. -W. H., Hooper, L. V., Hoppe, T., Horos, R., Hoshida, Y., Hsin, I. -L., Hsu, H. -Y., Hu, B., Hu, D., Hu, L. -F., Hu, M. C., Hu, R., Hu, W., Hu, Y. -C., Hu, Z. -W., Hua, F., Hua, J., Hua, Y., Huan, C., Huang, C., Huang, H., Huang, K., Huang, M. L. H., Huang, R., Huang, S., Huang, T., Huang, X., Huang, Y. J., Huber, T. B., Hubert, V., Hubner, C. A., Hughes, S. M., Hughes, W. E., Humbert, M., Hummer, G., Hurley, J. H., Hussain, S., Hussey, P. J., Hutabarat, M., Hwang, H. -Y., Hwang, S., Ieni, A., Ikeda, F., Imagawa, Y., Imai, Y., Imbriano, C., Imoto, M., Inman, D. M., Inoki, K., Iovanna, J., Iozzo, R. V., Ippolito, G., Irazoqui, J. E., Iribarren, P., Ishaq, M., Ishikawa, M., Ishimwe, N., Isidoro, C., Ismail, N., Issazadeh-Navikas, S., Itakura, E., Ito, D., Ivankovic, D., Ivanova, S., Iyer, A. K. V., Izquierdo, J. M., Izumi, M., Jaattela, M., Jabir, M. S., Jackson, W. T., Jacobo-Herrera, N., Jacomin, A. -C., Jacquin, E., Jadiya, P., Jaeschke, H., Jagannath, C., Jakobi, A. J., Jakobsson, J., Janji, B., Jansen-Durr, P., Jansson, P. J., Jantsch, J., Januszewski, S., Jassey, A., Jean, S., Jeltsch-David, H., Jendelova, P., Jenny, A., Jensen, T. E., Jessen, N., Jewell, J. 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B., Schramm, M., Schroder, B., Schuh, K., Schuller, C., Schulze, R. J., Schurmanns, L., Schwamborn, J. C., Schwarten, M., Scialo, F., Sciarretta, S., Scott, M. J., Scotto, K. W., Scovassi, A. I., Scrima, A., Scrivo, A., Sebastian, D., Sebti, S., Sedej, S., Segatori, L., Segev, N., Seglen, P. O., Seiliez, I., Seki, E., Selleck, S. B., Sellke, F. W., Selsby, J. T., Sendtner, M., Senturk, S., Seranova, E., Sergi, C., Serra-Moreno, R., Sesaki, H., Settembre, C., Setty, S. R. G., Sgarbi, G., Sha, O., Shacka, J. J., Shah, J. A., Shang, D., Shao, C., Shao, F., Sharbati, S., Sharkey, L. M., Sharma, D., Sharma, G., Sharma, K., Sharma, P., Sharma, S., Shen, H. -M., Shen, H., Shen, J., Shen, M., Shen, W., Shen, Z., Sheng, R., Sheng, Z., Sheng, Z. -H., Shi, J., Shi, X., Shi, Y. -H., Shiba-Fukushima, K., Shieh, J. -J., Shimada, Y., Shimizu, S., Shimozawa, M., Shintani, T., Shoemaker, C. J., Shojaei, S., Shoji, I., Shravage, B. V., Shridhar, V., Shu, C. -W., Shu, H. -B., Shui, K., Shukla, A. K., Shutt, T. E., Sica, V., Siddiqui, A., Sierra, A., Sierra-Torre, V., Signorelli, S., Sil, P., Silva, B. J. D. A., Silva, J. D., Silva-Pavez, E., Silvente-Poirot, S., Simmonds, R. E., Simon, A. K., Simon, H. -U., Simons, M., Singh, A., Singh, L. P., Singh, R., Singh, S. V., Singh, S. K., Singh, S. B., Singh, S., Singh, S. P., Sinha, D., Sinha, R. A., Sinha, S., Sirko, A., Sirohi, K., Sivridis, E. L., Skendros, P., Skirycz, A., Slaninova, I., Smaili, S. S., Smertenko, A., Smith, M. D., Soenen, S. J., Sohn, E. J., Sok, S. P. M., Solaini, G., Soldati, T., Soleimanpour, S. A., Soler, R. M., Solovchenko, A., Somarelli, J. A., Sonawane, A., Song, F., Song, H. K., Song, J. -X., Song, K., Song, Z., Soria, L. R., Sorice, M., Soukas, A. A., Soukup, S. -F., Sousa, D., Sousa, N., Spagnuolo, P. A., Spector, S. A., Srinivas Bharath, M. M., S, t. Clair D., Stagni, V., Staiano, L., Stalnecker, C. A., Stankov, M. V., Stathopulos, P. B., Stefan, K., Stefan, S. M., Stefanis, L., Steffan, J. S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A. M., Stupack, D. G., Su, H., Su, L. -Y., Su, L., Suarez-Fontes, A. M., Subauste, C. S., Subbian, S., Subirada, P. V., Sudhandiran, G., Sue, C. M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M. -X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K. K. S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J. D., Sze, S. C. W., Szewczyk, N. J., Tabecka-Lonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S. W. G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S. Y., Tampellini, D., Tamura, A., Tan, C. T., Tan, E. -K., Tan, Y. -Q., Tanaka, M., Tang, D., Tang, J., Tang, T. -S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G. A., Taylor, J. M., Tchetina, E., Tee, A. R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K. A., Tencomnao, T., Tenreiro, S., Tepikin, A. V., Testillano, P. S., Tettamanti, G., Tharaux, P. -L., Thedieck, K., Thekkinghat, A. A., Thellung, S., Thinwa, J. W., Thirumalaikumar, V. P., Thomas, S. M., Thomes, P. G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V. I., Todi, S. V., Todorova, K., Toivonen, J. M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomic, S., Tong, B. C. -K., Tong, C., Tong, X., Tooze, S. A., Torgersen, M. L., Torii, S., Torres-Lopez, L., Torriglia, A., Towers, C. G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q. -G., Travassos, L. H., Trelford, C. B., Tremel, S., Trougakos, I. P., Tsao, B. P., Tschan, M. P., Tse, H. -F., Tse, T. F., Tsugawa, H., Tsvetkov, A. S., Tumbarello, D. A., Tumtas, Y., Tunon, M. J., Turcotte, S., Turk, B., Turk, V., Turner, B. J., Tuxworth, R. I., Tyler, J. K., Tyutereva, E. V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H. H., Ulamek-Koziol, M., Ulasov, I. V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Ustun, S., Uversky, V. N., Vaccari, T., Vaccaro, M. I., Vahsen, B. F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M. J., Valko, A., Vallee, R. B., Valverde, A. M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S. J. L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M. A., Vannini, N., Vanrell, M. C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M. H., Vats, S., Vavvas, D. G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velazquez, A. P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A. T., Victor, V. M., Vidal, M., Vidoni, C., Vieira, O. V., Vierstra, R. D., Vigano, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J. M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M. T., Visnjic, D., Vitale, I., Vocadlo, D. J., Voitsekhovskaja, O. V., Volonte, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M. A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K. A., Wakatsuki, S., Walker, D. W., Walker, M. J., Walker, S. A., Walter, J., Wandosell, F. G., Wang, B., Wang, C. -Y., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, H. -G., Wang, J., Wang, K., Wang, L., Wang, M. H., Wang, M., Wang, N., Wang, P., Wang, Q. J., Wang, Q., Wang, Q. K., Wang, Q. A., Wang, W. -T., Wang, W., Wang, X., Wang, Y., Wang, Y. -Y., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzynska, A., Weaver, T. E., Wegrzyn, G., Wehman, A. M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergraber, O. H., Weihl, C. C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R. H., Wen, X., Werner, A., Weykopf, B., Wheatley, S. P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S. -J., Yan, Z., Yanagi, Y., Yang, C., Yang, D. -S., Yang, H., Yang, H. -T., Yang, J. -M., Yang, J., Yang, L., Yang, M., Yang, P. -M., Yang, Q., Yang, S., Yang, S. -F., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y. -G., Yao, Y. -M., Yasui, T., Yazdankhah, M., Yen, P. M., Yi, C., Yin, X. -M., Yin, Y., Yin, Z., Ying, M., Ying, Z., Yip, C. K., Yiu, S. P. T., Yoo, Y. H., Yoshida, K., Yoshii, S. R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, L., Yu, M. -L., Yu, S. -W., Yu, V. C., Yu, W. H., Yu, Z., Yuan, J., Yuan, L. -Q., Yuan, S., Yuan, S. -S. F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R. L., Zacks, D. N., Zaffagnini, G., Zambelli, V. O., Zanella, I., Zang, Q. S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K. S., Zarebkohan, A., Zarrouk, A., Zeitlin, S. O., Zeng, J., Zeng, J. -D., Zerovnik, E., Zhan, L., Zhang, B., Zhang, D. D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

12. Effects of Fusarium metabolites beauvericin and enniatins alone or in mixture with deoxynivalenol on weaning piglets

Author: Isabelle P. Oswald, Barbara Novak, Caroline Emsenhuber, Dian Schatzmayr, Amanda Lopes Hasuda, Ana Paula Frederico Rodrigues Loureiro Bracarense, Viviane Mayumi Maruo, Manon Neves, Mahdi Ghanbari, Philippe Pinton, Silvia Wein, Biomin Research Center, State University of Londrina = Universidade Estadual de Londrina, ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Universidade Federal do Tocantins (UFT), Universidade Federal do Tocantins, Biosynthèse & Toxicité des Mycotoxines (ToxAlim-BioToMyc), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), This research was funded by Austrian Research Promotion Agency (FFG) via the research project Early Stage, grant number 879467 and by the French ANR project 'EmergingMyco' (ANR-18-CE34-0014). Amanda L. Hasuda received a fellowship from the Coordenaç˜ao de Aperfeiçoamento de Pessoal de Nível Superior-CAPES/Cofecub (Grant 0389/2019). This study was financed in part by the Coordenaç˜ao de Aperfeiçoamento de Pessoal de Nível Superior - Brasil (CAPES) - FinanceCode 001., and ANR-18-CE34-0014,EmergingMyco,Les mycotoxines émergentes : un nouveau risque pour l'Homme et les animaux ?(2018)
Subjects: Fusarium, Swine, [SDV]Life Sciences [q-bio], Weaning, Gut microbiota, Gut flora, Toxicology, Weight Gain, Jejunum, 03 medical and health sciences, chemistry.chemical_compound, Eating, Animal science, Depsipeptides, medicine, Animals, Mycotoxin, 030304 developmental biology, 0303 health sciences, biology, 030306 microbiology, food and beverages, General Medicine, Mycotoxins, biology.organism_classification, Biomarker of effect, Beauvericin, 3. Good health, Gastrointestinal Microbiome, Intestines, medicine.anatomical_structure, chemistry, Liver, Fungal metabolites, Lymph, medicine.symptom, Trichothecenes, Weight gain, Histological alterations, Cyclic hexadepsipeptides, Food Science
Abstract: International audience; The impact of the Fusarium-derived metabolites beauvericin, enniatin B and B1 (EB) alone or in combination with deoxynivalenol (DON) was investigated in 28-29 days old weaning piglets over a time period of 14 days. The coapplication of EB and DON (EB + DON) led to a significant decrease in the weight gain of the animals. Liver enzyme activities in plasma were significantly decreased at day 14 in piglets receiving the EB + DON-containing diet compared to piglets receiving the control diet. All mycotoxin-contaminated diets led to moderate to severe histological lesions in the jejunum, the liver and lymph nodes. Shotgun metagenomics revealed a significant effect of EB-application on the gut microbiota. Our results provide novel insights into the harmful impact of emerging mycotoxins alone or with DON on the performance, gut health and immunological parameters in pigs.
Published: 2021

13. ACE2 expression and localization are regulated by CFTR: implications beyond cystic fibrosis

Author: Roberta Rizzo, Martina Duca, Francesco Blasi, Erika Tedesco, Sara Leo, Marco Cipolli, Valentino Bezzerri, Giuseppe Lippi, Sonia Volpi, Anna Tamanini, Debora Olioso, Martina Api, Alessia Finotti, Giulio Cabrini, Paolo Pinton, Valentina Gentili, Monica Borgatti, Chiara Papi, Roberto Gambari, and Alessandro Rimessi
Subjects: biology, Coronavirus disease 2019 (COVID-19), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Immunology, Angiotensin-converting enzyme 2, biology.protein, medicine, Interleukin, Pulmonary disease, Receptor, medicine.disease, Cystic fibrosis, Cystic fibrosis transmembrane conductance regulator
Abstract: As an inherited disorder characterized by severe pulmonary disease, cystic fibrosis (CF) could be considered a comorbidity for coronavirus disease 2019 (COVID-19)1. Instead, CF seems to constitute an advantage in COVID-19 infection2-5.To clarify whether host factors expressed by the CF epithelia may influence COVID-19 progression, we investigated the expression of SARS-CoV-2 receptor and coreceptors in primary airway epithelial cells. We found that angiotensin converting enzyme 2 (ACE2) expression and localization are regulated by cystic fibrosis transmembrane conductance regulator (CFTR) channels. Consistently, our results indicate that dysfunctional CFTR channels alter susceptibility to SARS-CoV-2 infection, resulting in reduced viral infection in CF cells. Depending on the pattern of ACE2 expression, the SARS-CoV-2 spike (S) protein induced high levels of Interleukin (IL)-6 in healthy donor-derived primary airway epithelial cells but a very weak response in primary CF cells. Collectively, these data support the hypothesis that CF condition is unfavorable for SARS-CoV-2 infection.
Published: 2021

14. Identification of an Isoflavonoid Transporter Required for the Nodule Establishment of the Rhizobium-Fabaceae Symbiotic Interaction

Author: Wanda Biała-Leonhard, Laura Zanin, Stefano Gottardi, Rita de Brito Francisco, Silvia Venuti, Fabio Valentinuzzi, Tanja Mimmo, Stefano Cesco, Barbara Bassin, Enrico Martinoia, Roberto Pinton, Michał Jasiński, Nicola Tomasi, University of Zurich, Jasiński, Michał, and Tomasi, Nicola
Subjects: Cell signaling, Plant Science, 580 Plants (Botany), Bradyrhizobium, nitrogen, Rhizobia, Bradyrhizobium, genistein, Lupinus albus, MATE transporter, nitrogen, phosphorus, plant-microbe interaction, SB1-1110, genistein, Isoflavonoid, Symbiosis, 10126 Department of Plant and Microbial Biology, 1110 Plant Science, 10211 Zurich-Basel Plant Science Center, phosphorus, MATE transporter, plant-microbe interaction, biology, Chemistry, Plant culture, Fabaceae, biology.organism_classification, Biochemistry, Lupinus albus, Rhizobium, Bacteria
Abstract: Nitrogen (N) as well as Phosphorus (P) are key nutrients determining crop productivity. Legumes have developed strategies to overcome nutrient limitation by, for example, forming a symbiotic relationship with N-fixing rhizobia and the release of P-mobilizing exudates and are thus able to grow without supply of N or P fertilizers. The legume-rhizobial symbiosis starts with root release of isoflavonoids that act as signaling molecules perceived by compatible bacteria. Subsequently, bacteria release nod factors, which induce signaling cascades allowing the formation of functional N-fixing nodules. We report here the identification and functional characterization of a plasma membrane-localized MATE-type transporter (LaMATE2) involved in the release of genistein from white lupin roots. The LaMATE2 expression in the root is upregulated under N deficiency as well as low phosphate availability, two nutritional deficiencies that induce the release of this isoflavonoid. LaMATE2 silencing reduced genistein efflux and even more the formation of symbiotic nodules, supporting the crucial role of LaMATE2 in isoflavonoid release and nodulation. Furthermore, silencing of LaMATE2 limited the P-solubilization activity of lupin root exudates. Transport assays in yeast vesicles demonstrated that LaMATE2 acts as a proton-driven isoflavonoid transporter.
Published: 2021

15. A liquid biopsy-based approach identifies myeloid cells, STAT3 and arginase-1 as predictors of glioma risk score and patients' survival

Author: Elena Masetto, Stefania Canè, Vittorina Zagonel, Susanna Mandruzzato, Domenico D'Avella, Vincenzo Bronte, Paola Del Bianco, Laura Pinton, Sara Magri, Giuseppe Lombardi, Francesco Volpin, Marta Padovan, Daniela Basso, and Alessandro Della Puppa
Subjects: Oncology, medicine.medical_specialty, Framingham Risk Score, biology, business.industry, medicine.disease, Arginase, Internal medicine, Glioma, Myeloid cells, medicine, biology.protein, Liquid biopsy, business, STAT3
Abstract: Background Although gliomas are strictly confined to the central nervous system, their negative influence over the immune system can extend to peripheral circulation. The immune suppression exerted by myeloid cells is capable of affecting both response to therapy and disease outcome. Here we analyzed the expansion of several myeloid parameters in the blood of low- and high-grade gliomas and assessed their relevance as biomarkers of disease and clinical outcome. Methods Peripheral blood was obtained from 134 low- and high-grade glioma patients before surgery and treatment. Myeloid cell subsets such as total CD14+, CD14+/p-STAT3+, CD14+/PD-L1+, CD15+ cells and 4 myeloid derived suppressor cell (MDSC) subsets, were evaluated by multiparametric flow cytometry. Arginase-1 (ARG1) quantity and activity was determined in the plasma. Principal component analysis was performed to define correlations between myeloid markers. Multivariable logistic regression model was used to obtain a diagnostic score to discriminate glioma patients from healthy controls, and between each glioma grade. A glioblastoma prognostic model was determined by multiple Cox regression using clinical and myeloid parameters. Results In the blood of glioma patients, changes in myeloid parameters associated with immune suppression were identified and allowed us to define a diagnostic score calculating the risk of being a glioma patient, that included CD15+ cells, MDSC1, MDSC3, p-STAT3 and ARG1 activity. Of note, the same parameters, together with age, can also be used to calculate the risk score in differentiating each glioma grade. Finally, a prognostic model for glioblastoma patients stemmed out from a Cox multiple analysis, highlighting the role of MDSC, p-STAT3 and ARG1 activity together with clinical parameters in predicting the patient outcome. Conclusions This work emphasizes the role of systemic immune suppression carried out by myeloid cells in gliomas. The identification of biomarkers associated with immune landscape, diagnosis and outcome of glioblastoma patients lays the ground for their clinical use for stratification and follow up.
Published: 2021

16. Potential Effects of Essential Oils Extracted from Mediterranean Aromatic Plants on Target Weeds and Soil Microorganisms

Author: Vito Armando Laudicina, Samuele Pinton, Fabrizio Araniti, Amira Jouini, Eristanna Palazzolo, Luigi Badalucco, Mercedes Verdeguer, Amira Jouini, Mercedes Verdeguer Sancho, Samuele Pinton, Fabrizio Araniti, Eristanna Palazzolo, Luigi Badalucco, and Vito Armando Laudicina
Subjects: 0106 biological sciences, Irrigation, Settore AGR/13 - Chimica Agraria, BOTANICA, Microbial biomass, Biomass, Plant Science, Echinochloa, natural herbicide, 01 natural sciences, Article, Santolina chamaecyparissus, microbial bioma, Microbial respiration, lcsh:Botany, Avena fatua, Ecology, Evolution, Behavior and Systematics, Ecology, biology, Bacteria, Chemistry, Fungi, food and beverages, 04 agricultural and veterinary sciences, biology.organism_classification, Weed control, lcsh:QK1-989, Horticulture, Phytotoxicity, 040103 agronomy & agriculture, 0401 agriculture, forestry, and fisheries, Natural herbicides, Weed, 010606 plant biology & botany
Abstract: Essential oils (EOs), extracted from aromatic plants, have been proposed as candidates to develop natural herbicides. This study aimed to evaluate the herbicidal potential of Thymbra capitata (L.) Cav., Mentha &times, piperita L. and Santolina chamaecyparissus L. essential oils (EOs) on Avena fatua L., Echinochloa crus-galli (L.) P. Beauv, Portulaca oleracea L. and Amaranthus retroflexus L. and their effects on soil microorganisms. A pot experiment was set up and three EOs at three doses were applied by irrigation. Efficacy and effects of EOs on weed growth were determined. Soil microbial biomass carbon and nitrogen, microbial respiration, and the main microbial groups were determined at days 7, 28 and 56. EOs demonstrated herbicidal activity, increasing their toxicity with the dose. T. capitata was the most effective against all weeds at the maximum dose. P. oleracea was the most resistant weed. Soil microorganisms, after a transient upheaval period induced by the addition of EOs, recovered their initial function and biomass. T. capitata EO at the highest dose did not allow soil microorganisms to recover their initial functionality. EOs exhibited great potential as natural herbicides but the optimum dose of application must be identified to control weeds and not negatively affect soil microorganisms.
Published: 2020

17. Identification of an isoflavonoid transporter required for the nodule establishment of the Rhizobium-Fabaceae symbiotic interaction

Author: Roberto Pinton, Tanja Mimmo, Nicola Tomasi, Rita Francisco, Silvia Venuti, Stefano Cesco, Barbara Bassin, Stefano Gottardi, Enrico Martinoia, Michał Jasiński, Laura Zanin, Wanda Biała-Leonhard, and Fabio Valentinuzzi
Subjects: chemistry.chemical_compound, Cell signaling, chemistry, Isoflavonoid, Biochemistry, biology, Symbiosis, Genistein, Rhizobium, Fabaceae, biology.organism_classification, Bacteria, Rhizobia
Abstract: SUMMARYNitrogen (N) as well as Phosphorus (P) are key nutrients determining crop productivity. Legumes have developed strategies to overcome nutrient limitation by e.g., forming a symbiotic relationship with N-fixing rhizobia and the release of P-mobilizing exudates and are thus able to grow without supply of N or P fertilizers. The legume-rhizobial symbiosis starts with root release of isoflavonoids, that act as signaling molecules perceived by compatible bacteria. Subsequently, bacteria release nod factors, which induce signaling cascades allowing the formation of functional N-fixing nodules.We report here the identification and functional characterization of a plasma membrane-localized MATE-type transporter (LaMATE2) involved in the release of genistein from white lupin roots.The LaMATE2 expression in the root is upregulated under N deficiency as well as low phosphate availability, two nutritional deficiencies that induce the release of this isoflavonoid. LaMATE2 silencing reduced genistein efflux and even more the formation of symbiotic nodules, supporting the crucial role of LaMATE2 in isoflavonoid release and nodulation. Furthermore, silencing of LaMATE2 limited the P-solubilization activity of lupin root exudates. Transport assays in yeast vesicles demonstrated that LaMATE2 acts as a proton-driven isoflavonoid transporter.
Published: 2021

18. Control of host mitochondria by bacterial pathogens

Author: Lorenzo Galluzzi, Paolo Pinton, Saverio Marchi, and Gianluca Morroni
Subjects: Microbiology (medical), Programmed cell death, biology, Bioenergetics, Autophagy, Pathogenic bacteria, Oxidative phosphorylation, Mitochondrion, biology.organism_classification, medicine.disease_cause, Microbiology, Listeria monocytogenes, Cell biology, Mitochondria, Infectious Diseases, Virology, medicine, Compartment (development), Homeostasis, Energy Metabolism, Bacteria
Abstract: Mitochondria control various processes that are integral to cellular and organismal homeostasis, including Ca2+ fluxes, bioenergetic metabolism, and cell death. Perhaps not surprisingly, multiple pathogenic bacteria have evolved strategies to subvert mitochondrial functions in support of their survival and dissemination. Here, we discuss nonimmunological pathogenic mechanisms that converge on the ability of bacteria to control the mitochondrial compartment of host cells.
Published: 2021

19. CDKN2A Determines Mesothelioma Cell Fate to EZH2 Inhibition

Author: Sara Missaglia, Renzo Boldorini, Dean A. Fennell, Cecilia Balzano, Laura Moro, Martin Griffin, Daniela Tavian, Giulia Pinton, and Zhuo Wang
Subjects: 0301 basic medicine, Cancer Research, ink4a, EZH2 inhibitor, 03 medical and health sciences, Histone H3, CDKN2A/p16ink4a, 0302 clinical medicine, TG2, medicine, malignant pleural mesothelioma, Mesothelioma, multicellular spheroids, Settore BIO/10 - BIOCHIMICA, RC254-282, CDKN2A/p16, Original Research, BAP1, biology, Cell growth, Chemistry, Sirtuin 1, EZH2, Neoplasms. Tumors. Oncology. Including cancer and carcinogens, medicine.disease, 030104 developmental biology, Oncology, Apoptosis, 030220 oncology & carcinogenesis, Histone methyltransferase, biology.protein, Cancer research
Abstract: Malignant pleural mesothelioma is an aggressive cancer, heterogeneous in its presentation and behaviour. Despite an increasing knowledge about molecular markers and their diagnostic and prognostic value, they are not used as much as they might be for treatment allocation. It has been recently reported that mesothelioma cells that lack BAP1 (BRCA1 Associated Protein) are sensitive to inhibition of the EZH2 (Enhancer of Zeste Homolog 2) histone methyltransferase. Since we observed strong H3K27me3 (histone H3 lysine 27 trimetylation) immunoreactivity in BAP1 wild-type mesothelioma biopsies, we decided to characterize in vitro the response/resistance of BAP1 wild-type mesothelioma cells to the EZH2 selective inhibitor, EPZ-6438. Here we demonstrate that BAP1 wild-type mesothelioma cells were rendered sensitive to EPZ-6438 upon SIRT1 (Sirtuin 1) silencing/inhibition or when cultured as multicellular spheroids, in which SIRT1 expression was lower compared to cells grown in monolayers. Notably, treatment of spheroids with EPZ-6438 abolished H3K27me3 and induced the expression of CDKN2A (Cyclin-Dependent Kinase Inhibitor 2A), causing cell growth arrest. EPZ-6438 treatment also resulted in a rapid and sustained induction of the genes encoding HIF2α (Hypoxia Inducible Factor 2α), TG2 (Transglutaminase 2) and IL-6 (Interleukin 6). Loss of CDKN2 is a common event in mesothelioma. CDKN2A silencing in combination with EPZ-6438 treatment induced apoptotic death in mesothelioma spheroids. In a CDKN2A wild-type setting apoptosis was induced by combining EPZ-6438 with 1-155, a TG2 selective and irreversible inhibitor. In conclusion, our data suggests that the expression of CDKN2A predicts cell fate in response to EZH2 inhibition and could potentially stratify tumors likely to undergo apoptosis.
Published: 2021

20. Statistical Integration of ‘Omics Data Increases Biological Knowledge Extracted from Metabolomics Data: Application to Intestinal Exposure to the Mycotoxin Deoxynivalenol

Author: Marie Tremblay-Franco, Claire Naylies, Imourana Alassane-Kpembi, Cécile Canlet, Philippe Pinton, Yannick Lippi, Isabelle P. Oswald, Roselyne Gautier, Manon Neves, Laurent Debrauwer, ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Metatoul AXIOM (E20 ), MetaboHUB-MetaToul, Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-ToxAlim (ToxAlim), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Biosynthèse & Toxicité des Mycotoxines (ToxAlim-BioToMyc), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), Université de Montréal (UdeM), This research was funded by the French National Infrastructure for metabolomics and fluxomics MetaboHUB ANR-11-INBS-010 and by the ExpoMycoPig project ANR-17-Carn012 and by an internal Toxalim grant., ANR-11-INBS-0010,METABOHUB,Développement d'une infrastructure française distribuée pour la métabolomique dédiée à l'innovation(2011), LESUR, Hélène, Développement d'une infrastructure française distribuée pour la métabolomique dédiée à l'innovation - - METABOHUB2011 - ANR-11-INBS-0010 - INBS - VALID, Analyse de Xénobiotiques, Identification, Métabolisme (E20 Metatoul-AXIOM), MetaToul-MetaboHUB, Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse)
Subjects: Endocrinology, Diabetes and Metabolism, [SDV]Life Sciences [q-bio], Computational biology, Biology, Biochemistry, Microbiology, Article, Omics data, Transcriptome, 03 medical and health sciences, chemistry.chemical_compound, transcriptomics, 0302 clinical medicine, Metabolomics, statistical integration, Gene expression, mycotoxin exposure 1, metabolomics 3, mycotoxin exposure, Mycotoxin, Molecular Biology, Organism, 030304 developmental biology, 0303 health sciences, Phenotype, metabolomics, QR1-502, Metabolomics data, [SDV] Life Sciences [q-bio], chemistry, 030220 oncology & carcinogenesis, statistical integration 4, transcriptomics 2
Abstract: International audience; The effects of low doses of toxicants are often subtle and information extracted from metabolomic data alone may not always be sufficient. As end products of enzymatic reactions, metabolites represent the final phenotypic expression of an organism and can also reflect gene expression changes caused by this exposure. Therefore, the integration of metabolomic and transcriptomic data could improve the extracted biological knowledge on these toxicants induced disruptions. In the present study, we applied statistical integration tools to metabolomic and transcriptomic data obtained from jejunal explants of pigs exposed to the food contaminant, deoxynivalenol (DON). Canonical correlation analysis (CCA) and self-organizing map (SOM) were compared for the identification of correlated transcriptomic and metabolomic features, and O2-PLS was used to model the relationship between exposure and selected features. The integration of both ‘omics data increased the number of discriminant metabolites discovered (39) by about 10 times compared to the analysis of the metabolomic dataset alone (3). Besides the disturbance of energy metabolism previously reported, assessing correlations between both functional levels revealed several other types of damage linked to the intestinal exposure to DON, including the alteration of protein synthesis, oxidative stress, and inflammasome activation. This confirms the added value of integration to enrich the biological knowledge extracted from metabolomics
Published: 2021
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21. An Updated Understanding of the Role of YAP in Driving Oncogenic Responses

Author: Paolo Pinton, Carlotta Giorgi, Sonia Missiroli, Bianca Vezzani, Giampaolo Morciano, and Caterina Boncompagni
Subjects: 0301 basic medicine, Cancer Research, Hippo pathway, Cell, WWTR1, Review, Biology, NO, 03 medical and health sciences, 0302 clinical medicine, Mediator, medicine, cancer, RC254-282, Hippo signaling pathway, Oncogene, Neoplasms. Tumors. Oncology. Including cancer and carcinogens, Cancer, medicine.disease, immunity, Immunity, Targeted therapies, YAP, targeted therapies, 3. Good health, Cell biology, Crosstalk (biology), 030104 developmental biology, medicine.anatomical_structure, Oncology, 030220 oncology & carcinogenesis, Cancer cell
Abstract: Simple Summary In 2020, the global cancer database GLOBOCAN estimated 19.3 million new cancer cases worldwide. The discovery of targeted therapies may help prognosis and outcome of the patients affected, but the understanding of the plethora of highly interconnected pathways that modulate cell transformation, proliferation, invasion, migration and survival remains an ambitious goal. Here we propose an updated state of the art of YAP as the key protein driving oncogenic response via promoting all those steps at multiple levels. Of interest, the role of YAP in immunosuppression is a field of evolving research and growing interest and this summary about the current pharmacological therapies impacting YAP serves as starting point for future studies. Abstract Yes-associated protein (YAP) has emerged as a key component in cancer signaling and is considered a potent oncogene. As such, nuclear YAP participates in complex and only partially understood molecular cascades that are responsible for the oncogenic response by regulating multiple processes, including cell transformation, tumor growth, migration, and metastasis, and by acting as an important mediator of immune and cancer cell interactions. YAP is finely regulated at multiple levels, and its localization in cells in terms of cytoplasm–nucleus shuttling (and vice versa) sheds light on interesting novel anticancer treatment opportunities and putative unconventional functions of the protein when retained in the cytosol. This review aims to summarize and present the state of the art knowledge about the role of YAP in cancer signaling, first focusing on how YAP differs from WW domain-containing transcription regulator 1 (WWTR1, also named as TAZ) and which upstream factors regulate it; then, this review focuses on the role of YAP in different cancer stages and in the crosstalk between immune and cancer cells as well as growing translational strategies derived from its inhibitory and synergistic effects with existing chemo-, immuno- and radiotherapies.
Published: 2021

22. Mitochondrial functionality and metabolism in T cells from progressive multiple sclerosis patients

Author: Marcello Pinti, Domenico Lo Tartaro, Patrizia Sola, Lara Gibellini, Anna Maria Simone, Diana Ferraro, Milena Nasi, Simone Patergnani, Elena Bianchini, Sara De Biasi, Simone Pecorini, Gianluca Carnevale, Paolo Pinton, Francesca Vitetta, and Andrea Cossarizza
Subjects: Adult, 0301 basic medicine, medicine.medical_specialty, Multiple Sclerosis, T-Lymphocytes, T cell, Immunology, T cells, Mitochondrion, Biology, NO, 03 medical and health sciences, Oxygen Consumption, 0302 clinical medicine, Downregulation and upregulation, Internal medicine, Respiration, medicine, Humans, Immunology and Allergy, Cytotoxic T cell, Glycolysis, Aged, flow cytometry, metabolism, mitochondria, multiple sclerosis, Glucose Transporter Type 1, Multiple sclerosis, Glucose transporter, Middle Aged, medicine.disease, Mitochondria, 030104 developmental biology, Endocrinology, medicine.anatomical_structure, Female, Immunologic Memory, 030215 immunology
Abstract: Patients with primary progressive (PP) and secondary progressive (SP) forms of multiple sclerosis (MS) exhibit a sustained increase in the number of Th1, T cytotoxic type-1 and Th17 cells in peripheral blood, suggesting that the progressive phase is characterized by a permanent peripheral immune activation. As T cell functionality and activation are strictly connected to their metabolic profile, we investigated the mitochondrial functionality and metabolic changes of T cell subpopulations in a cohort of progressive MS patients. T cells from progressive patients were characterized by low proliferation and increase of terminally differentiated/exhausted cells. T cells from PP patients showed lower Oxygen Consumption Rate and Extracellular Acidification Rate, lower mitochondrial mass, membrane potential and respiration than those of SP patients, a downregulation of transcription factors supporting respiration and higher tendency to shift towards glycolysis upon stimulation. Furthermore, PP effector memory T cells were characterized by higher Glucose transporter -1 levels and a higher expression of glycolytic-supporting genes if compared to SP patients. Overall, our data suggest that profound differences exist in the phenotypic and metabolic features of T cells from PP and SP patients, even though the two clinical phenotypes are considered part of the same disease spectrum.
Published: 2019

23. Reducing 50% sodium chloride in healthier jerked beef: An efficient design to ensure suitable stability, technological and sensory properties

Author: Erick A. Esmerino, João Paulo Biachi, Vitor Andre Silva Vidal, Marcelo Antonio Morgano, Mariana Basso Pinton, Marise Aparecida Rodrigues Pollonio, Camila de Souza Paglarini, Adriano G. Cruz, and Paulo Cezar Bastianello Campagnol
Subjects: Adult, Male, Food Handling, Sodium, chemistry.chemical_element, Sensory system, Potassium Chloride, Calcium Chloride, 0404 agricultural biotechnology, TBARS, Animals, Humans, Food science, Sodium Chloride, Dietary, Sodium reduction, Aroma, Control treatment, biology, Chemistry, 0402 animal and dairy science, Salting, food and beverages, 04 agricultural and veterinary sciences, Middle Aged, biology.organism_classification, 040401 food science, 040201 dairy & animal science, Meat Products, Ionic strength, Taste, Odorants, Food Microbiology, Cattle, Female, Food Science
Abstract: The objective of this study was to evaluate the effects of the partial replacement of NaCl by blends of KCl and CaCl2 on the physicochemical, microbiological, and sensory properties of jerked beef. For that, in the dry and wet salting stages, 50% NaCl of the control treatment (FC1) was replaced by 50% KCl (F1), 50% CaCl2 (F2), and a blend containing 25% KCl and 25% CaCl2 (F3) at equivalent concentrations based on the ionic strength. All reformulated treatments presented a significant sodium reduction when compared to the control (27.57% F1, 41.59% F2, and 36.74% F3). The CaCl2 blends resulted in final products with bitter taste and rancid aroma accompanied by a higher TBARS and shear force and lower a* values (P .05). The present results demonstrate that adding 50% KCl may be a good strategy to reduce sodium in jerked beef.
Published: 2019

24. Thimerosal inhibitsDrosophila melanogastertyrosine hydroxylase (DmTyrH) leading to changes in dopamine levels and impaired motor behavior: implications for neurotoxicity

Author: Mateus Cristofari Gayer, Daniel Henrique Roos, Pablo A. Nogara, Matheus Chimelo Bianchini, Bárbara Nunes Krum, Roselei Fachinetto, Frank Hirth, Daiana Silva Ávila, Claudia Ortiz Alves Gularte, João Rocha, Simone Pinton, Rafael Roehrs, Robson Luiz Puntel, and Jessika Cristina Bridi
Subjects: Male, 0301 basic medicine, Thioredoxin-Disulfide Reductase, Tyrosine 3-Monooxygenase, Dopamine, Biophysics, Biology, Pharmacology, medicine.disease_cause, Thiobarbituric Acid Reactive Substances, Biochemistry, Biomaterials, 03 medical and health sciences, chemistry.chemical_compound, Monoaminergic, medicine, Animals, MTT assay, Glutathione Transferase, 030102 biochemistry & molecular biology, Tyrosine hydroxylase, Thimerosal, Dopaminergic, Metals and Alloys, Neurotoxicity, medicine.disease, Acetylcholinesterase, Drosophila melanogaster, 030104 developmental biology, chemistry, Chemistry (miscellaneous), Female, Oxidative stress, medicine.drug
Abstract: Thimerosal (THIM) is a well-established antifungal and antiseptic agent widely used as a preservative in vaccines. Recent studies identified the neurotoxic effects of THIM, including malfunction of the monoaminergic system. However, the underlying cytotoxic mechanisms are not well understood. Here we used the fruit fly Drosophila melanogaster to investigate the mechanisms of THIM-induced neurotoxicity. We focused on the dopaminergic system, and the rate-limiting enzyme tyrosine hydroxylase (DmTyrH), to test the hypothesis that THIM can impair dopamine (DA) homeostasis and subsequently cause dysfunction. We studied the effect of THIM by feeding 1-2 day old flies (both sexes) food supplemented with 25 μM THIM for 4 days and determined THIM-induced effects on survival, oxidative stress, and metabolic activity based on MTT assay and acetylcholinesterase (AChE) activity. Our results demonstrate that D. melanogaster exposed to THIM present changes in DmTyrH expression and activity, together with altered DA levels that led to impaired motor behavior. These phenotypes were accompanied by an increase in oxidative stress, with a decrease in MTT reduction, in AChE activity, and also in survival rate. These findings suggest an initiating and primary role for THIM-mediated DmTyrH dysfunction that leads to impaired DA function and behavioral abnormalities, ultimately causing oxidative stress-related neurotoxicity.
Published: 2019

25. A naturally occurring mutation in ATP synthase subunit c is associated with increased damage following hypoxia/reoxygenation in STEMI patients

Author: Roberto Ferrari, Mariusz R. Wieckowski, Gaia Pedriali, Matteo Bovolenta, Magdalena Lebiedzinska-Arciszewska, Rita Pavasini, Massimo Bonora, Lorenzo Galluzzi, Alberto Albertini, Mirko Pinotti, Gianluca Campo, Giampaolo Morciano, Paolo Pinton, Elisa Mikus, Simone Calvi, and Carlotta Giorgi
Subjects: 0301 basic medicine, Male, Pore complex, Gene Expression, Pharmacology, Mitochondrion, 0302 clinical medicine, Myocytes, Cardiac, Prospective Studies, STEMI patients, Biology (General), Hypoxia, ATP synthase, biology, Chemistry, glycine-rich domain, Exons, Middle Aged, Mitochondrial Proton-Translocating ATPases, reperfusion injury, mitochondria, Female, subunit c, QH301-705.5, Protein subunit, PTP, Socio-culturale, ischemia, General Biochemistry, Genetics and Molecular Biology, cardiovascular diseases, 03 medical and health sciences, medicine, Animals, Humans, ATP5G1, Uniporter, Aged, Base Sequence, Mitochondrial Permeability Transition Pore, medicine.disease, Introns, ATP synthase subunit C, Oxygen, 030104 developmental biology, Mutation, biology.protein, ST Elevation Myocardial Infarction, Calcium Channels, Reperfusion injury, 030217 neurology & neurosurgery
Abstract: Summary: Preclinical models of ischemia/reperfusion injury (RI) demonstrate the deleterious effects of permeability transition pore complex (PTPC) opening in the first minutes upon revascularization of the occluded vessel. The ATP synthase c subunit (Csub) influences PTPC activity in cells, thus impacting tissue injury. A conserved glycine-rich domain in Csub is classified as critical because, when mutated, it modifies ATP synthase properties, protein interaction with the mitochondrial calcium (Ca2+) uniporter complex, and the conductance of the PTPC. Here, we document the role of a naturally occurring mutation in the Csub-encoding ATP5G1 gene at the G87 position found in two ST-segment elevation myocardial infarction (STEMI) patients and how PTPC opening is related to RI in patients affected by the same disease. We report a link between the expression of ATP5G1G87E and the response to hypoxia/reoxygenation of human cardiomyocytes, which worsen when compared to those expressing the wild-type protein, and a positive correlation between PTPC and RI.
Published: 2021

26. Mitochondrial Control of Genomic Instability in Cancer

Author: Sonia Missiroli, Francesco Fiorica, Massimo Bonora, Paolo Pinton, Mariasole Perrone, and Carlotta Giorgi
Subjects: 0301 basic medicine, Genome instability, Mi, p53, Cancer Research, DNA damage, tumor progression, Review, Biology, Mitochondrion, lcsh:RC254-282, NO, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Mitophagy, tochondria, calcium, apoptosis, ROS, lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens, Apoptosis, Calcium, Genomic instability, Mi, tochondria, Mitophagy, P53, ROS, Tumor progression, genomic instability, 3. Good health, Cell biology, mitochondria, 030104 developmental biology, mitophagy, Oncology, chemistry, Apoptosis, Tumor progression, 030220 oncology & carcinogenesis, Signal transduction, DNA
Abstract: Simple Summary Cancer cells display among its hallmark genomic instability. This is a progressive tendency in accumulate genome alteration which contributes to the damage of genes regulating cell division and tumor suppression. Genomic instability favors the appearance of survival-promoting mutations, increasing the likelihood that those mutations will propagate into daughter cells and have a significant impact on cancer progression. Among the many factor influencing this phenomenon, mitochondrial physiology is emerging. Mitochondria are bound to genomic instability by responding to DNA alteration to trigger cell death programs and as a source for DNA damage. Mitochondrial alterations prototypical of cancer can desensitize the mitochondrial route of cell death, facilitating the survival of cell acquiring new mutations, or can stimulate mitochondrial mediated DNA damage, boosting the mutation rate and genomic instability itself. Abstract Mitochondria are well known to participate in multiple aspects of tumor formation and progression. They indeed can alter the susceptibility of cells to engage regulated cell death, regulate pro-survival signal transduction pathways and confer metabolic plasticity that adapts to specific tumor cell demands. Interestingly, a relatively poorly explored aspect of mitochondria in neoplastic disease is their contribution to the characteristic genomic instability that underlies the evolution of the disease. In this review, we summarize the known mechanisms by which mitochondrial alterations in cancer tolerate and support the accumulation of DNA mutations which leads to genomic instability. We describe recent studies elucidating mitochondrial responses to DNA damage as well as the direct contribution of mitochondria to favor the accumulation of DNA alterations.
Published: 2021

27. Mitochondria: Insights into Crucial Features to Overcome Cancer Chemoresistance

Author: Ilaria Genovese, Lorenzo Modesti, Gianluca Aguiari, Paolo Pinton, Marianna Carinci, and Carlotta Giorgi
Subjects: Programmed cell death, QH301-705.5, Cell Survival, Antineoplastic Agents, Review, Mitochondrion, Biology, medicine.disease_cause, Mitochondrial Dynamics, Catalysis, NO, Inorganic Chemistry, Mitochondrial Proteins, mitochondrial dynamics, mitochondrial Ca2+ homeostasis, metabolic plasticity, drug resistance, cancer, Neoplasms, Mitophagy, medicine, Animals, Humans, cancer, Calcium Signaling, Physical and Theoretical Chemistry, Biology (General), Molecular Biology, QD1-999, Spectroscopy, drug resistance, Organic Chemistry, Cancer, General Medicine, medicine.disease, metabolic plasticity, Computer Science Applications, Cell biology, Mitochondria, mitochondrial Ca2+ homeostasis, Chemistry, Oxidative Stress, Apoptosis, Drug Resistance, Neoplasm, Cancer cell, Carcinogenesis, Oxidative stress
Abstract: Mitochondria are key regulators of cell survival and are involved in a plethora of mechanisms, such as metabolism, Ca2+ signaling, reactive oxygen species (ROS) production, mitophagy and mitochondrial transfer, fusion, and fission (known as mitochondrial dynamics). The tuning of these processes in pathophysiological conditions is fundamental to the balance between cell death and survival. Indeed, ROS overproduction and mitochondrial Ca2+ overload are linked to the induction of apoptosis, while the impairment of mitochondrial dynamics and metabolism can have a double-faceted role in the decision between cell survival and death. Tumorigenesis involves an intricate series of cellular impairments not yet completely clarified, and a further level of complexity is added by the onset of apoptosis resistance mechanisms in cancer cells. In the majority of cases, cancer relapse or lack of responsiveness is related to the emergence of chemoresistance, which may be due to the cooperation of several cellular protection mechanisms, often mitochondria-related. With this review, we aim to critically report the current evidence on the relationship between mitochondria and cancer chemoresistance with a particular focus on the involvement of mitochondrial dynamics, mitochondrial Ca2+ signaling, oxidative stress, and metabolism to possibly identify new approaches or targets for overcoming cancer resistance.
Published: 2021

28. Beyond residence time: quantifying factors that drive the spatially explicit filtration services of a 'pristine' oyster population

Author: Nicole Dix, Matthew Gray, David L. Kimbro, Pamela Marcum, Daniele Pinton, Alberto Canestrelli, and Raymond Grizzle
Subjects: Oyster, geography, education.field_of_study, geography.geographical_feature_category, Watershed, biology, Population, Estuary, Spatial distribution, biology.organism_classification, Ecosystem services, Oceanography, biology.animal, Environmental science, Crassostrea, education, Reef
Abstract: The Guana-Tolomato-Matanzas (GTM) system is a relatively pristine and well-flushed estuary in Northeastern Florida, USA and characterized as having an extraordinarily high abundance of oysters. Historically, dense populations of oysters, such as those found in GTM, are believed to play an important role in water filtration; however, few biofiltration studies have had access to such pristine populations. To quantify the filtration service (FS) of Eastern oysters (Crassostrea virginica) in GTM at several spatial scales (i.e. reef, watershed, estuary), we implemented a model that solves for the hydrodynamics and depletion of particulate matter passing over model oyster populations, the latter of which were derived from detailed bay-wide surveys. The model results suggested that oyster reefs populating the GTM play an important role in water quality by filtering ~60% of the estuary’s volume within its residence time. Our approach teases apart the role of reef size, residence time, particle concentration, and other physical factors on the generation of FS at different spatial scales. Downstream effects were found to be very important for estuary FS, which depend on the spatial distribution of the reefs in the GTM and local and estuarine-scale hydrodynamics. Therefore, the difference between “realized” FS and the “potential” FS of a given reef may be substantial when considering the complex hydrodynamic and connectivity among populations at several scales. Our model results provide clear and actionable information for management of these oyster populations and conservation of their ecosystem services.
Published: 2021

29. Disrupters of the Thymidylate Synthase Homodimer Accelerate Its Proteasomal Degradation and Inhibit Cancer Growth

Author: Matteo Santucci, Godefridus J. Peters, Outi M. H. Salo-Ahen, Domenico D'Arca, Matteo Trande, Angela L, Rosaria Luciani, Gabriele Cruciani, Rimessi A, Maria Paola Costi, Silvia Franchini, Cecilia Pozzi, Elisa Giovannetti, Antonio Quotadamo, Stefania Ferrari, Gaia G, Alberto Venturelli, Lorena Losi, Nuno Santarém, Daniela Cardinale, Gaetano Marverti, Emanuele C, Giuseppe Cannazza, Pacifico S, Silvia A, Pasquale Linciano, Stefan H, Anabela Cordeiro-da-Silva, Rebecca C. Wade, Robert M. Stroud, Remo Guerrini, Luca C, Pinton P, Stefano Mangani, Filippo Genovese, Puneet Saxena, and Glauco Ponterini
Subjects: biology, Chemistry, Cancer, Prodrug, medicine.disease, Thymidylate synthase, Small molecule, law.invention, Fluorouracil, law, Pancreatic cancer, Cancer cell, medicine, Cancer research, Recombinant DNA, biology.protein, medicine.drug
Abstract: Drugs that target human thymidylate synthase (hTS) are widely used in anti-cancer therapy. However, treatment with classical substrate-site-directed TS inhibitors induces its over-expression and the development of drug resistance. We thus pursued an alternative strategy that led to the discovery of TS-dimer disrupters that bind at the monomer-monomer interface and shift the dimerization equilibrium of both the recombinant and the intracellular protein toward the inactive monomers. We performed a structural, spectroscopic and kinetic investigation of the effects of these small molecules andthe best one, E7, accelerates the proteasomal degradation of hTS in cancer cells. E7 showed a superior anticancer profile to fluorouracil in a mouse model of human pancreatic and ovarian cancer. Thus, over sixty years after the discovery of the first TS prodrug inhibitor, fluorouracil, E7 breaks the link between TS inhibition and enhanced expression in response, providing a strategy to fight drug-resistant cancers.
Published: 2021

30. Relevance of Autophagy and Mitophagy Dynamics and Markers in Neurodegenerative Diseases

Author: Simone Patergnani, Alberto Danese, Carlotta Giorgi, Esmaa Bouhamida, Maurizio Previati, and Paolo Pinton
Subjects: autophagy, Parkinson's disease, Medicine (miscellaneous), Review, Disease, Biology, multiple sclerosis, General Biochemistry, Genetics and Molecular Biology, NO, 03 medical and health sciences, 0302 clinical medicine, Mitophagy, medicine, lcsh:QH301-705.5, 030304 developmental biology, therapy, 0303 health sciences, autophagy, mitophagy, neurodegeneration, multiple sclerosis, Alzheimer’s disease, Parkinson’s disease, biomarker, therapy, Neurodegeneration, Autophagy, neurodegeneration, medicine.disease, 3. Good health, mitophagy, lcsh:Biology (General), Potential biomarkers, Parkinson’s disease, biomarker, Neuroscience, Alzheimer’s disease, 030217 neurology & neurosurgery
Abstract: During the past few decades, considerable efforts have been made to discover and validate new molecular mechanisms and biomarkers of neurodegenerative diseases. Recent discoveries have demonstrated how autophagy and its specialized form mitophagy are extensively associated with the development, maintenance, and progression of several neurodegenerative diseases. These mechanisms play a pivotal role in the homeostasis of neural cells and are responsible for the clearance of intracellular aggregates and misfolded proteins and the turnover of organelles, in particular, mitochondria. In this review, we summarize recent advances describing the importance of autophagy and mitophagy in neurodegenerative diseases, with particular attention given to multiple sclerosis, Parkinson’s disease, and Alzheimer’s disease. We also review how elements involved in autophagy and mitophagy may represent potential biomarkers for these common neurodegenerative diseases. Finally, we examine the possibility that the modulation of autophagic and mitophagic mechanisms may be an innovative strategy for overcoming neurodegenerative conditions. A deeper knowledge of autophagic and mitophagic mechanisms could facilitate diagnosis and prognostication as well as accelerate the development of therapeutic strategies for neurodegenerative diseases.
Published: 2021

31. The enteric nerve system as target of regulated and emerging food-associated mycotoxins

Author: Marc Maresca, Amine Kadri, Łukasz Zielonka, Isabelle P. Oswald, Michał Dąbrowski, Hamza Olleik, Philippe Pinton, and Valérie Camps
Subjects: Necrosis, Membrane permeability, Biology, In vitro, Microbiology, chemistry.chemical_compound, chemistry, Apoptosis, Toxicity, medicine, Cytotoxic T cell, medicine.symptom, Mycotoxin, Organism
Abstract: Food and feed are frequently contaminated by numerous regulated and emerging mycotoxins. Humans and animals are thus exposed daily to mycotoxins through the oral route making of the gut the first and the more exposed tissue. Although many studies have evaluated and demonstrated the impact of mycotoxins on the intestinal epithelial cells (IECs) and on the brain cells, surprisingly only few studies have investigated their impact on cells of the enteric nerve system (ENS). In the present work, we measured the impact of major regulated and emerging mycotoxins (17 mycotoxins in total) on the proliferation and viability of ENS cells in vitro. On the 17 mycotoxins tested, 9 were found active with anti-proliferative and cytotoxic effects observed at doses ranging from 0.19 to 16.4 µM and 0.4 to 38.4 µM, respectively. Mechanistic approaches revealed that toxicity on ENS cells was related to i) alteration of the membrane permeability, ii) ROS production and/or iii) induction of apoptosis/necrosis. Importantly, toxic doses found on ENS cells were compared to toxic doses found on IECs in order to determine if toxicity toward ENS was selective or not. Finally, toxic doses on ENS cells were compared to PMTDI and range of exposure in humans and animals in order to evaluate if ENS’s cells are a realistic target of food-associated mycotoxins and if alterations of ENS participate in the global impact of these toxins on the gut and the full organism.
Published: 2021

32. Different Roles of Mitochondria in Cell Death and Inflammation: Focusing on Mitochondrial Quality Control in Ischemic Stroke and Reperfusion

Author: Bianca Vezzani, Marianna Carinci, Ilaria Casetta, Maura Pugliatti, Paolo Pinton, Katrin Lessmann, Peter Ludewig, Carlotta Giorgi, Simone Patergnani, and Tim Magnus
Subjects: Programmed cell death, Medicine (miscellaneous), Review, Mitochondrion, Biology, Neuroprotection, General Biochemistry, Genetics and Molecular Biology, NO, 03 medical and health sciences, 0302 clinical medicine, LS5_1, Mitophagy, medicine, ischemic stroke, lcsh:QH301-705.5, ischemic stroke, ischemic reperfusion, cell death, inflammation, mitophagy, mitochondrial fusion, mitochondrial fission, mitochondrial transfer, 030304 developmental biology, ischemic reperfusion, 0303 health sciences, mitochondrial fission, mitochondrial transfer, medicine.disease, Cell biology, cell death, mitophagy, mitochondrial fusion, lcsh:Biology (General), Mitochondrial permeability transition pore, inflammation, Mitochondrial fission, Reperfusion injury, 030217 neurology & neurosurgery
Abstract: Mitochondrial dysfunctions are among the main hallmarks of several brain diseases, including ischemic stroke. An insufficient supply of oxygen and glucose in brain cells, primarily neurons, triggers a cascade of events in which mitochondria are the leading characters. Mitochondrial calcium overload, reactive oxygen species (ROS) overproduction, mitochondrial permeability transition pore (mPTP) opening, and damage-associated molecular pattern (DAMP) release place mitochondria in the center of an intricate series of chance interactions. Depending on the degree to which mitochondria are affected, they promote different pathways, ranging from inflammatory response pathways to cell death pathways. In this review, we will explore the principal mitochondrial molecular mechanisms compromised during ischemic and reperfusion injury, and we will delineate potential neuroprotective strategies targeting mitochondrial dysfunction and mitochondrial homeostasis.
Published: 2021

33. Methods to Monitor Mitophagy and Mitochondrial Quality: Implications in Cancer, Neurodegeneration, and Cardiovascular Diseases

Author: Maurizio Previati, Saverio Marchi, Gaia Pedriali, Carlotta Giorgi, Giampaolo Morciano, Alessandro Rimessi, Alberto Danese, Massimo Bonora, Gabriele Anania, Esmaa Bouhamida, Simone Patergnani, and Paolo Pinton
Subjects: 0301 basic medicine, Cardiovascular diseases (CVD), Homeostasis, Metabolism, Mitochondrial morphology, Mitochondrial quality control, Pathology, Cell, Population, Cellular homeostasis, Mitochondrion, Biology, NO, 03 medical and health sciences, 0302 clinical medicine, Mitophagy, medicine, education, education.field_of_study, Autophagy, Neurodegeneration, medicine.disease, 030104 developmental biology, medicine.anatomical_structure, Neuroscience, 030217 neurology & neurosurgery, Function (biology)
Abstract: Mitochondria are dynamic organelles that participate in a broad array of molecular functions within the cell. They are responsible for maintaining the appropriate energetic levels and control the cellular homeostasis throughout the generation of intermediary metabolites. Preserving a healthy and functional mitochondrial population is of fundamental importance throughout the life of the cells under pathophysiological conditions. Hence, cells have evolved fine-tuned mechanisms of quality control that help to preserve the right amount of functional mitochondria to meet the demand of the cell. The specific recycling of mitochondria by autophagy, termed mitophagy, represents the primary contributor to mitochondrial quality control. During this process, damaged or unnecessary mitochondria are recognized and selectively degraded. In the past few years, the knowledge in mitophagy has seen rapid progress, and a growing body of evidence confirms that mitophagy holds a central role in controlling cellular functions and the progression of various human diseases.In this chapter, we will discuss the pathophysiological roles of mitophagy and provide a general overview of the current methods used to monitor and quantify mitophagy. We will also outline the main established approaches to investigate the mitochondrial function, metabolism, morphology, and protein damage.
Published: 2021

34. BAP1 forms a trimer with HMGB1 and HDAC1 that modulates gene × environment interaction with asbestos

Author: Yasutaka Takanishi, Giovanni Gaudino, Ellinor Haglund, Michael Minaai, Haithem Barbour, Mika Tanji, Fang Bai, Qian Wang, Simone Patergnani, Sandra Pastorino, Michele Carbone, Angela Bononi, Harvey I. Pass, Paul Morris, Carlotta Giorgi, Joelle S. Suarez, Franz Kricek, Haining Yang, Paolo Pinton, Ronghui Xu, José N. Onuchic, Greg Sakamoto, and Flavia Novelli
Subjects: germline BAP1 mutations, Male, Mesothelioma, gene × environment, Heterozygote, Carcinogenesis, chemical and pharmacologic phenomena, Histone Deacetylase 1, HMGB1, medicine.disease_cause, Asbestos, NO, Mice, medicine, Biomarkers, Tumor, mesothelioma, gene × environment, germline BAP1 mutations, asbestos, HMGB1, Carcinogenesis, Animals, HMGB1 Protein, Carcinogen, Germ-Line Mutation, Cell Nucleus, Inflammation, BAP1, Multidisciplinary, biology, Chemistry, Ubiquitin, Incidence, Tumor Suppressor Proteins, Biological Sciences, medicine.disease, Prognosis, HDAC1, Acetylation, Mutation, Cancer research, biology.protein, Female, Gene-Environment Interaction, Ubiquitin Thiolesterase, Protein Binding
Abstract: Significance Our findings explain mechanistically the observed gene × environment (G×E) interaction in mesotheliomas occurring in carriers of heterozygous germline BAP1 mutations ( BAP1 +/− ) exposed to asbestos. The increased amount of acetylated HMGB1 can be measured in the serum and may prove useful as a diagnostic/prognostic biomarker of mesothelioma in BAP1 +/− individuals. Inhibition of HMGB1 secretion in Bap1 +/− mutant mice exposed to asbestos significantly decreased the incidence of mesothelioma and prolonged the survival of those who developed mesothelioma. This strategy may be translated to carriers of germline BAP1 mutations with the aim of decreasing their incidence of mesothelioma.
Published: 2021
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35. Calcium flux control by Pacs1-Wdr37 promotes lymphocyte quiescence and lymphoproliferative diseases

Author: Massimo Bonora, Jamie Russell, Bruce Beutler, Nathan Stewart, Paolo Pinton, Amber Miranda, Thomas Gallagher, Xue Zhong, Evan Nair-Gill, Aijie Liu, and Sara Ludwig
Subjects: Male, Lymphocyte, Vesicular Transport Proteins, Wdr37, Biology, medicine.disease_cause, Endoplasmic Reticulum, General Biochemistry, Genetics and Molecular Biology, NO, 03 medical and health sciences, Mice, 0302 clinical medicine, Immune system, Lymphopenia, Calcium flux, medicine, Animals, Humans, calcium homeostasis, lymphocyte quiescence, lymphoproliferative disease, Pacs1, Wdr37, Calcium Signaling, Molecular Biology, lymphoproliferative disease, 030304 developmental biology, Calcium metabolism, 0303 health sciences, B-Lymphocytes, General Immunology and Microbiology, calcium homeostasis, Pacs1, General Neuroscience, Endoplasmic reticulum, Nuclear Proteins, Articles, Inositol trisphosphate receptor, Lymphoproliferative Disorders, Cell biology, Disease Models, Animal, medicine.anatomical_structure, Proteostasis, HEK293 Cells, NIH 3T3 Cells, Female, lymphocyte quiescence, 030217 neurology & neurosurgery, Oxidative stress, Gene Deletion
Abstract: Endoplasmic reticulum (ER) calcium (Ca(2+)) stores are critical to proteostasis, intracellular signaling, and cellular bioenergetics. Through forward genetic screening in mice, we identified two members of a new complex, Pacs1 and Wdr37, which are required for normal ER Ca(2+) handling in lymphocytes. Deletion of Pacs1 or Wdr37 caused peripheral lymphopenia that was linked to blunted Ca(2+) release from the ER after antigen receptor stimulation. Pacs1‐deficient cells showed diminished inositol triphosphate receptor expression together with increased ER and oxidative stress. Mature Pacs1 (−/−) B cells proliferated and died in vivo under lymphocyte replete conditions, indicating spontaneous loss of cellular quiescence. Disruption of Pacs1‐Wdr37 did not diminish adaptive immune responses, but potently suppressed lymphoproliferative disease models by forcing loss of quiescence. Thus, Pacs1‐Wdr37 plays a critical role in stabilizing lymphocyte populations through ER Ca(2+) handling and presents a new target for lymphoproliferative disease therapy.
Published: 2021

36. Mitochondrial Function and Dysfunction in Dilated Cardiomyopathy

Author: Daniela Ramaccini, Vanessa Montoya-Uribe, Femke J. Aan, Lorenzo Modesti, Yaiza Potes, Mariusz R. Wieckowski, Irena Krga, Marija Glibetić, Paolo Pinton, Carlotta Giorgi, and Michelle L. Matter
Subjects: 0301 basic medicine, cardiomyopathies, cardiomyocytes, Review, 030204 cardiovascular system & hematology, Mitochondrion, Biology, medicine.disease_cause, Ca ATPase (SERCA) 2+, NO, 03 medical and health sciences, Cell and Developmental Biology, 0302 clinical medicine, heart function, Mitophagy, Organelle, medicine, lcsh:QH301-705.5, calcium, Endoplasmic reticulum, organoids model, Dilated cardiomyopathy, Cell Biology, medicine.disease, Cell biology, mitochondria, cardiomyocytes, cardiomyopathies, organoids model, sarcoplasmic reticulum, Ca ATPase (SERCA) 2+, calcium, heart function, sarcoplasmic reticulum, mitochondria, 030104 developmental biology, lcsh:Biology (General), Apoptosis, Function (biology), Oxidative stress, Developmental Biology
Abstract: Cardiac tissue requires a persistent production of energy in order to exert its pumping function. Therefore, the maintenance of this function relies on mitochondria that represent the “powerhouse” of all cardiac activities. Mitochondria being one of the key players for the proper functioning of the mammalian heart suggests continual regulation and organization. Mitochondria adapt to cellular energy demands via fusion-fission events and, as a proof-reading ability, undergo mitophagy in cases of abnormalities. Ca2+ fluxes play a pivotal role in regulating all mitochondrial functions, including ATP production, metabolism, oxidative stress balance and apoptosis. Communication between mitochondria and others organelles, especially the sarcoplasmic reticulum is required for optimal function. Consequently, abnormal mitochondrial activity results in decreased energy production leading to pathological conditions. In this review, we will describe how mitochondrial function or dysfunction impacts cardiac activities and the development of dilated cardiomyopathy.
Published: 2021

37. Inhibition of the Histone Methyltransferase EZH2 Enhances Protumor Monocyte Recruitment in Human Mesothelioma Spheroids

Author: Laura Moro, Silvia Mola, Ambra A. Grolla, Marco Corazzari, Giulia Pinton, Veronica Martini, Marco De Andrea, Chiara Porta, and Marco Erreni
Subjects: Mesothelioma, Pyridones, QH301-705.5, Morpholines, Cell, Malignant pleural mesothelioma, epigenetic reprogramming, spheroids, Biology, Catalysis, Article, Inorganic Chemistry, Immune system, stomatognathic system, Spheroids, Cellular, EPZ-6438, medicine, Tumor Cells, Cultured, Humans, tumor microenvironment, Enhancer of Zeste Homolog 2 Protein, tumor-associated macrophages, monocytes, EZH2, tazemetostat, Physical and Theoretical Chemistry, Biology (General), skin and connective tissue diseases, Molecular Biology, QD1-999, Spectroscopy, Cell Proliferation, Tumor microenvironment, Monocyte, Organic Chemistry, Biphenyl Compounds, General Medicine, Phenotype, Computer Science Applications, Chemistry, medicine.anatomical_structure, Histone methyltransferase, Benzamides, Cancer research, Reprogramming, hormones, hormone substitutes, and hormone antagonists
Abstract: Malignant pleural mesothelioma (MPM) is a highly aggressive cancer with a long latency period and dismal prognosis. Recently, tazemetostat (EPZ-6438), an inhibitor of the histone methyltransferase EZH2, has entered clinical trials due to the antiproliferative effects reported on MPM cells. However, the direct and indirect effects of epigenetic reprogramming on the tumor microenvironment are hitherto unexplored. To investigate the impact of tumor-associated macrophages (TAMs) on MPM cell responsiveness to tazemetostat, we developed a three-dimensional MPM spheroid model that recapitulates in vitro, both monocytes’ recruitment in tumors and their functional differentiation toward a TAM-like phenotype (Mo-TAMs). Along with an increased expression of genes for monocyte chemoattractants, inhibitory immune checkpoints, immunosuppressive and M2-like molecules, Mo-TAMs promote tumor cell proliferation and spreading. Prolonged treatment of MPM spheroids with tazemetostat enhances both the recruitment of Mo-TAMs and the expression of their protumor phenotype. Therefore, Mo-TAMs profoundly suppress the antiproliferative effects due to EZH2 inhibition in MPM cells. Overall, our findings indicate that TAMs are a driving force for MPM growth, progression, and resistance to tazemetostat, therefore, strategies of TAM depletion might be evaluated to improve the therapeutic efficacy of pharmacological inhibition of EZH2.
Published: 2021

38. Update on Calcium Signaling in Cystic Fibrosis Lung Disease

Author: Alessandro Rimessi, Veronica A. M. Vitto, Simone Patergnani, and Paolo Pinton
Subjects: 0301 basic medicine, lung disease, Mini Review, Socio-culturale, Inflammation, calcium signaling, Cystic fibrosis, Proinflammatory cytokine, cystic fibrosis, 03 medical and health sciences, 0302 clinical medicine, Immune system, medicine, Pharmacology (medical), Calcium signaling, Pharmacology, Lung, calcium, biology, business.industry, lcsh:RM1-950, inflammation, inflammatory disease, respiratory system, medicine.disease, Cystic fibrosis transmembrane conductance regulator, respiratory tract diseases, 030104 developmental biology, medicine.anatomical_structure, lcsh:Therapeutics. Pharmacology, Cancer research, biology.protein, medicine.symptom, business, 030217 neurology & neurosurgery, Homeostasis
Abstract: Cystic fibrosis (CF) is an autosomal recessive disorder characterized by mutations in the cystic fibrosis transmembrane conductance regulator gene, which causes multifunctional defects that preferentially affect the airways. Abnormal viscosity of mucus secretions, persistent pathogen infections, hyperinflammation, and lung tissue damage compose the classical pathological manifestation referred to as CF lung disease. Among the multifunctional defects associated with defective CFTR, increasing evidence supports the relevant role of perturbed calcium (Ca2+) signaling in the pathophysiology of CF lung disease. The Ca2+ ion is a critical player in cell functioning and survival. Its intracellular homeostasis is maintained by a fine balance between channels, transporters, and exchangers, mediating the influx and efflux of the ion across the plasma membrane and the intracellular organelles. An abnormal Ca2+ profile has been observed in CF cells, including airway epithelial and immune cells, with heavy repercussions on cell function, viability, and susceptibility to pathogens, contributing to proinflammatory overstimulation, organelle dysfunction, oxidative stress, and excessive cytokines release in CF lung. This review discusses the role of Ca2+ signaling in CF and how its dysregulation in airway epithelial and immune cells contributes to hyperinflammation in the CF lung. Finally, we provide an outlook on the therapeutic options that target the Ca2+ signaling to treat the CF lung disease.
Published: 2021

39. Cell death as a result of calcium signaling modulation: A cancer-centric prospective

Author: Paolo Pinton, Carlotta Giorgi, Francesco Fiorica, Alessandro Rimessi, Sara Leo, Alberto Danese, and Mariusz R. Wieckowski
Subjects: 0301 basic medicine, Programmed cell death, Cell, Socio-culturale, Biology, Mitochondrion, 03 medical and health sciences, 0302 clinical medicine, Neoplasms, medicine, Animals, Humans, Calcium Signaling, Molecular Biology, Calcium signaling, Cell Death, Cell growth, Cancer, Cell Biology, medicine.disease, 030104 developmental biology, medicine.anatomical_structure, 030220 oncology & carcinogenesis, Second messenger system, Calcium, Neuroscience, Homeostasis
Abstract: Calcium ions (Ca2+) and the complex regulatory system governed by Ca2+ signaling have been described to be of crucial importance in numerous aspects related to cell life and death decisions, especially in recent years. The growing attention given to this second messenger is justified by the pleiotropic nature of Ca2+-binding proteins and transporters and their consequent involvement in cell fate decisions. A growing number of works highlight that deregulation of Ca2+ signaling and homoeostasis is often deleterious and drives pathological conditions; in particular, a disruption of the main Ca2+-mediated death mechanisms may lead to uncontrolled cell growth that results in cancer. In this work, we review the latest useful evidence to better understand the complex network of pathways by which Ca2+ regulates cell life and death decisions.
Published: 2021

40. Mitochondrial calcium homeostasis in hematopoietic stem cell: Molecular regulation of quiescence, function, and differentiation

Author: Massimo Bonora, Paolo Pinton, and Asrat Endrias Kahsay
Subjects: Cellular differentiation, Hematopoietic stem cell, Cell fate determination, Mitochondrion, Biology, Cell biology, NO, Mitochondria, Transcriptome, Haematopoiesis, medicine.anatomical_structure, AML, Ca2 +, MDS, Preleukemia, Self-renewal, medicine, Epigenetics, Stem cell
Abstract: Hematopoiesis is based on the existence of hematopoietic stem cells (HSC) with the capacity to self-proliferate and self-renew or to differentiate into specialized cells. The hematopoietic niche is the essential microenvironment where stem cells reside and integrate various stimuli to determine their fate. Recent studies have identified niche containing high level of calcium (Ca2+) suggesting that HSCs are sensitive to Ca2+. This is a highly versatile and ubiquitous second messenger that regulates a wide variety of cellular functions. Advanced methods for measuring its concentrations, genetic experiments, cell fate tracing data, single-cell imaging, and transcriptomics studies provide information into its specific roles to integrate signaling into an array of mechanisms that determine HSC identity, lineage potential, maintenance, and self-renewal. Accumulating and contrasting evidence, are revealing Ca2+ as a previously unacknowledged feature of HSC, involved in functional maintenance, by regulating multiple actors including transcription and epigenetic factors, Ca2+-dependent kinases and mitochondrial physiology. Mitochondria are significant participants in HSC functions and their responsiveness to cellular demands is controlled to a significant extent via Ca2+ signals. Recent reports indicate that mitochondrial Ca2+ uptake also controls HSC fate. These observations reveal a physiological feature of hematopoietic stem cells that can be harnessed to improve HSC-related disease. In this review, we discuss the current knowledge Ca2+ in hematopoietic stem cell focusing on its potential involvement in proliferation, self-renewal and maintenance of HSC and discuss future research directions.
Published: 2021

41. Dietary exposure to the food contaminant deoxynivalenol triggers colonic breakdown by activating the mitochondrial and the death receptor pathways

Author: Delphine Payros, Philippe Pinton, Joëlle Laffitte, Corine Lencina, Isabelle P. Oswald, Ana Paula Frederico Rodrigues Loureiro Bracarense, Imourana Alassane-Kpembi, Sandrine Ménard, Manon Neves, ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut de Recherche en Santé Digestive (IRSD ), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Montréal (UdeM), Biosynthèse & Toxicité des Mycotoxines (ToxAlim-BioToMyc), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), State University of Londrina = Universidade Estadual de Londrina, and Neuro-Gastroentérologie & Nutrition (ToxAlim-NGN)
Subjects: medicine.medical_specialty, Colon, [SDV]Life Sciences [q-bio], Inflammation, Food Contamination, Dietary Exposure, 03 medical and health sciences, 0302 clinical medicine, Downregulation and upregulation, Internal medicine, Medicine, Animals, Intestinal Mucosa, Rats, Wistar, Receptor, 030304 developmental biology, 0303 health sciences, biology, Tight junction, business.industry, Cytochrome c, Receptors, Death Domain, digestive system diseases, 3. Good health, Rats, Endocrinology, Apoptosis, Myeloperoxidase, biology.protein, 030211 gastroenterology & hepatology, Tumor necrosis factor alpha, medicine.symptom, business, Trichothecenes, Food Science, Biotechnology
Abstract: Scope The food contamination by mycotoxins is of increasing public health concerns. Deoxynivalenol (DON), a mycotoxin contaminating cereals has been associated with the exacerbation of inflammatory bowel diseases (IBD), thereby raising the question of its role in the development of IBD. Moreover, the effect of DON on the colon is poorly described. Methods and results Wistar rats exposed (1-4 weeks) to low doses of DON (2 or 9 mg.kg-1 feed) showed microscopic alterations of colonic tissue (dilated lymphatic vessels, luminal debris, and cubic and flattened enterocytes). Ingestion of DON also altered colonic functions by increasing paracellular permeability while reducing the expression of the tight junction proteins and increased apoptosis in colonic tissue. Pro-apoptotic factors Bax/Bak, cytochrome C and caspase 9 were upregulated whereas expression of anti-apoptotic protein Bcl2 tended to decrease for the mitochondrial pathway. An increased expression of FasR and caspase-8 was observed for the extrinsic pathway. An increase in the pro-inflammatory markers TNFα, IL-17 and myeloperoxidase was also observed. Conclusion These results indicate that the dietary exposure to low levels of DON in food targets the colon inducing a health-threatening breakdown of the colonic barrier, highlighting oral exposure to DON as a potential risk factor in triggering IBD. This article is protected by copyright. All rights reserved.
Published: 2021

42. Mitochondrial Ca 2+ Signaling in Health, Disease and Therapy

Author: Gianluca Aguiari, Paolo Pinton, Carlotta Giorgi, Roberta Gafà, Alberto Danese, Giovanni Lanza, Lorenzo Modesti, Daniela Ramaccini, and Veronica Angela Maria Vitto
Subjects: Programmed cell death, QH301-705.5, Context (language use), Disease, Biology, Mitochondrion, mPTP, NO, chemistry.chemical_compound, TheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITY, Ca2+, cancer, neurodegenerative diseases, Biology (General), therapy, MPTP, Transporter, mitochondria, Ca2+, cancer, cardiovascular diseases, neurodegenerative diseases, mPTP, therapy, General Medicine, Cell biology, cardiovascular diseases, mitochondria, chemistry, Second messenger system, Homeostasis
Abstract: The divalent cation calcium (Ca2+) is considered one of the main second messengers inside cells and acts as the most prominent signal in a plethora of biological processes. Its homeostasis is guaranteed by an intricate and complex system of channels, pumps, and exchangers. In this context, by regulating cellular Ca2+ levels, mitochondria control both the uptake and release of Ca2+. Therefore, at the mitochondrial level, Ca2+ plays a dual role, participating in both vital physiological processes (ATP production and regulation of mitochondrial metabolism) and pathophysiological processes (cell death, cancer progression and metastasis). Hence, it is not surprising that alterations in mitochondrial Ca2+ (mCa2+) pathways or mutations in Ca2+ transporters affect the activities and functions of the entire cell. Indeed, it is widely recognized that dysregulation of mCa2+ signaling leads to various pathological scenarios, including cancer, neurological defects and cardiovascular diseases (CVDs). This review summarizes the current knowledge on the regulation of mCa2+ homeostasis, the related mechanisms and the significance of this regulation in physiology and human diseases. We also highlight strategies aimed at remedying mCa2+ dysregulation as promising therapeutical approaches.
Published: 2021
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43. Hmx1 regulates urfh1 expression in the craniofacial region in zebrafish

Author: Nathalie Allaman-Pillet, Younes El Fersioui, Gaëtan Pinton, and Daniel F. Schorderet
Subjects: Embryology, Embryo, Nonmammalian, family, neurons, dna methylation, Biochemistry, Animals, Genetically Modified, Medicine and Health Sciences, Promoter Regions, Genetic, genes, Zebrafish, In Situ Hybridization, Regulation of gene expression, Eye Lens, Multidisciplinary, Eukaryota, Gene Expression Regulation, Developmental, Animal Models, eye, Chromatin, Cell biology, Nucleic acids, Experimental Organism Systems, Osteichthyes, Vertebrates, DNA methylation, Medicine, Epigenetics, Anatomy, DNA modification, Dimerization, Chromatin modification, Research Article, Chromosome biology, Ocular Anatomy, growth, Science, Molecular Probe Techniques, In situ hybridization, system, Biology, Research and Analysis Methods, Retina, Model Organisms, Protein Domains, Ocular System, Genetics, Animals, Homeobox, Luciferase, Amino Acid Sequence, Craniofacial, Molecular Biology Techniques, Molecular Biology, Homeodomain Proteins, Embryos, Organisms, Biology and Life Sciences, Proteins, DNA, Zebrafish Proteins, biology.organism_classification, Probe Hybridization, Fish, Mutagenesis, Animal Studies, Trans-Activators, Eyes, Gene expression, Zoology, Head, Developmental Biology
Abstract: H6 family homeobox 1 (HMX1) regulates multiple aspects of craniofacial development as it is widely expressed in the eye, peripheral ganglia and branchial arches. Mutations in HMX1 are linked to an ocular defect termed Oculo-auricular syndrome of Schorderet-Munier-Franceschetti (MIM #612109). We identified UHRF1 as a target of HMX1 during development. UHRF1 and its partner proteins actively regulate chromatin modifications and cellular proliferation. Luciferase assays and in situ hybridization analyses showed that HMX1 exerts a transcriptional inhibitory effect on UHRF1 and a modification of its expression pattern. Overexpression of hmx1 in hsp70-hmx1 zebrafish increased uhrf1 expression in the cranial region, while mutations in the hmx1 dimerization domains reduced uhrf1 expression. Moreover, the expression level of uhrf1 and its partner dnmt1 was increased in the eye field in response to hmx1 overexpression. These results indicate that hmx1 regulates uhrf1 expression and, potentially through regulating the expression of factors involved in DNA methylation, contribute to the development of the craniofacial region of zebrafish.
Published: 2021

44. Impaired mitochondrial quality control in Rett Syndrome

Author: Valeria Cordone, Saverio Marchi, Carlo Cervellati, Joussef Hayek, Ilaria Crivellari, Giuseppe Valacchi, Paolo Pinton, and Alessandra Pecorelli
Subjects: 0301 basic medicine, FIS1, Adult, Dynamins, congenital, hereditary, and neonatal diseases and abnormalities, RTT Syndrome, Mitochondrial quality control, Adolescent, Methyl-CpG-Binding Protein 2, Biophysics, PINK1, Apoptosis, Mitochondrion, Biology, Biochemistry, Mitochondrial Membrane Transport Proteins, NO, GTP Phosphohydrolases, Mitochondrial Proteins, 03 medical and health sciences, DNM1L, Mitophagy, Rett Syndrome, MFN1, Humans, Child, Molecular Biology, Caspase 7, 030102 biochemistry & molecular biology, Caspase 3, Membrane Proteins, Fibroblasts, Cell biology, Mitochondria, 030104 developmental biology, mitochondrial fusion, Oxidative stress, Mitochondrial fission, Female, Oxidation-Reduction
Abstract: Rett Syndrome (RTT) is a rare neurodevelopmental disorder caused in the 95% of cases by mutations in the X-linked MECP2 gene, affecting almost exclusively females. While the genetic basis of RTT is known, the exact pathogenic mechanisms that lead to the broad spectrum of symptoms still remain enigmatic. Alterations in the redox homeostasis have been proposed among the contributing factors to the development and progression of the syndrome. Mitochondria appears to play a central role in RTT oxidative damage and a plethora of mitochondrial defects has already been recognized. However, mitochondrial dynamics and mitophagy, which represent critical pathways in regulating mitochondrial quality control (QC), have not yet been investigated in RTT. The present work showed that RTT fibroblasts have networks of hyperfused mitochondria with morphological abnormalities and increased mitochondrial volume. Moreover, analysis of mitophagic flux revealed an impaired PINK1/Parkin-mediated mitochondrial removal associated with an increase of mitochondrial fusion proteins Mitofusins 1 and 2 (MFN1 and 2) and a decrease of fission mediators including Dynamin related protein 1 (DRP1) and Mitochondrial fission 1 protein (FIS1). Finally, challenging RTT fibroblasts with FCCP and 2,4-DNP did not trigger a proper apoptotic cell death due to a defective caspase 3/7 activation. Altogether, our findings shed light on new aspects of mitochondrial dysfunction in RTT that are represented by defective mitochondrial QC pathways, also providing new potential targets for a therapeutic intervention aimed at slowing down clinical course and manifestations in the affected patients.
Published: 2020

45. Deficiency of Mitochondrial Aspartate-Glutamate Carrier 1 Leads to Oligodendrocyte Precursor Cell Proliferation Defects Both In Vitro and In Vivo

Author: Ferdinando Palmieri, Francesca Massenzio, Marco Virgili, Miriam Capri, Alberto Danese, Carlotta Giorgi, Sabrina Petralla, Luis Emiliano Peña-Altamira, Barbara Monti, Paolo Pinton, Emanuela Profilo, Luigi Sbano, Simona N. Barile, Francesco M. Lasorsa, Mariangela Corricelli, Eleonora Poeta, Rita Ostan, Petralla S., Pena-Altamira L.E., Poeta E., Massenzio F., Virgili M., Barile S.N., Sbano L., Profilo E., Corricelli M., Danese A., Giorgi C., Ostan R., Capri M., Pinton P., Palmieri F., Lasorsa F.M., and Monti B.
Subjects: Platelet-derived growth factor, Amino Acid Transport Systems, endocrine system diseases, medicine.medical_treatment, Cellular differentiation, Antiporters, lcsh:Chemistry, chemistry.chemical_compound, Mice, Adenosine Triphosphate, Transforming Growth Factor beta, Lateral Ventricles, Receptors, Glutamate aspartate transporter, lcsh:QH301-705.5, Spectroscopy, Membrane Potential, Mitochondrial, Neurons, Platelet-Derived Growth Factor, biology, subventricular zone, growth factor, Cell Differentiation, General Medicine, Mitochondrial, Computer Science Applications, Cell biology, Mitochondria, mitochondrial disease, medicine.anatomical_structure, Lactates, hormones, hormone substitutes, and hormone antagonists, Signal Transduction, AGC1 deficiency, Growth factors, Mitochondrial disease, Mouse model, Subventricular zone, Amino Acid Transport Systems, Acidic, Animals, Cell Line, Cell Proliferation, Down-Regulation, Gene Silencing, Oligodendrocyte Precursor Cells, Reactive Oxygen Species, Receptors, Transforming Growth Factor beta, mouse model, Membrane Potential, Catalysis, Article, NO, Inorganic Chemistry, Precursor cell, Neurosphere, growth factors, medicine, Physical and Theoretical Chemistry, Molecular Biology, Growth factor, Acidic, Organic Chemistry, nutritional and metabolic diseases, Transforming growth factor beta, lcsh:Biology (General), lcsh:QD1-999, chemistry, nervous system, biology.protein
Abstract: Aspartate-Glutamate Carrier 1 (AGC1) deficiency is a rare neurological disease caused by mutations in the solute carrier family 25, member 12 (SLC25A12) gene, encoding for the mitochondrial aspartate-glutamate carrier isoform 1 (AGC1), a component of the malate&ndash, aspartate NADH shuttle (MAS), expressed in excitable tissues only. AGC1 deficiency patients are children showing severe hypotonia, arrested psychomotor development, seizures and global hypomyelination. While the effect of AGC1 deficiency in neurons and neuronal function has been deeply studied, little is known about oligodendrocytes and their precursors, the brain cells involved in myelination. Here we studied the effect of AGC1 down-regulation on oligodendrocyte precursor cells (OPCs), using both in vitro and in vivo mouse disease models. In the cell model, we showed that a reduced expression of AGC1 induces a deficit of OPC proliferation leading to their spontaneous and precocious differentiation into oligodendrocytes. Interestingly, this effect seems to be related to a dysregulation in the expression of trophic factors and receptors involved in OPC proliferation/differentiation, such as Platelet-Derived Growth Factor &alpha, (PDGF&alpha, ) and Transforming Growth Factor &beta, s (TGF&beta, s). We also confirmed the OPC reduction in vivo in AGC1-deficent mice, as well as a proliferation deficit in neurospheres from the Subventricular Zone (SVZ) of these animals, thus indicating that AGC1 reduction could affect the proliferation of different brain precursor cells. These data clearly show that AGC1 impairment alters myelination not only by acting on N-acetyl-aspartate production in neurons but also on OPC proliferation and suggest new potential therapeutic targets for the treatment of AGC1 deficiency.
Published: 2019
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46. Co-occurrence of DON and emerging mycotoxins in worldwide finished pig feed and their combined toxicity in intestinal cells

Author: Barbara Novak, Abdullah Khan Khoshal, Isabelle P. Oswald, Gerd Schatzmayr, Timothy P. Jenkins, Manon Neves, Philippe Pinton, Pascal G.P. Martin, ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA), BIOMIN Research Center, Biosynthèse & Toxicité des Mycotoxines (ToxAlim-BioToMyc), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), and Pinton, Philippe
Subjects: Fusarium, IPEC-1, Cell Survival, Swine, Health, Toxicology and Mutagenesis, emerging mycotoxins, global survey, Food Contamination, Toxicology, 01 natural sciences, DON, co-occurrence, combined toxicitty, finished pig feed, toxicity, Article, Cell Line, 03 medical and health sciences, chemistry.chemical_compound, Animals, Food science, Mycotoxin, Toxicologie, 030304 developmental biology, 0303 health sciences, biology, 010401 analytical chemistry, Brevianamide F, food and beverages, Epithelial Cells, Mycotoxins, biology.organism_classification, Animal Feed, Beauvericin, 0104 chemical sciences, 3. Good health, Intestines, chemistry, [SDV.TOX]Life Sciences [q-bio]/Toxicology, Penicillium, Toxicity, Emodin, combined toxicity, Enniatin
Abstract: Food and feed can be naturally contaminated by several mycotoxins, and concern about the hazard of exposure to mycotoxin mixtures is increasing. In this study, more than 800 metabolites were analyzed in 524 finished pig feed samples collected worldwide. Eighty-eight percent of the samples were co-contaminated with deoxynivalenol (DON) and other regulated/emerging mycotoxins. The Top 60 emerging/regulated mycotoxins co-occurring with DON in pig feed shows that 48%, 13%, 8% and 12% are produced by Fusarium, Aspergillus, Penicillium and Alternaria species, respectively. Then, the individual and combined toxicity of DON and the 10 most prevalent emerging mycotoxins (brevianamide F, cyclo-(L-Pro-L-Tyr), tryptophol, enniatins A1, B, B1, emodin, aurofusarin, beauvericin and apicidin) was measured at three ratios corresponding to pig feed contamination. Toxicity was assessed by measuring the viability of intestinal porcine epithelial cells, IPEC-1, at 48-h. BRV-F, Cyclo and TRPT did not alter cell viability. The other metabolites were ranked in the following order of toxicity: apicidin &gt, enniatin A1 &gt, DON &gt, beauvericin &gt, enniatin B &gt, enniatin B1 &gt, emodin &gt, aurofusarin. In most of the mixtures, combined toxicity was similar to the toxicity of DON alone. In terms of pig health, these results demonstrate that the co-occurrence of emerging mycotoxins that we tested with DON does not exacerbate toxicity.
Published: 2019

47. Analysis of Polycerate Mutants Reveals the Evolutionary Co-option of HOXD1 to Determine the Number and Topology of Horns in Bovidae

Author: Louisa Gidney, Nathalie Hirter, Aurélie Allais-Bonnet, Tracy Hadfield, Coralie M. Reich, Olivier Putelat, Ashleigh Haruda, Marina Naval-Sanchez, Rachel Rupp, Ben J. Hayes, Noelle E. Cockett, Renate Schafberg, van Marle-Koster E, Cord Drögemüller, Philippe Bardou, Marie-Dominique Wandhammer, Cécile Grohs, Coralie Danchin-Burge, Denis Duboule, Fiona Menzi, Amandine Blin, Raphaël Cornette, Isabelle Palhiere, Abdelhak Boukadiri, Marie-Christine Deloche, Johannes A. Lenstra, Rose-Marie Arbogast, Daniele Bigi, Ben Jemaa S, Eric Pailhoux, Stache M, Julia M. Paris, J. Zakany, Aurélie Hintermann, Julie Rivière, Cécile Donnadieu, Aurélien Capitan, Diane Esquerre, Joséphine Lesur, Ivica Medugorac, Alain Pinton, Ockert Greyvenstein, Gjoko Bunevski, Hedges J, David G. Riley, James Kijas, Gwenola Tosser-Klopp, and Claude Guintard
Subjects: biology, Evolutionary biology, Mutant, Locus (genetics), Bovidae, Morphogenetic field, Allele, biology.organism_classification, Haploinsufficiency, Gene, Bilateria
Abstract: In the course of evolution, pecorans (i.e. higher ruminants) developed a remarkable diversity of osseous cranial appendages, collectively referred to as ‘headgear’, which likely share the same origin and genetic basis. However, the nature and function of the genetic determinants underlying their number and position remain elusive. Jacob and other rare populations of sheep and goats, are characterized by polyceraty, the presence of more than two horns. Here, we characterize distinct POLYCERATE alleles in each species, both associated with defective HOXD1 function. We show that haploinsufficiency at this locus results in the splitting of horn bud primordia, likely following the abnormal extension of an initial morphogenetic field. These results highlight the key role played by this gene in headgear patterning and illustrate the evolutionary co-option of a gene involved in the early development of bilateria to properly fix the position and number of these distinctive organs of Bovidae.
Published: 2020

48. An expanded palette of improved SPLICS reporters detects multiple organelle contacts in vitro and in vivo

Author: Tito Calì, Cristina Catoni, Lucia Barazzuol, Massimo Bonora, Omar Ramirez, Paolo Pinton, Francesca Vallese, Marisa Brini, Valentina Calore, Flavia Giamogante, and Domenico Cieri
Subjects: 0301 basic medicine, Cell signaling, Science, Green Fluorescent Proteins, General Physics and Astronomy, Computational biology, Biology, Endoplasmic Reticulum, General Biochemistry, Genetics and Molecular Biology, Article, NO, Imaging, Rats, Sprague-Dawley, 03 medical and health sciences, Membrane biophysics, 0302 clinical medicine, Cytosol, In vivo, Genes, Reporter, Organelle, SPLICS, split GFP, Animals, Humans, Zebrafish, Flexibility (engineering), Neurons, Organelles, Microscopy, Multidisciplinary, Molecular engineering, Cell Membrane, Animals, Calcium, Cell Membrane, Cytosol, Endoplasmic Reticulum, Green Fluorescent Proteins, HeLa Cells, Humans, Neurons, Rats, Sprague-Dawley, Organelles, Zebrafish, General Chemistry, organelle contact sites, SPLICS, split GFP, Rats, Sprague dawley, 030104 developmental biology, Palette (painting), organelle contact sites, Calcium, Sprague-Dawley, 030217 neurology & neurosurgery, Cell signalling, HeLa Cells
Abstract: Membrane contact sites between virtually any known organelle have been documented and, in the last decades, their study received momentum due to their importance for fundamental activities of the cell and for the subtle comprehension of many human diseases. The lack of tools to finely image inter-organelle proximity hindered our understanding on how these subcellular communication hubs mediate and regulate cell homeostasis. We develop an improved and expanded palette of split-GFP-based contact site sensors (SPLICS) for the detection of single and multiple organelle contact sites within a scalable distance range. We demonstrate their flexibility under physiological conditions and in living organisms., The authors have previously reported split-GFP-based contact site sensors (SPLICS) to document endoplasmic reticulum/mitochondria contact sites. Here they extend this work and develop a range of improved SPLICS sensors to detect single and multiple organelle contact sites at different distances.
Published: 2020

49. Various Aspects of Calcium Signaling in the Regulation of Apoptosis, Autophagy, Cell Proliferation, and Cancer

Author: Esmaa Bouhamida, Alberto Danese, Gianluca Aguiari, Paolo Pinton, Simone Patergnani, Carlotta Giorgi, and Maurizio Previati
Subjects: autophagy, Apoptosis, Autophagy, Calcium, Cancer, Cell cycle, Chemotherapy, Therapy, Cell, Review, Biology, chemotherapy, Catalysis, NO, Inorganic Chemistry, Neoplasms, medicine, cancer, Animals, Homeostasis, Humans, Calcium Signaling, Physical and Theoretical Chemistry, Molecular Biology, Spectroscopy, Calcium signaling, Cell Proliferation, therapy, calcium, Cell growth, Organic Chemistry, apoptosis, General Medicine, medicine.disease, Computer Science Applications, Cell biology, medicine.anatomical_structure, Second messenger system, Cancer cell, cell cycle, Calcium Channels, Signal Transduction
Abstract: Calcium (Ca2+) is a major second messenger in cells and is essential for the fate and survival of all higher organisms. Different Ca2+ channels, pumps, or exchangers regulate variations in the duration and levels of intracellular Ca2+, which may be transient or sustained. These changes are then decoded by an elaborate toolkit of Ca2+-sensors, which translate Ca2+ signal to intracellular operational cell machinery, thereby regulating numerous Ca2+-dependent physiological processes. Alterations to Ca2+ homoeostasis and signaling are often deleterious and are associated with certain pathological states, including cancer. Altered Ca2+ transmission has been implicated in a variety of processes fundamental for the uncontrolled proliferation and invasiveness of tumor cells and other processes important for cancer progression, such as the development of resistance to cancer therapies. Here, we review what is known about Ca2+ signaling and how this fundamental second messenger regulates life and death decisions in the context of cancer, with particular attention directed to cell proliferation, apoptosis, and autophagy. We also explore the intersections of Ca2+ and the therapeutic targeting of cancer cells, summarizing the therapeutic opportunities for Ca2+ signal modulators to improve the effectiveness of current anticancer therapies.
Published: 2020

50. Mitochondrial Stress Responses and 'Mito-Inflammation' in Cystic Fibrosis

Author: Simone Patergnani, Veronica A.M. Vitto, Paolo Pinton, and Alessandro Rimessi
Subjects: 0301 basic medicine, Mini Review, Socio-culturale, Inflammation, Disease, Mitochondrion, Cystic fibrosis, mitochondria, inflammation, cystic fibrosis, mitochondrial stress response, lung, lung, Proinflammatory cytokine, cystic fibrosis, Pathogenesis, 03 medical and health sciences, 0302 clinical medicine, Medicine, Pharmacology (medical), Pharmacology, Lung, biology, business.industry, lcsh:RM1-950, medicine.disease, Cystic fibrosis transmembrane conductance regulator, mitochondrial stress response, mitochondria, lcsh:Therapeutics. Pharmacology, 030104 developmental biology, medicine.anatomical_structure, inflammation, 030220 oncology & carcinogenesis, Immunology, biology.protein, medicine.symptom, business
Abstract: Cystic fibrosis (CF) is a genetic disease associated to mutations in the cystic fibrosis transmembrane conductance regulator gene, which results in the alteration of biological fluid and electrolyte homeostasis. The characteristic pathological manifestation is represented by exaggerated proinflammatory response in lung of CF patients, driven by recurrent infections and worsen by hypersecretion of proinflammatory mediators and progressive tissue destruction. Treating inflammation remains a priority in CF. However, current anti-inflammatory treatments, including non-steroidal agents, are poorly effective and present dramatic side effects in CF patients. Different studies suggest an intimate relationship between mitochondria and CF lung disease, supporting the hypothesis that a decline in mitochondrial function endorses the development of the hyperinflammatory phenotype observed in CF lung. This allowed the implementation of a new concept: the “mito-inflammation,” a compartmentalization of inflammatory process, related to the role of mitochondria in engage and sustain the inflammatory responses, resulting a druggable target to counteract the amplification of inflammatory signals in CF. Here, we will offer an overview of the contribution of mitochondria in the pathogenesis of CF lung disease, delving into mitochondrial quality control responses, which concur significantly to exacerbation of CF lung inflammatory responses. Finally, we will discuss the new therapeutic avenues that aim to target the mito-inflammation, an alternative therapeutic advantage for mitochondrial quality control that improves CF patient’s inflammatory state.
Published: 2020

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