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115 results on '"Dinkova-Kostova AT"'

1. KEAP1-modifying small molecule reveals muted NRF2 signaling responses in neural stem cells from Huntington's disease patients

Author: Quinti, Luisa, Naidu, Sharadha Dayalan, Träger, Ulrike, Chen, Xiqun, Kegel-Gleason, Kimberly, Llères, David, Connolly, Colúm, Chopra, Vanita, Low, Cho, Moniot, Sébastien, Sapp, Ellen, Tousley, Adelaide R, Vodicka, Petr, Van Kanegan, Michael J, Kaltenbach, Linda S, Crawford, Lisa A, Fuszard, Matthew, Higgins, Maureen, Miller, James RC, Farmer, Ruth E, Potluri, Vijay, Samajdar, Susanta, Meisel, Lisa, Zhang, Ningzhe, Snyder, Andrew, Stein, Ross, Hersch, Steven M, Ellerby, Lisa M, Weerapana, Eranthie, Schwarzschild, Michael A, Steegborn, Clemens, Leavitt, Blair R, Degterev, Alexei, Tabrizi, Sarah J, Lo, Donald C, DiFiglia, Marian, Thompson, Leslie M, Dinkova-Kostova, Albena T, and Kazantsev, Aleksey G
Subjects: Brain Disorders, Neurodegenerative, Genetics, Huntington's Disease, Neurosciences, Rare Diseases, Clinical Research, Stem Cell Research, Aetiology, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Underpinning research, Adult, Aged, Animals, Brain, Cells, Cultured, Cytokines, Disease Models, Animal, Female, HEK293 Cells, Humans, Huntington Disease, Kelch-Like ECH-Associated Protein 1, MPTP Poisoning, Macrophages, Male, Mice, Mice, Inbred C57BL, Microglia, Middle Aged, NF-E2-Related Factor 2, Neural Stem Cells, Neuroprotective Agents, Protein Conformation, Rats, Signal Transduction, Huntington's disease, KEAP1/NRF2/ARE signaling, NRF2 inducer, antiinflammatory responses, human neural stem cells, Huntington’s disease
Abstract: The activity of the transcription factor nuclear factor-erythroid 2 p45-derived factor 2 (NRF2) is orchestrated and amplified through enhanced transcription of antioxidant and antiinflammatory target genes. The present study has characterized a triazole-containing inducer of NRF2 and elucidated the mechanism by which this molecule activates NRF2 signaling. In a highly selective manner, the compound covalently modifies a critical stress-sensor cysteine (C151) of the E3 ligase substrate adaptor protein Kelch-like ECH-associated protein 1 (KEAP1), the primary negative regulator of NRF2. We further used this inducer to probe the functional consequences of selective activation of NRF2 signaling in Huntington's disease (HD) mouse and human model systems. Surprisingly, we discovered a muted NRF2 activation response in human HD neural stem cells, which was restored by genetic correction of the disease-causing mutation. In contrast, selective activation of NRF2 signaling potently repressed the release of the proinflammatory cytokine IL-6 in primary mouse HD and WT microglia and astrocytes. Moreover, in primary monocytes from HD patients and healthy subjects, NRF2 induction repressed expression of the proinflammatory cytokines IL-1, IL-6, IL-8, and TNFα. Together, our results demonstrate a multifaceted protective potential of NRF2 signaling in key cell types relevant to HD pathology.
Published: 2017

2. SIRT2- and NRF2-Targeting Thiazole-Containing Compound with Therapeutic Activity in Huntington's Disease Models.

Author: Quinti, Luisa, Casale, Malcolm, Moniot, Sébastien, Pais, Teresa F, Van Kanegan, Michael J, Kaltenbach, Linda S, Pallos, Judit, Lim, Ryan G, Naidu, Sharadha Dayalan, Runne, Heike, Meisel, Lisa, Rauf, Nazifa Abdul, Leyfer, Dmitriy, Maxwell, Michele M, Saiah, Eddine, Landers, John E, Luthi-Carter, Ruth, Abagyan, Ruben, Dinkova-Kostova, Albena T, Steegborn, Clemens, Marsh, J Lawrence, Lo, Donald C, Thompson, Leslie M, and Kazantsev, Aleksey G
Subjects: Cell Line, Animals, Rats, Drosophila, Huntington Disease, Disease Models, Animal, Thiazoles, Neuroprotective Agents, Structure-Activity Relationship, Dose-Response Relationship, Drug, NF-E2-Related Factor 2, Sirtuin 2, Neurosciences, Huntington's Disease, Orphan Drug, Neurodegenerative, Brain Disorders, Rare Diseases, 5.1 Pharmaceuticals, Neurological
Abstract: There are currently no disease-modifying therapies for the neurodegenerative disorder Huntington's disease (HD). This study identified novel thiazole-containing inhibitors of the deacetylase sirtuin-2 (SIRT2) with neuroprotective activity in ex vivo brain slice and Drosophila models of HD. A systems biology approach revealed an additional SIRT2-independent property of the lead-compound, MIND4, as an inducer of cytoprotective NRF2 (nuclear factor-erythroid 2 p45-derived factor 2) activity. Structure-activity relationship studies further identified a potent NRF2 activator (MIND4-17) lacking SIRT2 inhibitory activity. MIND compounds induced NRF2 activation responses in neuronal and non-neuronal cells and reduced production of reactive oxygen species and nitrogen intermediates. These drug-like thiazole-containing compounds represent an exciting opportunity for development of multi-targeted agents with potentially synergistic therapeutic benefits in HD and related disorders.
Published: 2016

3. Chronic hyperglycaemia increases the vulnerability of the hippocampus to oxidative damage induced during post-hypoglycaemic hyperglycaemia in a mouse model of chemically induced type 1 diabetes

Author: McNeilly, Alison D, Gallagher, Jennifer R, Evans, Mark L, De Galan, Bastiaan E, Pedersen-Bjergaard, Ulrik, Thorens, Bernard, Dinkova-Kostova, Albena T, Huang, Jeffrey-T, Ashford, Michael LJ, McCrimmon, Rory J, Hypo-RESOLVE Consortium, Apollo - University of Cambridge Repository, and Evans, Mark [0000-0001-8122-8987]
Subjects: Blood Glucose, Mouse, NF-E2-Related Factor 2, Nfe2l2, Hippocampus, Glycaemic variability, Nrf2, Hypoglycemia, Diabetes Mellitus, Experimental, Mice, Oxidative Stress, Hyperinsulinaemic glucose clamp, Type 1 diabetes, Diabetes Mellitus, Type 1, Hyperglycemia, Animals, Hypoglycemic Agents, Hypoglycaemia, Proteotoxic stress
Abstract: AIMS/HYPOTHESIS: Chronic hyperglycaemia and recurrent hypoglycaemia are independently associated with accelerated cognitive decline in type 1 diabetes. Recurrent hypoglycaemia in rodent models of chemically induced (streptozotocin [STZ]) diabetes leads to cognitive impairment in memory-related tasks associated with hippocampal oxidative damage. This study examined the hypothesis that post-hypoglycaemic hyperglycaemia in STZ-diabetes exacerbates hippocampal oxidative stress and explored potential contributory mechanisms. METHODS: The hyperinsulinaemic glucose clamp technique was used to induce equivalent hypoglycaemia and to control post-hypoglycaemic glucose levels in mice with and without STZ-diabetes and Nrf2-/- mice (lacking Nrf2 [also known as Nfe2l2]). Subsequently, quantitative proteomics based on stable isotope labelling by amino acids in cell culture and biochemical approaches were used to assess oxidative damage and explore contributory pathways. RESULTS: Evidence of hippocampal oxidative damage was most marked in mice with STZ-diabetes exposed to post-hypoglycaemic hyperglycaemia; these mice also showed induction of Nrf2 and the Nrf2 transcriptional targets Sod2 and Hmox-1. In this group, hypoglycaemia induced a significant upregulation of proteins involved in alternative fuel provision, reductive biosynthesis and degradation of damaged proteins, and a significant downregulation of proteins mediating the stress response. Key differences emerged between mice with and without STZ-diabetes following recovery from hypoglycaemia in proteins mediating the stress response and reductive biosynthesis. CONCLUSIONS/INTERPRETATION: There is a disruption of the cellular response to a hypoglycaemic challenge in mice with STZ-induced diabetes that is not seen in wild-type non-diabetic animals. The chronic hyperglycaemia of diabetes and post-hypoglycaemic hyperglycaemia act synergistically to induce oxidative stress and damage in the hippocampus, possibly leading to irreversible damage/modification to proteins or synapses between cells. In conclusion, recurrent hypoglycaemia in sub-optimally controlled diabetes may contribute, at least in part, to accelerated cognitive decline through amplifying oxidative damage in key brain regions, such as the hippocampus. DATA AVAILABILITY: The datasets generated during and/or analysed during the current study are available in ProteomeXchange, accession no. 1-20220824-173727 ( www.proteomexchange.org ). Additional datasets generated during and/or analysed during the present study are available from the corresponding author upon reasonable request.
Published: 2023

4. Nonalcoholic steatohepatitis and mechanisms by which it is ameliorated by activation of the CNC-bZIP transcription factor Nrf2

Author: Boushra Bathish, Holly Robertson, John F. Dillon, Albena T. Dinkova-Kostova, and John D. Hayes
Subjects: Inflammation, Mice, Oxidative Stress, Iron Overload, Kelch-Like ECH-Associated Protein 1, Liver, NF-E2-Related Factor 2, Non-alcoholic Fatty Liver Disease, Physiology (medical), NF-kappa B, Animals, beta-Transducin Repeat-Containing Proteins, Biochemistry
Abstract: Non-alcoholic steatohepatitis (NASH) represents a global health concern. It is characterised by fatty liver, hepatocyte cell death and inflammation, which are associated with lipotoxicity, endoplasmic reticulum (ER) stress, mitochondrial dysfunction, iron overload and oxidative stress. NF-E2 p45-related factor 2 (Nrf2) is a transcription factor that combats oxidative stress. Remarkably, Nrf2 is downregulated during the development of NASH, which probably accelerates disease, whereas in pre-clinical studies the upregulation of Nrf2 inhibits NASH. We now review the scientific literature that proposes Nrf2 downregulation during NASH involves its increased ubiquitylation and proteasomal degradation, mediated by Kelch-like ECH-associated protein 1 (Keap1) and/or β-transducin repeat-containing protein (β-TrCP) and/or HMG-CoA reductase degradation protein 1 (Hrd1, also called synoviolin (SYVN1)). Additionally, downregulation of Nrf2-mediated transcription during NASH may involve diminished recruitment of coactivators by Nrf2, due to increased levels of activating transcription factor 3 (ATF3) and nuclear factor-kappaB (NF-κB) p65, or competition for promoter binding due to upregulation of BTB and CNC homology 1 (Bach1). Many processes that downregulate Nrf2 are triggered by transforming growth factor-beta (TGF-β), with oxidative stress amplifying its signalling. Oxidative stress may also increase suppression of Nrf2 by β-TrCP through facilitating formation of the DSGIS-containing phosphodegron in Nrf2 by glycogen synthase kinase-3. In animal models, knockout of Nrf2 increases susceptibility to NASH, while pharmacological activation of Nrf2 by inducing agents that target Keap1 inhibits development of NASH. These inducing agents probably counter Nrf2 downregulation affected by β-TrCP, Hrd1/SYVN1, ATF3, NF-κB p65 and Bach1, by suppressing oxidative stress. Activation of Nrf2 is also likely to inhibit NASH by ameliorating lipotoxicity, inflammation, ER stress and iron overload. Crucially, pharmacological activation of Nrf2 in mice in which NASH has already been established supresses liver steatosis and inflammation. There is therefore compelling evidence that pharmacological activation of Nrf2 provides a comprehensive multipronged strategy to treat NASH.
Published: 2022

5. DIA label-free proteomic analysis of murine bone-marrow-derived macrophages

Author: Christa P. Baker, Iain R. Phair, Alejandro J. Brenes, Abdelmadjid Atrih, Dylan G. Ryan, Roland Bruderer, Albena T. Dinkova-Kostova, Douglas J. Lamont, J. Simon C. Arthur, Andrew J.M. Howden, Dinkova-Kostova, Albena T [0000-0003-0316-9859], and Apollo - University of Cambridge Repository
Subjects: FOS: Computer and information sciences, Proteomics, General Immunology and Microbiology, Mass spectrometry, Bioinformatics, General Neuroscience, FOS: Clinical medicine, Immunology, Reproducibility of Results, Protein biochemistry, General Biochemistry, Genetics and Molecular Biology, Mice, Bone Marrow, Animals, Peptides
Abstract: Here, we describe an optimized protocol to analyze murine bone-marrow-derived macrophages using label-free data-independent acquisition (DIA) proteomics. We provide a complete step-by-step protocol describing sample preparation utilizing the S-Trap approach for on-column digestion and peptide purification. We then detail mass spectrometry data acquisition and approaches for data analysis. Single-shot DIA protocols achieve comparable proteomic depth with data-dependent MS approaches without the need for fractionation. This allows for better scaling for large sample numbers with high inter-experimental reproducibility. For complete details on the use and execution of this protocol, please refer to Ryan et al. (2022).
Published: 2022

6. Nrf2 activation does not affect adenoma development in a mouse model of colorectal cancer

Author: Albena T. Dinkova-Kostova, Julian L. Griffin, Elena V. Knatko, Colin J. Henderson, Cecilia Castro, Ying Zhang, C. Roland Wolf, Maureen Higgins, Tadashi Honda, Honda, Tadashi [0000-0003-0746-9453], Griffin, Julian L. [0000-0003-1336-7744], Dinkova-Kostova, Albena T. [0000-0003-0316-9859], Apollo - University of Cambridge Repository, Griffin, Julian L [0000-0003-1336-7744], and Dinkova-Kostova, Albena T [0000-0003-0316-9859]
Subjects: Adenoma, Male, 631/67, Colorectal cancer, QH301-705.5, Carcinogenesis, NF-E2-Related Factor 2, Medicine (miscellaneous), Colorectal adenoma, Biology, medicine.disease_cause, digestive system, environment and public health, General Biochemistry, Genetics and Molecular Biology, Mice, medicine, Animals, Biology (General), Transcription factor, Cancer, 64, Gene knockdown, Drug discovery, 631/154, article, respiratory system, medicine.disease, KEAP1, digestive system diseases, Disease Models, Animal, Cancer research, Female, 64/60, General Agricultural and Biological Sciences, Colorectal Neoplasms
Abstract: Funder: Stony Brook Foundation Reata Pharmaceuticals, Transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) and its main negative regulator, Kelch-like ECH associated protein 1 (Keap1), are at the interface between redox and intermediary metabolism. Nrf2 activation is protective in models of human disease and has benefits in clinical trials. Consequently, the Keap1/Nrf2 protein complex is a drug target. However, in cancer Nrf2 plays a dual role, raising concerns that Nrf2 activators may promote growth of early neoplasms. To address this concern, we examined the role of Nrf2 in development of colorectal adenomas by employing genetic, pharmacological, and metabolomic approaches. We found that colorectal adenomas that form in Gstp−/−: ApcMin/+ mice are characterized by altered one-carbon metabolism and that genetic activation, but not disruption of Nrf2, enhances these metabolic alterations. However, this enhancement is modest compared to the magnitude of metabolic differences between tumor and peri-tumoral tissues, suggesting that the metabolic changes conferred by Nrf2 activation may have little contribution to the early stages of carcinogenesis. Indeed, neither genetic (by Keap1 knockdown) nor pharmacological Nrf2 activation, nor its disruption, affected colorectal adenoma formation in this model. We conclude that pharmacological Nrf2 activation is unlikely to impact the early stages of development of colorectal cancer.
Published: 2021
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7. Synthesis and Anti‐Inflammatory Activity of 2‐Amino‐4,5,6,7‐tetrahydrobenzo[ b ]thiophene‐Derived NRF2 Activators

Author: Kit‐Kay Mak, Zhang Shiming, Ola Epemolu, Albena T. Dinkova‐Kostova, Geoffrey Wells, Irina G. Gazaryan, Raghavendra Sakirolla, Zulkefeli Mohd, and Mallikarjuna Rao Pichika
Subjects: Lipopolysaccharides, Kelch-Like ECH-Associated Protein 1, NF-E2-Related Factor 2, Tumor Necrosis Factor-alpha, Interleukin-6, NF-kappa B, Anti-Inflammatory Agents, Thiophenes, General Chemistry, Dinoprostone, Rats, Mice, Cyclooxygenase 2, Humans, Animals, Cytokines, RNA, Messenger, Inflammation Mediators
Abstract: This is the first study investigating the nuclear factor (erythroid-derived 2)-like 2 (NRF2) activity of compounds containing a new scaffold, tetrahydrobenzo[b]thiophene. Eighteen compounds were synthesised and confirmed their NRF2 activation through NQO1 enzymatic activity and mRNA expression of NQO1 and HO-1 in Hepa-1c1c7 cells. The compounds disrupted the interaction between Kelch-like ECH-associated protein 1 (KEAP1) and NRF2 via interfering with the KEAP1's Kelch domain. The compounds exhibited anti-inflammatory activity in Escherichia coli Lipopolysaccharide (LPS
Published: 2022

8. Anti-Inflammatory Effects of Auranamide and Patriscabratine—Mechanisms and In Silico Studies

Author: Kit-Kay Mak, Zhang Shiming, Jun Sheng Low, Madhu Katyayani Balijepalli, Raghavendra Sakirolla, Albena T. Dinkova-Kostova, Ola Epemolu, Zulkefeli Mohd, and Mallikarjuna Rao Pichika
Subjects: Flavonoids, Lipopolysaccharides, Glycogen Synthase Kinase 3 beta, Kelch-Like ECH-Associated Protein 1, NF-E2-Related Factor 2, Organic Chemistry, Anti-Inflammatory Agents, NF-kappa B, Pharmaceutical Science, Nitric Oxide, Amides, Rats, Analytical Chemistry, Molecular Docking Simulation, Mice, Chemistry (miscellaneous), Drug Discovery, Animals, Cytokines, Humans, Molecular Medicine, Physical and Theoretical Chemistry, Heme Oxygenase-1, auranamide, patriscabratine, Melastoma malabathricum, NRF2, KEAP1, anti-inflammatory
Abstract: Auranamide and patriscabratine are amides from Melastoma malabathricum (L.) Smith. Their anti-inflammatory activity and nuclear factor erythroid 2-related factor 2 (NRF2) activation ability were evaluated using Escherichia coli lipopolysaccharide (LPSEc)-stimulated murine macrophages (RAW264.7) and murine hepatoma (Hepa-1c1c7) cells, respectively. The cytotoxicity of the compounds was assessed using a 3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyl tetrazolium bromide (MTT) assay. The anti-inflammatory activity was determined by measuring the nitric oxide (NO) production and pro-inflammatory cytokines (Interleukin (IL)-1β, Interferon (IFN)-γ, tumour necrosis factor (TNF)-α, and IL-6) and mediators (NF-κB and COX-2). NRF2 activation was determined by measuring the nicotinamide adenine dinucleotide phosphate hydrogen (NADPH) quinone oxidoreductase 1 (NQO1), nuclear NRF2 and hemeoxygenase (HO)-1. In vitro metabolic stability was assessed using the mouse, rat, and human liver microsomes. The compounds were non-toxic to the cells at 10 μM. Both compounds showed dose-dependent effects in downregulating NO production and pro-inflammatory cytokines and mediators. The compounds also showed upregulation of NQO1 activity and nuclear NRF2 and HO-1 levels. The compounds were metabolically stable in mouse, rat and human liver microsomes. The possible molecular targets of NRF2 activation by these two compounds were predicted using molecular docking studies and it was found that the compounds might inhibit the Kelch domain of KEAP1 and GSK-3β activity. The physicochemical and drug-like properties of the test compounds were predicted using Schrodinger small molecule drug discovery suite (v.2022-2).
Published: 2022
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9. Oxidative Stress in Cancer

Author: John D. Hayes, Albena T. Dinkova-Kostova, and Kenneth D. Tew
Subjects: 0301 basic medicine, Cancer Research, Apoptosis, Pentose phosphate pathway, medicine.disease_cause, Article, Antioxidants, 03 medical and health sciences, 0302 clinical medicine, Neoplasms, medicine, Animals, Humans, HSF1, Transcription factor, chemistry.chemical_classification, Reactive oxygen species, AMPK, Cell Biology, Cell biology, Oxidative Stress, Glucose, 030104 developmental biology, Oncology, chemistry, 030220 oncology & carcinogenesis, Cancer cell, Energy Metabolism, Reactive Oxygen Species, Carcinogenesis, NADP, Oxidative stress
Abstract: Contingent upon concentration, reactive oxygen species (ROS) influence cancer evolution in apparently contradictory ways, either initiating/stimulating tumorigenesis and supporting transformation/proliferation of cancer cells or causing cell death. To accommodate high ROS levels, tumor cells modify sulfur-based metabolism, NADPH generation, and the activity of antioxidant transcription factors. During initiation, genetic changes enable cell survival under high ROS levels by activating antioxidant transcription factors or increasing NADPH via the pentose phosphate pathway (PPP). During progression and metastasis, tumor cells adapt to oxidative stress by increasing NADPH in various ways, including activation of AMPK, the PPP, and reductive glutamine and folate metabolism.
Published: 2020

10. Activation of transcription factor Nrf2 to counteract mitochondrial dysfunction in Parkinson's disease

Author: Albena T. Dinkova-Kostova and Claudia Bento-Pereira
Subjects: Parkinson's disease, NF-E2-Related Factor 2, Disease, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, Drug Discovery, medicine, Genetic predisposition, Animals, Transcription factor, Gene, Neuroinflammation, 030304 developmental biology, Pharmacology, 0303 health sciences, business.industry, Parkinson Disease, medicine.disease, NFE2L2, Mitochondria, Oxidative Stress, Gene Expression Regulation, 030220 oncology & carcinogenesis, Molecular Medicine, business, Neuroscience, Oxidative stress
Abstract: Parkinson's disease (PD) is a progressive neurodegenerative disorder, for which no disease-modifying therapies are available to date. Although understanding of the precise aetiology of PD is incomplete, it is clear that age, genetic predisposition and environmental stressors increase the risk. At the cellular level, oxidative stress, chronic neuroinflammation, mitochondrial dysfunction and aberrant protein aggregation have been implicated as contributing factors. These detrimental processes are counteracted by elaborate networks of cellular defence mechanisms, one of which is orchestrated by transcription factor nuclear factor-erythroid 2 p45-related factor 2 (Nrf2; gene name NFE2L2). A wealth of preclinical evidence suggests that Nrf2 activation is beneficial in cellular and animal models of PD. In this review, we summarise the current understanding of mitochondrial dysfunction in PD, the role of Nrf2 in mitochondrial function and explore the potential of Nrf2 as a therapeutic target for mitochondrial dysfunction in PD.
Published: 2020

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, 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Da-Hye, Lee, Edward, Lee, Erinna, Lee, Gyun Min, Lee, He-Jin, Lee, Heung Kyu, Lee, Jae Man, Lee, Jason, Lee, Jin-A, Lee, Joo-Yong, Lee, Jun Hee, Lee, Michael, Lee, Min Goo, Lee, Min Jae, Lee, Myung-Shik, Lee, Sang Yoon, Lee, Seung-Jae, Lee, Stella, Lee, Sung Bae, Lee, Won Hee, Lee, Ying-Ray, Lee, Yong-ho, Lee, Youngil, Lefebvre, Christophe, Legouis, Renaud, Lei, Yu, Lei, Yuchen, Leikin, Sergey, Leitinger, Gerd, Lemus, Leticia, Leng, Shuilong, Lenoir, Olivia, Lenz, Guido, Lenz, Heinz Josef, Lenzi, Paola, León, Yolanda, Leopoldino, Andréia, Leschczyk, Christoph, Leskelä, Stina, Letellier, Elisabeth, Leung, Chi-Ting, Leung, Po Sing, Leventhal, Jeremy, Levine, Beth, Lewis, Patrick, Ley, Klaus, Li, Bin, Li, Da-Qiang, Li, Jianming, Li, Jing, Li, Jiong, Li, Ke, Li, Liwu, Li, Mei, Li, Min, Li, Ming, Li, Mingchuan, Li, Pin-Lan, Li, Ming-Qing, Li, Qing, Li, Sheng, Li, Tiangang, Li, Wei, Li, Wenming, Li, Xue, Li, Yi-Ping, Li, Yuan, Li, Zhiqiang, Li, Zhiyong, Li, Zhiyuan, Lian, Jiqin, Liang, Chengyu, Liang, Qiangrong, Liang, Weicheng, Liang, Yongheng, Liang, YongTian, Liao, Guanghong, Liao, Lujian, Liao, Mingzhi, Liao, Yung-Feng, Librizzi, Mariangela, Lie, Pearl, Lilly, Mary, Lim, Hyunjung, Lima, Thania, Limana, Federica, Lin, Chao, Lin, Chih-Wen, Lin, Dar-Shong, Lin, Fu-Cheng, Lin, Jiandie, Lin, Kurt, Lin, Kwang-Huei, Lin, Liang-Tzung, LIN, Pei-Hui, Lin, Qiong, Lin, Shaofeng, Lin, Su-Ju, Lin, Wenyu, Lin, Xueying, Lin, Yao-Xin, Lin, Yee-Shin, Linden, Rafael, Lindner, Paula, Ling, Shuo-Chien, Lingor, Paul, Linnemann, Amelia, Liou, Yih-Cherng, Lipinski, Marta, Lipovšek, Saška, Lira, Vitor, Lisiak, Natalia, Liton, Paloma, Liu, Chao, Liu, Ching-Hsuan, Liu, Chun-Feng, Liu, Cui Hua, Liu, Fang, Liu, Hao, Liu, Hsiao-Sheng, Liu, Hua-feng, Liu, Huifang, Liu, Jia, Liu, Jing, Liu, Julia, Liu, Leyuan, Liu, Longhua, Liu, Meilian, Liu, Qin, Liu, Wei, Liu, Wende, Liu, Xiao-Hong, Liu, Xiaodong, Liu, Xingguo, Liu, Xu, Liu, Xuedong, Liu, Yanfen, Liu, Yang, Liu, Yueyang, Liu, Yule, Livingston, J Andrew, Lizard, Gerard, Lizcano, Jose, Ljubojevic-Holzer, Senka, LLeonart, Matilde, Llobet-Navàs, David, Llorente, Alicia, Lo, Chih Hung, Lobato-Márquez, Damián, Long, Qi, Long, Yun Chau, Loos, Ben, Loos, Julia, López, Manuela, López-Doménech, Guillermo, López-Guerrero, José Antonio, López-Jiménez, Ana, López-Pérez, Óscar, López-Valero, Israel, Lorenowicz, Magdalena, Lorente, Mar, Lorincz, Peter, Lossi, Laura, Lotersztajn, Sophie, Lovat, Penny, Lovell, Jonathan, Lovy, Alenka, Lőw, Péter, Lu, Guang, Lu, Haocheng, Lu, Jia-Hong, Lu, Jin-Jian, Lu, Mengji, Lu, Shuyan, Luciani, Alessandro, Lucocq, John, Ludovico, Paula, Luftig, Micah, Luhr, Morten, Luis-Ravelo, Diego, Lum, Julian, Luna-Dulcey, Liany, Lund, Anders, Lund, Viktor, Lünemann, Jan, Lüningschrör, Patrick, Luo, Honglin, Luo, Rongcan, Luo, Shouqing, Luo, Zhi, Luparello, Claudio, Lüscher, Bernhard, Luu, Luan, Lyakhovich, Alex, Lyamzaev, Konstantin, Lystad, Alf Håkon, Lytvynchuk, Lyubomyr, Ma, Alvin, Ma, Changle, Ma, Mengxiao, Ma, Ning-Fang, Ma, Quan-Hong, Ma, Xinliang, Ma, Yueyun, Ma, Zhenyi, MacDougald, Ormond, Macian, Fernando, MacIntosh, Gustavo, MacKeigan, Jeffrey, Macleod, Kay, Maday, Sandra, Madeo, Frank, Madesh, Muniswamy, Madl, Tobias, Madrigal-Matute, Julio, Maeda, Akiko, Maejima, Yasuhiro, Magarinos, Marta, Mahavadi, Poornima, Maiani, Emiliano, Maiese, Kenneth, Maiti, Panchanan, Maiuri, Maria Chiara, Majello, Barbara, Major, Michael, Makareeva, Elena, Malik, Fayaz, Mallilankaraman, Karthik, Malorni, Walter, Maloyan, Alina, Mammadova, Najiba, Man, Gene Chi Wai, Manai, Federico, Mancias, Joseph, Mandelkow, Eva-Maria, Mandell, Michael, Manfredi, Angelo, Manjili, Masoud, Manjithaya, Ravi, Manque, Patricio, Manshian, Bella, Manzano, Raquel, Manzoni, Claudia, Mao, Kai, Marchese, Cinzia, Marchetti, Sandrine, Marconi, Anna Maria, Marcucci, Fabrizio, Mardente, Stefania, Mareninova, Olga, Margeta, Marta, Mari, Muriel, Marinelli, Sara, Marinelli, Oliviero, Mariño, Guillermo, Mariotto, Sofia, Marshall, Richard, Marten, Mark, Martens, Sascha, Martin, Alexandre, Martin, Katie, Martin, Sara, Martin, Shaun, Martín-Segura, Adrián, Martín-Acebes, Miguel, Martin-Burriel, Inmaculada, Martin-Rincon, Marcos, Martin-Sanz, Paloma, Martina, José, Martinet, Wim, Martinez, Aitor, Martinez, Ana, Martinez, Jennifer, Martinez Velazquez, Moises, Martinez-Lopez, Nuria, Martinez-Vicente, Marta, Martins, Daniel, Martins, Joilson, Martins, Waleska, Martins-Marques, Tania, Marzetti, Emanuele, Masaldan, Shashank, Masclaux-Daubresse, Celine, Mashek, Douglas, Massa, Valentina, Massieu, Lourdes, Masson, Glenn, Masuelli, Laura, Masyuk, Anatoliy, Masyuk, Tetyana, Matarrese, Paola, Matheu, Ander, Matoba, Satoaki, Matsuzaki, Sachiko, Mattar, Pamela, Matte, Alessandro, Mattoscio, Domenico, Mauriz, José, Mauthe, Mario, Mauvezin, Caroline, Maverakis, Emanual, Maycotte, Paola, Mayer, Johanna, Mazzoccoli, Gianluigi, Mazzoni, Cristina, Mazzulli, Joseph, McCarty, Nami, Mcdonald, Christine, McGill, Mitchell, McKenna, Sharon, Mclaughlin, Bethann, McLoughlin, Fionn, McNiven, Mark, McWilliams, Thomas, Mechta-Grigoriou, Fatima, Medeiros, Tania Catarina, Medina, Diego, Megeney, Lynn, Megyeri, Klara, Mehrpour, Maryam, Mehta, Jawahar, Meijer, Alfred, Meijer, Annemarie, Mejlvang, Jakob, Meléndez, Alicia, Melk, Annette, Memisoglu, Gonen, Mendes, Alexandrina, Meng, Delong, Meng, Fei, Meng, Tian, Menna-Barreto, Rubem, Menon, Manoj, Mercer, Carol, Mercier, Anne, MERGNY, Jean-Louis, Merighi, Adalberto, Merkley, Seth, Merla, Giuseppe, Meske, Volker, Mestre, Ana Cecilia, Metur, Shree Padma, Meyer, Christian, Meyer, Hemmo, Mi, Wenyi, Mialet-Perez, Jeanne, Miao, Junying, Micale, Lucia, Miki, Yasuo, Milan, Enrico, Milczarek, Małgorzata, Miller, Dana, Miller, Samuel, Miller, Silke, Millward, Steven, Milosevic, Ira, Minina, Elena, Mirzaei, Hamed, Mirzaei, Hamid Reza, Mirzaei, Mehdi, Mishra, Amit, Mishra, Nandita, Mishra, Paras Kumar, Misirkic Marjanovic, Maja, Misasi, Roberta, Misra, Amit, Misso, Gabriella, Mitchell, Claire, Mitou, Geraldine, Miura, Tetsuji, Miyamoto, Shigeki, MIYAZAKI, Makoto, Miyazaki, Mitsunori, Miyazaki, Taiga, Miyazawa, Keisuke, Mizushima, Noboru, Mogensen, Trine, Mograbi, Baharia, Mohammadinejad, Reza, Mohamud, Yasir, Mohanty, Abhishek, Mohapatra, Sipra, Möhlmann, Torsten, Mohmmed, Asif, Moles, Anna, Moley, Kelle, Molinari, Maurizio, Mollace, Vincenzo, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Montagna, Costanza, Monteiro, Mervyn, Montella, Andrea, Montes, L Ruth, Montico, Barbara, Mony, Vinod, Monzio Compagnoni, Giacomo, Moore, Michael, Moosavi, Mohammad, Mora, Ana, Mora, Marina, Morales-Alamo, David, Moratalla, Rosario, Moreira, Paula, Morelli, Elena, Moreno, Sandra, Moreno-Blas, Daniel, Moresi, Viviana, Morga, Benjamin, Morgan, Alwena, Morin, Fabrice, Morishita, Hideaki, Moritz, Orson, Moriyama, Mariko, Moriyasu, Yuji, Morleo, Manuela, Morselli, Eugenia, Moruno-Manchon, Jose, Moscat, Jorge, Mostowy, Serge, Motori, Elisa, Moura, Andrea 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Ney, Paul, Nezis, Ioannis, Ng, Charlene, Ng, Tzi Bun, Nguyen, Hang, Nguyen, Long, Ni, Hong-Min, Ní Cheallaigh, Clíona, Ni, Zhenhong, Nicolao, M Celeste, Nicoli, Francesco, Nieto-Diaz, Manuel, Nilsson, Per, Ning, Shunbin, Niranjan, Rituraj, Nishimune, Hiroshi, Niso-Santano, Mireia, Nixon, Ralph, Nobili, Annalisa, Nobrega, Clevio, Noda, Takeshi, Nogueira-Recalde, Uxía, Nolan, Trevor, Nombela, Ivan, Novak, Ivana, Novoa, Beatriz, Nozawa, Takashi, Nukina, Nobuyuki, Nussbaum-Krammer, Carmen, Nylandsted, Jesper, O'Donovan, Tracey, O'Leary, Seónadh, O'Rourke, Eyleen, O'Sullivan, Mary, O'Sullivan, Timothy, Oddo, Salvatore, Oehme, Ina, Ogawa, Michinaga, Ogier-Denis, Eric, Ogmundsdottir, Margret, Ogretmen, Besim, Oh, Goo Taeg, Oh, Seon-Hee, Oh, Young, Ohama, Takashi, Ohashi, Yohei, Ohmuraya, Masaki, Oikonomou, Vasileios, Ojha, Rani, Okamoto, Koji, Okazawa, Hitoshi, Oku, Masahide, Oliván, Sara, Oliveira, Jorge, Ollmann, Michael, Olzmann, James, Omari, Shakib, Omary, M Bishr, Önal, Gizem, Ondrej, 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Andrei, Smith, Matthew, Soenen, Stefaan, Sohn, Eun Jung, Sok, Sophia, Solaini, Giancarlo, Soldati, Thierry, Soleimanpour, Scott, Soler, Rosa, Solovchenko, Alexei, Somarelli, Jason, Sonawane, Avinash, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Kunhua, Song, Zhiyin, Soria, Leandro, Sorice, Maurizio, Soukas, Alexander, Soukup, Sandra-Fausia, Sousa, Diana, Sousa, Nadia, Spagnuolo, Paul, Spector, Stephen, Srinivas Bharath, M., St Clair, Daret, Stagni, Venturina, Staiano, Leopoldo, Stalnecker, Clint, Stankov, Metodi, Stathopulos, Peter, Stefan, Katja, Stefan, Sven Marcel, Stefanis, Leonidas, Steffan, Joan, Steinkasserer, Alexander, Stenmark, Harald, Sterneckert, Jared, Stevens, Craig, Stoka, Veronika, Storch, Stephan, Stork, Björn, Strappazzon, Flavie, Strohecker, Anne Marie, Stupack, Dwayne, Su, Huanxing, Su, Ling-Yan, Su, Longxiang, Suarez-Fontes, Ana, Subauste, Carlos, Subbian, Selvakumar, Subirada, Paula, Sudhandiran, Ganapasam, Sue, Carolyn, Sui, Xinbing, Summers, Corey, Sun, Guangchao, Sun, Jun, SUN, Kang, Sun, Meng-xiang, Sun, Qiming, Sun, Yi, Sun, Zhongjie, Sunahara, Karen, Sundberg, Eva, Susztak, Katalin, Sutovsky, Peter, Suzuki, Hidekazu, Sweeney, Gary, Symons, J David, Sze, Stephen Cho Wing, Szewczyk, Nathaniel, Tabęcka-Łonczynska, Anna, Tabolacci, Claudio, Tacke, Frank, Taegtmeyer, Heinrich, Tafani, Marco, Tagaya, Mitsuo, Tai, Haoran, Tait, Stephen, Takahashi, Yoshinori, Takats, Szabolcs, Talwar, Priti, Tam, Chit, Tam, Shing Yau, Tampellini, Davide, Tamura, Atsushi, Tan, Chong Teik, Tan, Eng-King, Tan, Ya-Qin, Tanaka, Masaki, Tanaka, Motomasa, Tang, Daolin, Tang, Jingfeng, Tang, Tie-Shan, Tanida, Isei, Tao, Zhipeng, Taouis, Mohammed, Tatenhorst, Lars, Tavernarakis, Nektarios, Taylor, Allen, Taylor, Gregory, Taylor, Joan, Tchetina, Elena, Tee, Andrew, Tegeder, Irmgard, Teis, David, Teixeira, Natercia, Teixeira-Clerc, Fatima, Tekirdag, Kumsal, Tencomnao, Tewin, Tenreiro, Sandra, Tepikin, Alexei, Testillano, Pilar, Tettamanti, Gianluca, Tharaux, Pierre-Louis, Thedieck, Kathrin, Thekkinghat, Arvind, Thellung, Stefano, Thinwa, Josephine, Thirumalaikumar, V.P., Thomas, Sufi Mary, Thomes, Paul, Thorburn, Andrew, Thukral, Lipi, Thum, Thomas, Thumm, Michael, Tian, Ling, Tichy, Ales, Till, Andreas, Timmerman, Vincent, Titorenko, Vladimir, Todi, Sokol, Todorova, Krassimira, Toivonen, Janne, Tomaipitinca, Luana, Tomar, Dhanendra, Tomas-Zapico, Cristina, Tomić, Sergej, Tong, Benjamin Chun-Kit, Tong, Chao, Tong, Xin, Tooze, Sharon, Torgersen, Maria, Torii, Satoru, Torres-López, Liliana, Torriglia, Alicia, Towers, Christina, Towns, Roberto, Toyokuni, Shinya, Trajkovic, Vladimir, Tramontano, Donatella, Tran, Quynh-Giao, Travassos, Leonardo, Trelford, Charles, Tremel, Shirley, Trougakos, Ioannis, Tsao, Betty, Tschan, Mario, Tse, Hung-Fat, Tse, Tak Fu, Tsugawa, Hitoshi, Tsvetkov, Andrey, Tumbarello, David, Tumtas, Yasin, Tuñón, María, Turcotte, Sandra, Turk, Boris, Turk, Vito, Turner, Bradley, Tuxworth, Richard, Tyler, Jessica, Tyutereva, Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, 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. 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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. H., Cardenal-Munoz, E., Cardenas, C., Cardenas, L., Cardoso, S. M., Carew, J. S., Carle, G. F., Carleton, G., Carloni, S., Carmona-Gutierrez, D., Carneiro, L. A., Carnevali, O., Carosi, J. M., Carra, S., Carrier, A., Carrier, L., Carroll, B., Carter, A. B., Carvalho, A. N., Casanova, M., Casas, C., Casas, J., Cassioli, C., Castillo, E. F., Castillo, K., Castillo-Lluva, S., Castoldi, F., Castori, M., Castro, A. F., Castro-Caldas, M., Castro-Hernandez, J., Castro-Obregon, S., Catz, S. D., Cavadas, C., Cavaliere, F., Cavallini, G., Cavinato, M., Cayuela, M. L., Cebollada Rica, P., Cecarini, V., Cecconi, F., Cechowska-Pasko, M., Cenci, S., Ceperuelo-Mallafre, V., Cerqueira, J. J., Cerutti, J. M., Cervia, D., Cetintas, V. B., Cetrullo, S., Chae, H. -J., Chagin, A. S., Chai, C. -Y., Chakrabarti, G., Chakrabarti, O., Chakraborty, T., Chami, M., Chamilos, G., Chan, D. W., Chan, E. Y. W., Chan, E. D., Chan, H. Y. E., Chan, H. H., Chan, H., Chan, M. T. V., Chan, Y. S., Chandra, P. 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. 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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. 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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. Therapeutic targeting of the NRF2 and KEAP1 partnership in chronic diseases

Author: Attucks Otis Clinton, John D. Hayes, Geoffrey Wells, Anna-Liisa Levonen, Thomas W. Kensler, Albena T. Dinkova-Kostova, Sharon P. Cousin, Ana I. Rojo, Stephen Franklin, Antonio Cuadrado, William L. Rumsey, Ministerio de Economía y Competitividad (España), National Institutes of Health (US), Cancer Research UK, European Commission, Biotechnology and Biological Sciences Research Council (UK), Medical Research Council (UK), Tenovus Scotland, and Sigrid Juselius Foundation
Subjects: 0301 basic medicine, NF-E2-Related Factor 2, education, Inflammation, Bioinformatics, Activation, Metabolic, 03 medical and health sciences, 0302 clinical medicine, Drug Therapy, Drug Discovery, Animals, Humans, Medicine, Transcription factor, health care economics and organizations, Pharmacology, Kelch-Like ECH-Associated Protein 1, biology, business.industry, Activator (genetics), General Medicine, respiratory system, Cytoprotection, KEAP1, NFE2L2, Ubiquitin ligase, 030104 developmental biology, 030220 oncology & carcinogenesis, biology.protein, medicine.symptom, business
Abstract: The transcription factor NF-E2 p45-related factor 2 (NRF2; encoded by NFE2L2) and its principal negative regulator, the E3 ligase adaptor Kelch-like ECH-associated protein 1 (KEAP1), are critical in the maintenance of redox, metabolic and protein homeostasis, as well as the regulation of inflammation. Thus, NRF2 activation provides cytoprotection against numerous pathologies including chronic diseases of the lung and liver; autoimmune, neurodegenerative and metabolic disorders; and cancer initiation. One NRF2 activator has received clinical approval and several electrophilic modifiers of the cysteine-based sensor KEAP1 and inhibitors of its interaction with NRF2 are now in clinical development. However, challenges regarding target specificity, pharmacodynamic properties, efficacy and safety remain., This work was supported by grants SAF2015-71304-REDT and SAF2016-76520-R from the Spanish Ministry Economy and Competitiveness; P_37_732/2016 REDBRAIN from the European Regional Development Fund; Competitiveness Operational Program 2014–2020; US National Institutes of Health grant R35 CA197222; Cancer Research UK grant C20953/A18644; Medical Research Council grant MR/N009851/1; Biotechnology and Biological Sciences Research Council grant BB/L01923X/1; Tenovus Scotland grant T17/14; and grant 275147 from the Academy of Finland, Sigrid Juselius Foundation and Finnish Cancer Foundation.
Published: 2019

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

Author: Klionsky, Daniel J, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie H, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis E, Adeli, Khosrow, Adolph, Timon E, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat B, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed N, Agrotis, Alexander, Aguilar, Patricia V, Ahmad, S Tariq, Ahmed, Zubair M, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed M, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay A, 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 D, Altan-Bonnet, Nihal, Altieri, Dario C, Álvarez, Élida MC, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen M, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal O, Ammanathan, Veena, An, Zhenyi, Andersen, Stig U, Andrabi, Shaida A, Andrade-Silva, Magaiver, Andres, Allen M, Angelini, Sabrina, Ann, David, Anozie, Uche C, Ansari, Mohammad Y, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner L, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela S, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas G, Au, Alicia K, Auberger, Patrick, Auner, Holger W, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, 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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 M, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry B, 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 C, Stallings, Christina L, and Tong, Chun-Kit
Subjects: phagophore, vacuole, Autophagosome, neurodegeneration, Autophagosomes, Autophagy-Related Proteins, flux, macroautophagy, stress, LC3, lysosome, Autophagy, cancer, Animals, Humans, Biological Assay, Lysosomes, Biomarkers
Abstract: 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
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14. The Cell-Permeable Derivative of the Immunoregulatory Metabolite Itaconate, 4-Octyl Itaconate, Is Anti-Fibrotic in Systemic Sclerosis

Author: Steven O′Reilly, Albena T. Dinkova-Kostova, John Henderson, Sharadha Dayalan Naidu, Stefan Przyborski, and Richard Stratton
Subjects: QH301-705.5, systemic sclerosis, NF-E2-Related Factor 2, medicine.medical_treatment, Down-Regulation, Article, Nrf2, Transforming Growth Factor beta1, Mice, Downregulation and upregulation, Fibrosis, medicine, NAD(P)H Dehydrogenase (Quinone), Animals, Humans, Biology (General), Interleukin 6, chemistry.chemical_classification, Mice, Knockout, Reactive oxygen species, Scleroderma, Systemic, biology, integumentary system, Interleukin-6, fibrosis, Connective Tissue Growth Factor, Succinates, General Medicine, Transforming growth factor beta, Fibroblasts, medicine.disease, C700, Connective tissue disease, Molecular biology, Antioxidant Response Elements, Up-Regulation, Heme oxygenase, MicroRNAs, Cytokine, chemistry, itaconate, biology.protein, metabolism, Collagen, Reactive Oxygen Species, Heme Oxygenase-1
Abstract: Systemic sclerosis (SSc) is an autoimmune connective tissue disease that leads to skin fibrosis. Altered metabolism has recently been described in autoimmune diseases and SSc. Itaconate is a product of the Krebs cycle intermediate cis-aconitate and is an immunomodulator. This work examines the role of the cell-permeable derivative of itaconate, 4-octyl itaconate (4-OI), in SSc. SSc and healthy dermal fibroblasts were exposed to 4-OI. The levels of collagen Nrf2-target genes and pro-inflammatory cytokines interleukin 6 (IL-6) and monocyte chemotactic protein 1 (MCP-1) were determined. Levels of reactive oxygen species (ROS) as well as the gene expression of collagen and Cellular Communication Network Factor 2 (CCN2) were measured after transforming growth factor beta 1 (TGF-β1) stimulation in the presence or absence of 4-OI. Wild-type or Nrf2-knockout (Nrf2-KO) mouse embryonic fibroblasts (MEFs) were also treated with 4-OI to determine the role of Nrf2 in 4-OI-mediated effects. 4-OI reduced the levels of collagen in SSc dermal fibroblasts. Incubation with 4-OI led to activation of Nrf2 and its target genes heme oxygenase 1 (HO-1) and NAD(P)H quinone oxidoreductase 1 (NQO1). 4-OI activated antioxidant response element (ARE)-dependent gene expression, reduced inflammatory cytokine release and reduced TGF-β1-induced collagen and ROS production in dermal fibroblasts. The effects of 4-OI are dependent on Nrf2. The cell-permeable derivative of itaconate 4-OI is anti-fibrotic through upregulation of Nrf2 and could be a potential therapeutic option in an intractable disease.
Published: 2021

15. Clinically relevant aberrant Filip1l DNA methylation detected in a murine model of cutaneous squamous cell carcinoma

Author: Tim De Meyer, Louis Coussement, Maureen Higgins, Elena V. Knatko, Albena T. Dinkova-Kostova, Sandra Steyaert, Charlotte M. Proby, and Kevin Roth
Subjects: 5mC, 5-methylcytosine, 0301 basic medicine, Medicine (General), DOWN-REGULATION, Research paper, Skin Neoplasms, NHK, normal human keratinocyte, Bisulfite sequencing, iHS, independent healthy skin, Mice, chemistry.chemical_compound, 0302 clinical medicine, DS, dorsal skin, Medicine and Health Sciences, Filip1l, Filament A interacting protein 1-like, iso, isoform, 5hmC, 5-hydroxymethylcytosine, cSCC, cutaneous squamous cell carcinoma, DNA methylation, CARCINOGENESIS, DMR, differentially methylated region, General Medicine, Methylation, Gene Expression Regulation, Neoplastic, 5-Methylcytosine, CpG site, 030220 oncology & carcinogenesis, Carcinoma, Squamous Cell, CGI, CpG island, Medicine, cSCC, INTERACTING PROTEIN 1-LIKE, EXPRESSION, NMSC, non-melanoma skin cancer, INHIBITION, Down-Regulation, CpG, 5′-Cytosinephosphate-Guanine-3′, Biology, FILIP1L, General Biochemistry, Genetics and Molecular Biology, UVR, Ultraviolet radiation, 03 medical and health sciences, Tet, Ten-eleven-translocase, R5-920, Cell Line, Tumor, BENEFITS, Animals, Humans, Gene, 5-Hydroxymethylcytosine, VS, ventral skin, RRBS, SKIN-CANCER, LANDSCAPE, MUTATIONS, Promoter, (ox)RRBS, (oxidative) reduced representation bisulfite sequencing, ssUV mcSCC, solar simulated mouse cSCC, AK, actinic keratosis, Cytoskeletal Proteins, 030104 developmental biology, chemistry, Cancer research, RADIATION, Carrier Proteins
Abstract: Background Cutaneous squamous cell carcinomas (cSCC) are among the most common and highly mutated human malignancies. Understanding the impact of DNA methylation in cSCC may provide avenues for new therapeutic strategies. Methods We used reduced-representation bisulfite sequencing for DNA methylation analysis of murine cSCC. Differential methylation was assessed at the CpG level using limma. Next, we compared with human cSCC Infinium HumanMethylation BeadArray data. Genes were considered to be of major relevance when they featured at least one significantly differentially methylated CpGs (RRBS) / probes (Infinium) with at least a 30% difference between tumour vs. control in both a murine gene and its human orthologue. The human EPIC Infinium data were used to distinguish two cSCC subtypes, stem-cell-like and keratinocyte-like tumours. Findings We found increased average methylation in mouse cSCC (by 12.8%, p = 0.0011) as well as in stem-cell like (by 3.1%, p=0.002), but not keratinocyte-like (0.2%, p = 0.98), human cSCC. Comparison of differentially methylated genes revealed striking similarities between human and mouse cSCC. Locus specific methylation changes in mouse cSCC often occurred in regions of potential regulatory function, including enhancers and promoters. A key differentially methylated region was located in a potential enhancer of the tumour suppressor gene Filip1l and its expression was reduced in mouse tumours. Moreover, the FILIP1L locus showed hypermethylation in human cSCC and lower expression in human cSCC cell lines. Interpretation Deregulation of DNA methylation is an important feature of murine and human cSCC that likely contributes to silencing of tumour suppressor genes, as shown for Filip1l. Funding British Skin Foundation, Cancer Research UK
Published: 2021

16. Assessment of ROS Production in the Mitochondria of Live Cells

Author: Plamena R, Angelova, Albena T, Dinkova-Kostova, and Andrey Y, Abramov
Subjects: Oxidative Stress, Free Radicals, Animals, Humans, Hydrogen Peroxide, Lipid Peroxidation, Reactive Oxygen Species, Models, Biological, Single Molecule Imaging, Mitochondria
Abstract: Production of reactive oxygen species (ROS) in the mitochondria plays multiple roles in physiology, and excessive production of ROS leads to the development of various pathologies. ROS in the mitochondria are generated by various enzymes, mainly in the electron transporvt chain, and it is important to identify not only the trigger but also the source of free radical production. It is important to measure mitochondrial ROS in live, intact cells, because activation of ROS production could be initiated by changes in extramitochondrial processes which could be overseen when using isolated mitochondria. Here we describe the approaches, which allow to measure production of ROS in the matrix of mitochondria in live cells. We also demonstrate how to measure kinetic changes in lipid peroxidation in mitochondria of live cells. These methods could be used for understanding the mechanisms of pathology in a variety of disease models and also for testing neuro- or cardioprotective chemicals.
Published: 2020

17. Isomeric O-methyl cannabidiolquinones with dual BACH1/NRF2 activity

Author: Eduardo Muñoz, Albena T. Dinkova-Kostova, María E. Prados, Giovanni Apendino, Laura Casares, Juan D. Unciti-Broceta, Maureen Higgins, Laureano de la Vega, Diego Caprioglio, and Daiana Mattoteia
Subjects: Antioxidant, NF-E2-Related Factor 2, medicine.medical_treatment, Short Communication, Clinical Biochemistry, Inflammation, Pharmacology, medicine.disease_cause, Biochemistry, Neuroprotection, environment and public health, digestive system, Antioxidants, Cannabidiol derivative/ NRF2/ BACH1/ HMOX1/ neurodegenerative diseases, Cell Line, Mice, In vivo, medicine, Animals, lcsh:QH301-705.5, lcsh:R5-920, Chemistry, Multiple sclerosis, Organic Chemistry, Nrf2 activators, Neurodegenerative Diseases, respiratory system, medicine.disease, Disease Models, Animal, Oxidative Stress, Basic-Leucine Zipper Transcription Factors, lcsh:Biology (General), medicine.symptom, lcsh:Medicine (General), Cannabidiol, Oxidative stress, medicine.drug
Abstract: Oxidative stress and inflammation in the brain are two key hallmarks of neurodegenerative diseases (NDs) such as Alzheimer's, Parkinson's, Huntington's and multiple sclerosis. The axis NRF2-BACH1 has anti-inflammatory and anti-oxidant properties that could be exploited pharmacologically to obtain neuroprotective effects. Activation of NRF2 or inhibition of BACH1 are, individually, promising therapeutic approaches for NDs. Compounds with dual activity as NRF2 activators and BACH1 inhibitors, could therefore potentially provide a more robust antioxidant and anti-inflammatory effects, with an overall better neuroprotective outcome. The phytocannabinoid cannabidiol (CBD) inhibits BACH1 but lacks significant NRF2 activating properties. Based on this scaffold, we have developed a novel CBD derivative that is highly effective at both inhibiting BACH1 and activating NRF2. This new CBD derivative provides neuroprotection in cell models of relevance to Huntington's disease, setting the basis for further developments in vivo.
Published: 2020

18. Radiomodulatory effect of a non-electrophilic NQO1 inducer identified in a screen of new 6, 8-diiodoquinazolin-4(3H)-ones carrying a sulfonamide moiety

Author: Albena T. Dinkova-Kostova, Aiten M. Soliman, Mai H. Mekkawy, Mostafa M. Ghorab, Heba M. Karam, and Maureen Higgins
Subjects: Male, Antioxidant, Stereochemistry, medicine.medical_treatment, Thio, Sulfonamide, 01 natural sciences, Antioxidants, Article, Nrf2, Docking, 03 medical and health sciences, chemistry.chemical_compound, Mice, Structure-Activity Relationship, Drug Discovery, medicine, NAD(P)H Dehydrogenase (Quinone), Tumor Cells, Cultured, Moiety, Animals, Inducer, Quinazolinone, 030304 developmental biology, Quinazolinones, Diiodoquinazolinone, Pharmacology, chemistry.chemical_classification, 0303 health sciences, Sulfonamides, Dose-Response Relationship, Drug, Molecular Structure, 010405 organic chemistry, Organic Chemistry, General Medicine, 0104 chemical sciences, Molecular Docking Simulation, Enzyme, chemistry, Radiomodulatory, Docking (molecular), Oxidative stress, NQO1, Acetamide
Abstract: Fifteen new quinazolinone derivatives bearing benzenesulfonamide moiety with variable acetamide tail were synthesized. The structures assigned to the products were concordant with the microanalytical and spectral data. Compounds 4–18 were screened for their ability to induce the antioxidant enzyme NAD(P)H: quinone oxidoreductase 1 (NQO1) in cells, a classical target for transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2). The 2-((6,8-diiodo-4-oxo-3-(4-sulfamoylphenyl)-3,4-dihydroquinazolin-2-yl)thio)-N-(3,4,5-trimethoxyphenyl) acetamide 15 showed the most potent NQO1 inducer activity in vitro. Compound 15 had low toxicity in mice (LD50 = 500 mg/kg). It also reduced the damaging effects of gamma radiation, as assessed by the levels of Nrf2, NQO1, reactive oxygen species (ROS) and malondialdehyde (MDA) in liver tissues. In addition, compound 15 showed amelioration in the complete blood count of irradiated mice and enhanced survival over a period of 30 days following irradiation. Molecular docking of 15 inside the Nrf2-binding site of Kelch-like ECH associated protein 1 (Keap1), the main negative regulator of Nrf2, showed the same binding interactions as that of the co-crystallized ligand considering the binding possibilities and energy scores. These findings suggest that compound 15 could be considered as a promising antioxidant and radiomodulatory agent., Graphical abstract Image 1, Highlights • Novel 6,8-diiodoquinazolinone derivatives carrying sulfonamide moiety were synthetized. • Compounds 4-18 were assayed in vitro for their NQO1 inducer activity. • Acute toxicity of the most potent NQO1 inducer 15 was low in vivo (LD50 = 500 mg/kg). • Compound 15 inhibited oxidative stress and improved survival in irradiated mice. • Molecular docking showed interactions of 15 with the Nrf2-binding site of Keap1.
Published: 2020

19. Obesity and NRF2-mediated cytoprotection: Where is the missing link?

Author: Albena T. Dinkova-Kostova, Liliya V. Vasileva, Martina S. Savova, Milen I. Georgiev, and Kristiana M. Amirova
Subjects: 0301 basic medicine, medicine.medical_specialty, NF-E2-Related Factor 2, Population, Anti-Inflammatory Agents, Oxidative phosphorylation, medicine.disease_cause, Antioxidants, 03 medical and health sciences, 0302 clinical medicine, Insulin resistance, Internal medicine, medicine, Adipocytes, Animals, Humans, Obesity, education, Pharmacology, education.field_of_study, Adipogenesis, Kelch-Like ECH-Associated Protein 1, business.industry, medicine.disease, Cytoprotection, Antioxidant Response Elements, 3. Good health, Heme oxygenase, Oxidative Stress, 030104 developmental biology, Endocrinology, 030220 oncology & carcinogenesis, Anti-Obesity Agents, Metabolic syndrome, Steatohepatitis, Inflammation Mediators, business, Reactive Oxygen Species, Oxidative stress, Signal Transduction
Abstract: The expanding dimensions of the global health crisis of overweight population has defined the term "globesity". Among the most common pathological conditions connected with excessive adiposity are hyperglycemia, insulin resistance, dyslipidemia and hypertension which result in chronic non-communicable diseases (NCD) such as metabolic syndrome (MetS), type 2 diabetes (T2D), and nonalchoholic steatohepatitis (NASH). The contribution of inflammatory-immune reactions in obesity and its related co-morbidities is unequivocal. Increased levels of free fatty acids (FFA), reactive oxygen species (ROS) and reactive nitrogen species (RNS) overloads the homeostatic system resulting in pro-inflammatory adipokines secretion, immune-activation and chronic inflammation in obesity. The cellular mechanisms of defense against oxidative stress are orchestrated by the transcription factor nuclear factor erythroid 2 p45-related factor 2 (NRF2). Excessive oxidative stress in the cell activates NRF2 which upregulates genes encoding major cytoprotective enzymes such as NAD(P)H:quinone oxidoreductase 1 (NQO1), heme oxygenase 1 (HO1), and glutathione S-transferases (GST). The present review aims to clarify the interconnections between chronic inflammation, oxidative overload and NRF2-mediated cytoprotection as potential therapeutic approach in obesity.
Published: 2020

20. C151 in KEAP1 is the main cysteine sensor for the cyanoenone class of NRF2 activators, irrespective of molecular size or shape

Author: Dayalan Naidu, Sharadha, Muramatsu, Aki, Saito, Ryota, Asami, Soichiro, Honda, Tadashi, Hosoya, Tomonori, Itoh, Ken, Yamamoto, Masayuki, Suzuki, Takafumi, and Dinkova-Kostova, Albena T.
Subjects: Male, Mice, Knockout, Transcriptional Activation, Kelch-Like ECH-Associated Protein 1, NF-E2-Related Factor 2, lcsh:R, lcsh:Medicine, Mice, Transgenic, Fibroblasts, Phenanthrenes, respiratory system, Embryo, Mammalian, environment and public health, Article, Up-Regulation, Mice, Macrophages, Peritoneal, Animals, Female, lcsh:Q, Cysteine, lcsh:Science, Cells, Cultured
Abstract: Numerous small molecules (termed inducers), many of which are electrophiles, upregulate cytoprotective responses and inhibit pro-inflammatory pathways by activating nuclear factor-erythroid 2 p45-related factor 2 (NRF2). Key to NRF2 activation is the ability to chemically modifying critical sensor cysteines in the main negative regulator of NRF2, Kelch-like ECH-associated protein 1 (KEAP1), of which C151, C273 and C288 are best characterized. This study aimed to establish the requirement for these cysteine sensor(s) for the biological activities of the most potent NRF2 activators known to date, the cyclic cyanoenones, some of which are in clinical trials. It was found that C151 in KEAP1 is the main cysteine sensor for this class of inducers, irrespective of molecular size or shape. Furthermore, in primary macrophage cells expressing C151S mutant KEAP1, at low concentrations, the tricyclic cyanoenone TBE-31 is inactive as an activator of NRF2 as well as an inhibitor of lipopolysaccharide-stimulated gene expression of the pro-inflammatory cytokines IL6 and IL1β. However, at high inducer concentrations, NRF2 activation proceeds in the absence of C151, albeit at a lower magnitude. Our findings highlight the intrinsic flexibility of KEAP1 and emphasize the critical importance of establishing the precise dose of NRF2 activators for maintaining on-target selectivity.
Published: 2018

21. KEAP1 inhibition is neuroprotective and suppresses the development of epilepsy

Author: Stjepana Kovac, Sharadha Dayalan Naidu, Andrey Y. Abramov, Ramona Eckel, Tawfeeq Shekh-Ahmad, Maureen Higgins, Masayuki Yamamoto, Matthew C. Walker, and Albena T. Dinkova-Kostova
Subjects: Male, 0301 basic medicine, Mice, Transgenic, Status epilepticus, Mitochondrion, Pharmacology, medicine.disease_cause, Epileptogenesis, Neuroprotection, Rats, Sprague-Dawley, 03 medical and health sciences, Epilepsy, 0302 clinical medicine, Excitatory Amino Acid Agonists, medicine, Animals, Cells, Cultured, Cerebral Cortex, Membrane Potential, Mitochondrial, Neurons, chemistry.chemical_classification, Hippocampal sclerosis, Reactive oxygen species, Kainic Acid, Kelch-Like ECH-Associated Protein 1, medicine.disease, Glutathione, Triterpenes, Rats, Disease Models, Animal, Oxidative Stress, 030104 developmental biology, Animals, Newborn, Gene Expression Regulation, chemistry, Mutation, Anticonvulsants, Neurology (clinical), medicine.symptom, Neuroglia, 030217 neurology & neurosurgery, Oxidative stress
Abstract: Hippocampal sclerosis is a common acquired disease that is a major cause of drug-resistant epilepsy. A mechanism that has been proposed to lead from brain insult to hippocampal sclerosis is the excessive generation of reactive oxygen species, and consequent mitochondrial failure. Here we use a novel strategy to increase endogenous antioxidant defences using RTA 408, which we show activates nuclear factor erythroid 2-related factor 2 (Nrf2, encoded by NFE2L2) through inhibition of kelch like ECH associated protein 1 (KEAP1) through its primary sensor C151. Activation of Nrf2 with RTA 408 inhibited reactive oxygen species production, mitochondrial depolarization and cell death in an in vitro model of seizure-like activity. RTA 408 given after status epilepticus in vivo increased ATP, prevented neuronal death, and dramatically reduced (by 94%) the frequency of late spontaneous seizures for at least 4 months following status epilepticus. Thus, acute KEAP1 inhibition following status epilepticus exerts a neuroprotective and disease-modifying effect, supporting the hypothesis that reactive oxygen species generation is a key event in the development of epilepsy.
Published: 2018

22. The role of Nrf2 signaling in counteracting neurodegenerative diseases

Author: Dinkova‐Kostova, Albena T., Kostov, Rumen V., and Kazantsev, Aleksey G.
Subjects: Nrf2 activator, NF-E2-Related Factor 2, neurodegeneration, Neurodegenerative Diseases, Review Article, respiratory system, environment and public health, neuroinflammation, Oxidative Stress, Animals, Humans, neuroprotection, Molecular Targeted Therapy, Review Articles, Signal Transduction
Abstract: The transcription factor Nrf2 (nuclear factor-erythroid 2 p45-related factor 2) functions at the interface of cellular redox and intermediary metabolism. Nrf2 target genes encode antioxidant enzymes, and proteins involved in xenobiotic detoxification, repair and removal of damaged proteins and organelles, inflammation, and mitochondrial bioenergetics. The function of Nrf2 is altered in many neurodegenerative disorders, such as Huntington's disease, Alzheimer's disease, amyotrophic lateral sclerosis, and Friedreich's ataxia. Nrf2 activation mitigates multiple pathogenic processes involved in these neurodegenerative disorders through upregulation of antioxidant defenses, inhibition of inflammation, improvement of mitochondrial function, and maintenance of protein homeostasis. Small molecule pharmacological activators of Nrf2 have shown protective effects in numerous animal models of neurodegenerative diseases, and in cultures of human cells expressing mutant proteins. Targeting Nrf2 signaling may provide a therapeutic option to delay onset, slow progression, and ameliorate symptoms of neurodegenerative disorders.
Published: 2018

23. Transcription factors NRF2 and HSF1 have opposing functions in autophagy

Author: Dayalan Naidu, Sharadha, Dikovskaya, Dina, Gaurilcikaite, Egle, Knatko, Elena V., Healy, Zachary R., Mohan, Hema, Koh, Glenn, Laurell, Axel, Ball, Graeme, Olagnier, David, de la Vega, Laureano, Ganley, Ian G., Talalay, Paul, and Dinkova-Kostova, Albena T.
Subjects: Osteoblasts, Skin Neoplasms, NF-E2-Related Factor 2, lcsh:R, lcsh:Medicine, Neoplasms, Experimental, Article, Cell Line, Mice, Gene Expression Regulation, Heat Shock Transcription Factors, Autophagy, Animals, Humans, lcsh:Q, lcsh:Science
Abstract: Autophagy plays a critical role in the maintenance of cellular homeostasis by degrading proteins, lipids and organelles. Autophagy is activated in response to stress, but its regulation in the context of other stress response pathways, such as those mediated by heat shock factor 1 (HSF1) and nuclear factor-erythroid 2 p45-related factor 2 (NRF2), is not well understood. We found that the Michael acceptor bis(2-hydoxybenzylidene)acetone (HBB2), a dual activator of NRF2 and HSF1, protects against the development of UV irradiation-mediated cutaneous squamous cell carcinoma in mice. We further show that HBB2 is an inducer of autophagy. In cells, HBB2 increases the levels of the autophagy-cargo protein p62/sequestosome 1, and the lipidated form of microtubule-associated protein light chain 3 isoform B. Activation of autophagy by HBB2 is impaired in NRF2-deficient cells, which have reduced autophagic flux and low basal and induced levels of p62. Conversely, HSF1-deficient cells have increased autophagic flux under both basal as well as HBB2-induced conditions, accompanied by increased p62 levels. Our findings suggest that NRF2 and HSF1 have opposing roles during autophagy, and illustrate the existence of tight mechanistic links between the cellular stress responses.
Published: 2017

24. Crosstalk between NRF2 and HIPK2 shapes cytoprotective responses

Author: Torrente, L, Sanchez, C, Moreno, R, Chowdhry, S, Cabello, P, Isono, K, Koseki, H, Honda, T, Hayes, J D, Dinkova-Kostova, A T, and de la Vega, L
Subjects: Binding Sites, Lung Neoplasms, NF-E2-Related Factor 2, Short Communication, Apoptosis, respiratory system, Protein Serine-Threonine Kinases, environment and public health, Xenograft Model Antitumor Assays, Mice, A549 Cells, Doxorubicin, Drug Resistance, Neoplasm, Animals, Humans, Carrier Proteins, Cell Proliferation, Protein Binding, Signal Transduction
Abstract: Homeodomain interacting protein kinase-2 (HIPK2) is a member of the HIPK family of stress-responsive kinases that modulates cell growth, apoptosis, proliferation and development. HIPK2 has several well-characterised tumour suppressor roles, but recent studies suggest it can also contribute to tumour progression, although the underlying mechanisms are unknown. Herein, we have identified novel crosstalk between HIPK2 and the cytoprotective transcription factor NRF2. We show that HIPK2 is a direct transcriptional target of NRF2, identifying a functional NRF2 binding site in the HIPK2 gene locus and demonstrating for the first time a transcriptional mode of regulation for this kinase. In addition, HIPK2 is required for robust NRF2 responsiveness in cells and in vivo. By using both gain-of-function and loss-of-function approaches, we demonstrate that HIPK2 can elicit a cytoprotective response in cancer cells via NRF2. Our results have uncovered a new downstream effector of HIPK2, NRF2, which is frequently activated in human tumours correlating with chemoresistance and poor prognosis. Furthermore, our results suggest that modulation of either HIPK2 levels or activity could be exploited to impair NRF2-mediated signalling in cancer cells, and thus sensitise them to chemotherapeutic drugs.
Published: 2017

25. Activation of Nrf2 Signaling Augments Vesicular Stomatitis Virus Oncolysis via Autophagy-Driven Suppression of Antiviral Immunity

Author: Olagnier, David, Lababidi, Rassin R., Hadj, Samar Bel, Sze, Alexandre, Liu, Yiliu, Naidu, Sharadha Dayalan, Ferrari, Matteo, Jiang, Yuan, Chiang, Cindy, Beljanski, Vladimir, Goulet, Marie-Line, Knatko, Elena V., Dinkova-Kostova, Albena T., Hiscott, John, and Lin, Rongtuan
Subjects: autophagy, innate antiviral response, NF-E2-Related Factor 2, Antineoplastic Agents, Virus Replication, Nrf2, Antioxidants, Vesicular stomatitis Indiana virus, Cell Line, Viral Matrix Proteins, Mice, Isothiocyanates, Neoplasms, cancer, Animals, Humans, Sequence Deletion, Mice, Knockout, Oncolytic Virotherapy, oncolysis, Immunity, interferon, respiratory system, Combined Modality Therapy, Immunity, Innate, Disease Models, Animal, Oncolytic Viruses, VSV, Sulfoxides, Host-Pathogen Interactions, Original Article, Vesicular Stomatitis, Signal Transduction
Abstract: Oncolytic viruses (OVs) offer a promising therapeutic approach to treat multiple types of cancer. In this study, we show that the manipulation of the antioxidant network via transcription factor Nrf2 augments vesicular stomatitis virus Δ51 (VSVΔ51) replication and sensitizes cancer cells to viral oncolysis. Activation of Nrf2 signaling by the antioxidant compound sulforaphane (SFN) leads to enhanced VSVΔ51 spread in OV-resistant cancer cells and improves the therapeutic outcome in different murine syngeneic and xenograft tumor models. Chemoresistant A549 lung cancer cells that display constitutive dominant hyperactivation of Nrf2 signaling are particularly vulnerable to VSVΔ51 oncolysis. Mechanistically, enhanced Nrf2 signaling stimulated viral replication in cancer cells and disrupted the type I IFN response via increased autophagy. This study reveals a previously unappreciated role for Nrf2 in the regulation of autophagy and the innate antiviral response that complements the therapeutic potential of VSV-directed oncolysis against multiple types of OV-resistant or chemoresistant cancer., Graphical Abstract, Oncolytic viruses offer a promising therapeutic approach to treat cancer. In this issue, Olagnier et al. demonstrate that the antioxidant compound sulforaphane activates the transcriptional regulator Nrf2, leading to suppression of the innate antiviral response, stimulation of autophagy, and enhancement of vesicular stomatitis virus-directed oncolysis of tumor cells.
Published: 2017

26. Activation of Nrf2 signaling as a common treatment of neurodegenerative diseases

Author: Albena T. Dinkova-Kostova and Aleksey G. Kazantsev
Subjects: 0301 basic medicine, Aging, NF-E2-Related Factor 2, business.industry, Neurodegenerative Diseases, medicine.disease_cause, Neuroprotection, 03 medical and health sciences, 030104 developmental biology, Animals, Humans, Medicine, Neurology (clinical), business, Neuroscience, Oxidative stress, Neuroinflammation, Nrf2 signaling
Published: 2017

27. Regulation of the mammalian heat shock factor 1

Author: Albena T. Dinkova-Kostova and Sharadha Dayalan Naidu
Subjects: Models, Molecular, 0301 basic medicine, Proteasome Endopeptidase Complex, Protein Folding, Hot Temperature, Transcription, Genetic, Protein Conformation, SUMO protein, Biology, Biochemistry, 03 medical and health sciences, Heat Shock Transcription Factors, Stress, Physiological, Heat shock protein, Animals, Phosphorylation, HSF1, Molecular Biology, Transcription factor, Phylogeny, Mammals, Sumoylation, Acetylation, Cell Biology, Adaptation, Physiological, Cell biology, DNA-Binding Proteins, 030104 developmental biology, Gene Expression Regulation, Chaperone complex, Protein folding, Protein Processing, Post-Translational, Transcription Factors
Abstract: Living organisms are endowed with the capability to tackle various forms of cellular stress due to the presence of molecular chaperone machinery complexes that are ubiquitous throughout the cell. During conditions of proteotoxic stress, the transcription factor heat shock factor 1 (HSF1) mediates the elevation of heat shock proteins, which are crucial components of the chaperone complex machinery and function to ameliorate protein misfolding and aggregation and restore protein homeostasis. In addition, HSF1 orchestrates a versatile transcriptional programme that includes genes involved in repair and clearance of damaged macromolecules and maintenance of cell structure and metabolism, and provides protection against a broad range of cellular stress mediators, beyond heat shock. Here, we discuss the structure and function of the mammalian HSF1 and its regulation by post-translational modifications (phosphorylation, sumoylation and acetylation), proteasomal degradation, and small-molecule activators and inhibitors.
Published: 2017

28. Broccoli or Sulforaphane: Is It the Source or Dose That Matters?

Author: Jed W. Fahey, Yoko Yagishita, Thomas W. Kensler, and Albena T. Dinkova-Kostova
Subjects: 0301 basic medicine, Pharmaceutical Science, sulforaphane, Disease, Review, Bioinformatics, Analytical Chemistry, chemistry.chemical_compound, 0302 clinical medicine, Anti-Infective Agents, Isothiocyanates, Drug Discovery, Medicine, nrf2, Glucoraphanin, Clinical Trials as Topic, Molecular Structure, 3. Good health, Chemistry (miscellaneous), 030220 oncology & carcinogenesis, Sulfoxides, Chemoprotective, Molecular Medicine, allometric scaling, chemoprotection, Brassica, lcsh:QD241-441, 03 medical and health sciences, lcsh:Organic chemistry, Biomarkers, Tumor, Animals, Humans, Microbiome, Physical and Theoretical Chemistry, broccoli, clinical trials, business.industry, Plant Extracts, glucoraphanin, Organic Chemistry, myrosinase, toxicity, Antineoplastic Agents, Phytogenic, Bioavailability, Clinical trial, 030104 developmental biology, chemistry, Isothiocyanate, business, Sulforaphane
Abstract: There is robust epidemiological evidence for the beneficial effects of broccoli consumption on health, many of them clearly mediated by the isothiocyanate sulforaphane. Present in the plant as its precursor, glucoraphanin, sulforaphane is formed through the actions of myrosinase, a β-thioglucosidase present in either the plant tissue or the mammalian microbiome. Since first isolated from broccoli and demonstrated to have cancer chemoprotective properties in rats in the early 1990s, over 3000 publications have described its efficacy in rodent disease models, underlying mechanisms of action or, to date, over 50 clinical trials examining pharmacokinetics, pharmacodynamics and disease mitigation. This review evaluates the current state of knowledge regarding the relationships between formulation (e.g., plants, sprouts, beverages, supplements), bioavailability and efficacy, and the doses of glucoraphanin and/or sulforaphane that have been used in pre-clinical and clinical studies. We pay special attention to the challenges for better integration of animal model and clinical studies, particularly with regard to selection of dose and route of administration. More effort is required to elucidate underlying mechanisms of action and to develop and validate biomarkers of pharmacodynamic action in humans. A sobering lesson is that changes in approach will be required to implement a public health paradigm for dispensing benefit across all spectrums of the global population.
Published: 2019

29. Investigation into the use of histone deacetylase inhibitor MS-275 as a topical agent for the prevention and treatment of cutaneous squamous cell carcinoma in an SKH-1 hairless mouse model

Author: W. David Holtzclaw, Jay H. Kalin, Abdulkerim Eroglu, Albena T. Dinkova-Kostova, Hua Liu, Charlotte M. Proby, Irene M. Leigh, Jed W. Fahey, and Philip A. Cole
Subjects: Neoplasms, Radiation-Induced, Skin Neoplasms, Light, Carcinogenesis, Pyridines, Administration, Topical, Cell, Cancer Treatment, Gene Expression, medicine.disease_cause, Biochemistry, Histones, 030207 dermatology & venereal diseases, Mice, 0302 clinical medicine, Medicine and Health Sciences, Post-Translational Modification, Multidisciplinary, integumentary system, Chromosome Biology, Physics, Chromatin Modification, Histone deacetylase inhibitor, Chemical Reactions, Squamous Cell Carcinomas, Acetylation, Histone Modification, Animal Models, Chromatin, 3. Good health, Tumor Burden, Physical sciences, Gene Expression Regulation, Neoplastic, Chemistry, medicine.anatomical_structure, Oncology, Experimental Organism Systems, 030220 oncology & carcinogenesis, Benzamides, Carcinoma, Squamous Cell, Medicine, Epigenetics, Keratinocyte, Research Article, Ultraviolet radiation, Cyclin-Dependent Kinase Inhibitor p21, medicine.drug_class, Cell Survival, Science, Histone Acetylation, Mouse Models, Research and Analysis Methods, Carcinomas, 03 medical and health sciences, Model Organisms, Electromagnetic radiation, Cell Line, Tumor, DNA-binding proteins, Carcinoma, medicine, Genetics, Animals, Humans, Cell Proliferation, Mice, Hairless, Biology and life sciences, business.industry, Proteins, Cancers and Neoplasms, Cell Biology, medicine.disease, Xenograft Model Antitumor Assays, Hairless, Histone Deacetylase Inhibitors, Cancer research, Animal Studies, Histone deacetylase, business, Ultraviolet B
Abstract: Cutaneous squamous cell carcinomas are a common form of highly mutated keratinocyte skin cancers that are of particular concern in immunocompromised patients. Here we report on the efficacy of topically applied MS-275, a clinically used histone deacetylase inhibitor, for the treatment and management of this disease. At 2 mg/kg, MS-275 significantly decreased tumor burden in an SKH-1 hairless mouse model of UVB radiation-induced skin carcinogenesis. MS-275 was cell permeable as a topical formulation and induced histone acetylation changes in mouse tumor tissue. MS-275 was also effective at inhibiting the proliferation of patient derived cutaneous squamous cell carcinoma lines and was particularly potent toward cells isolated from a regional metastasis on an immunocompromised individual. Our findings support the use of alternative routes of administration for histone deacetylase inhibitors in the treatment of high-risk squamous cell carcinoma which may ultimately lead to more precise delivery and reduced systemic toxicity.
Published: 2019

30. Application of the in vivo oxidative stress reporter Hmox1 as mechanistic biomarker of arsenic toxicity

Author: Colin J. Henderson, C. Roland Wolf, Panida Navasumrit, Francisco Inesta-Vaquera, Albena T. Dinkova-Kostova, Tanya G. Frangova, Tadashi Honda, and Mathuros Ruchirawat
Subjects: HMOX1, 010504 meteorology & atmospheric sciences, DNA damage, Health, Toxicology and Mutagenesis, Inflammation, 010501 environmental sciences, Toxicology, medicine.disease_cause, 01 natural sciences, Antioxidants, Arsenic, Mice, Arsenic Poisoning, medicine, Animals, Transcription factor, 0105 earth and related environmental sciences, Arsenic toxicity, business.industry, Membrane Proteins, General Medicine, Pollution, Oxidative Stress, Toxicity, Cancer research, Biomarker (medicine), medicine.symptom, business, Biomarkers, Heme Oxygenase-1, Oxidative stress
Abstract: Inorganic arsenic (iAs) is a naturally occurring metalloid present in drinking water and polluted air exposing millions of people globally. Epidemiological studies have linked iAs exposure to the development of numerous diseases including cognitive impairment, cardiovascular failure and cancer. Despite intense research, an effective therapy for chronic arsenicosis has yet to be developed. Laboratory studies have been of great benefit in establishing the pathways involved in iAs toxicity and providing insights into its mechanism of action. However, the in vivo analysis of arsenic toxicity mechanisms has been difficult by the lack of reliable in vivo biomarkers of iAs’s effects. To address this issue we have applied the use of our recently developed stress reporter models to study iAs toxicity. The reporter mice Hmox1 (oxidative stress/inflammation; HOTT) and p21 (DNA damage) were exposed to iAs at acute and chronic, environmentally relevant, doses. We observed induction of the oxidative stress reporters in several cell types and tissues, which was largely dependent on the activation of transcription factor NRF2. We propose that our HOTT reporter model can be used as a surrogate biomarker of iAs-induced oxidative stress, and it constitutes a first-in-class platform to develop treatments aimed to counteract the role of oxidative stress in arsenicosis. Indeed, in a proof of concept experiment, the HOTT reporter mice were able to predict the therapeutic utility of the antioxidant N-acetyl cysteine in the prevention of iAs associated toxicity.
Published: 2021

31. The isothiocyanate sulforaphane inhibits mTOR in an NRF2-independent manner

Author: Albena T. Dinkova-Kostova, Amy Gilmour, Ying Zhang, Laureano de la Vega, and Young Hoon Ahn
Subjects: NF-E2-Related Factor 2, Pharmaceutical Science, Cellular homeostasis, KEAP1, Kelch-like ECH-associated protein 1, NRF2, nuclear factor erythroid 2 p45-related factor 2, HDAC, histone deacetylase, BITC, benzyl isothiocyanate, NRF2, 03 medical and health sciences, chemistry.chemical_compound, Phosphatidylinositol 3-Kinases, 0302 clinical medicine, Isothiocyanates, Cell Line, Tumor, Drug Discovery, Animals, Humans, Kinase activity, AMPK, 5′-AMP-activated protein kinase, PI3K-AKT, phosphatidylinositol 3-kinase-AKT/protein kinase B, Phosphorylation, Protein kinase A, Protein kinase B, Mechanistic target of rapamycin, PI3K/AKT/mTOR pathway, 030304 developmental biology, SFN, sulforaphane, Pharmacology, 0303 health sciences, biology, NRF2, nuclear factor erythroid 2 p45-related factor 2, Chemistry, PI3K-AKT, mTOR, mechanistic target of rapamycin, TOR Serine-Threonine Kinases, HDAC6, Cell biology, Complementary and alternative medicine, 030220 oncology & carcinogenesis, Sulfoxides, biology.protein, mTOR, Molecular Medicine, Original Article, Sulforaphane, CBHA, m-carboxycinnamic acid bis-hydroxamide, Proto-Oncogene Proteins c-akt
Abstract: Background The isothiocyanate sulforaphane (SFN) has multiple protein targets in mammalian cells, affecting processes of fundamental importance for the maintenance of cellular homeostasis, among which are those regulated by the stress response transcription factor nuclear factor erythroid 2 p45-related factor 2 (NRF2) and the serine/threonine protein kinase mechanistic target of rapamycin (mTOR). Whereas the way by which SFN activates NRF2 is well established, the molecular mechanism(s) of how SFN inhibits mTOR is not understood. Hypothesis/Purpose The aim of this study was to investigate the mechanism(s) by which SFN inhibits mTOR Study design and methods We used the human osteosarcoma cell line U2OS and its CRISPR/Cas9-generated NRF2-knockout counterpart to test the requirement for NRF2 and the involvement of mTOR regulators in the SFN-mediated inhibition of mTOR. Results SFN inhibits mTOR in a concentration- and time-dependent manner, and this inhibition occurs in the presence or in the absence of NRF2. The phosphatidylinositol 3-kinase (PI3K)-AKT/protein kinase B (PKB) is a positive regulator of mTOR, and treatment with SFN caused an increase in the phosphorylation of AKT at T308 and S473, two phosphorylation sites associated with AKT activation. Interestingly however, the levels of pS552 β-catenin, an AKT phosphorylation site, were decreased, suggesting that the catalytic activity of AKT was inhibited. In addition, SFN inhibited the activity of the cytoplasmic histone deacetylase 6 (HDAC6), the inhibition of which has been reported to promote the acetylation and decreases the kinase activity of AKT. Conclusion SFN inhibits HDAC6 and decreases the catalytic activity of AKT, and this partially explains the mechanism by which SFN inhibits mTOR., Graphical abstract Image, graphical abstract
Published: 2021

32. Nrf2 is activated by disruption of mitochondrial thiol homeostasis but not by enhanced mitochondrial superoxide production

Author: Albena T. Dinkova-Kostova, Filip Cvetko, Hiran A. Prag, Michael P. Murphy, Stuart T. Caldwell, Maureen Higgins, Takafumi Suzuki, Richard C. Hartley, and Masayuki Yamamoto
Subjects: 0301 basic medicine, GCLC, glutamate–cysteine ligase catalytic subunit, thiol oxidation, Mitochondrion, Biochemistry, FB, fractionation buffer, NQO1, NAD(P)H:quinone oxidoreductase-1, Mice, chemistry.chemical_compound, DNM1L, Superoxides, energy metabolism, Homeostasis, Hydrogen peroxide, Cells, Cultured, HO-1, heme oxygenase-1, NAC, N-acetyl-L-cysteine, SFN, sulforaphane, chemistry.chemical_classification, Kelch-Like ECH-Associated Protein 1, Nrf2, nuclear factor erythroid 2–related factor 2, respiratory system, DRP1, dynamin-related protein 1, Glutathione, Mitochondria, Cell biology, CDNB, 1-chloro-2,4-dinitrobenzene, Keap1, Kelch-like ECH-associated protein 1, TRX, thioredoxin, Thioredoxin, Oxidation-Reduction, Research Article, Signal Transduction, NF-E2-Related Factor 2, reactive oxygen species (ROS), Nrf2, MitoPQ, MitoParaquat, 03 medical and health sciences, MitoCDNB, CD, concentration required to double, ROS, reactive oxygen species, PGAM5, phosphoglycerate mutase family member 5, Animals, TRXR2, TRX reductase 2, Cysteine, Sulfhydryl Compounds, redox signaling, Molecular Biology, Reactive oxygen species, 030102 biochemistry & molecular biology, Cell Biology, ACN, acetonitrile, MitoCDNB, MitoChlorodinitrobenzoic acid, GSS, GSH synthetase, MEF, mouse embryonic fibroblast, KEAP1, 030104 developmental biology, chemistry, BSA, bovine serum albumin, MitoPQ
Abstract: The transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) regulates the expression of genes involved in antioxidant defenses to modulate fundamental cellular processes such as mitochondrial function and GSH metabolism. Previous reports proposed that mitochondrial reactive oxygen species production and disruption of the GSH pool activate the Nrf2 pathway, suggesting that Nrf2 senses mitochondrial redox signals and/or oxidative damage and signals to the nucleus to respond appropriately. However, until now, it has not been possible to disentangle the overlapping effects of mitochondrial superoxide/hydrogen peroxide production as a redox signal from changes to mitochondrial thiol homeostasis on Nrf2. Recently, we developed mitochondria-targeted reagents that can independently induce mitochondrial superoxide and hydrogen peroxide production mitoParaquat (MitoPQ) or selectively disrupt mitochondrial thiol homeostasis MitoChlorodinitrobenzoic acid (MitoCDNB). Using these reagents, here we have determined how enhanced generation of mitochondrial superoxide and hydrogen peroxide or disruption of mitochondrial thiol homeostasis affects activation of the Nrf2 system in cells, which was assessed by the Nrf2 protein level, nuclear translocation, and expression of its target genes. We found that selective disruption of the mitochondrial GSH pool and inhibition of its thioredoxin system by MitoCDNB led to Nrf2 activation, whereas using MitoPQ to enhance the production of mitochondrial superoxide and hydrogen peroxide alone did not. We further showed that Nrf2 activation by MitoCDNB requires cysteine sensors of Kelch-like ECH-associated protein 1 (Keap1). These findings provide important information on how disruption to mitochondrial redox homeostasis is sensed in the cytoplasm and signaled to the nucleus.
Published: 2021

33. Sulfoxythiocarbamate S-4 inhibits HSP90 in human cutaneous squamous cell carcinoma cells

Author: Albena T. Dinkova-Kostova, Garrett C. VanHecke, Young Hoon Ahn, Ying Zhang, and Charlotte M. Proby
Subjects: Keratinocytes, 0301 basic medicine, Skin Neoplasms, Cell cycle checkpoint, Cyclin D, Cell, Hsp90 inhibitor, Mice, 03 medical and health sciences, 0302 clinical medicine, Thiocarbamates, medicine, Animals, Humans, HSP90 Heat-Shock Proteins, E2F, Cells, Cultured, Pharmacology, Dose-Response Relationship, Drug, biology, Chemistry, Retinoblastoma protein, Isoxazoles, Resorcinols, 030104 developmental biology, medicine.anatomical_structure, Cancer cell, Carcinoma, Squamous Cell, NIH 3T3 Cells, Cancer research, biology.protein, Tyrosine kinase, 030217 neurology & neurosurgery
Abstract: Cancer cells rely heavily on molecular chaperones, such as heat shock protein 90 (HSP90), and their co-chaperones. The development of HSP90 inhibitors is an attractive therapeutic approach that has the potential to affect multiple hallmarks of cancer. Such approach is particularly needed for tumors that carry large mutational burdens, including cutaneous squamous cell carcinomas (cSCC). We previously identified sulfoxythiocarbamate S-4 as an HSP90 inhibitor. In this study, we investigated the mechanism(s) by which S-4 compromises the viability of human cSCC cells. S-4 inhibits HSP90 and causes depletion of its clients HER2, a tyrosine kinase oncoprotein, and Bcl-2, an anti-apoptotic protein. The decrease in Bcl-2 is accompanied by cytochrome c release from mitochondria into the cytoplasm, suggesting apoptosis. In the surviving cells, depletion of the HSP90 clients cyclin D and CDK4 by S-4 prevents phosphorylation of the retinoblastoma protein Rb and the release of transcription factor E2F, inhibiting G1-S cell cycle progression and cell division. These findings illustrate the comprehensive effectiveness of S-4 and encourage future development of compounds of this type for cancer prevention and treatment.
Published: 2020

34. Electron affinity of tricyclic, bicyclic, and monocyclic compounds containing cyanoenones correlates with their potency as inducers of a cytoprotective enzyme

Author: Suqing Zheng, René V. Bensasson, Albena T. Dinkova-Kostova, Wei Li, Akira Saito, Vincent Zoete, and Tadashi Honda
Subjects: 0301 basic medicine, Stereochemistry, Clinical Biochemistry, Pharmaceutical Science, Electrons, Alkenes, 01 natural sciences, Biochemistry, Mice, 03 medical and health sciences, Cell Line, Tumor, Nitriles, Drug Discovery, NAD(P)H Dehydrogenase (Quinone), Animals, Potency, Reactivity (chemistry), Sulfhydryl Compounds, Enzyme inducer, Molecular Biology, HOMO/LUMO, chemistry.chemical_classification, Kelch-Like ECH-Associated Protein 1, Molecular Structure, biology, Bicyclic molecule, 010405 organic chemistry, Chemistry, Organic Chemistry, Ketones, 0104 chemical sciences, 030104 developmental biology, Enzyme, Electron affinity (data page), Cyclization, Cytoprotection, Enzyme Induction, biology.protein, Quantum Theory, Molecular Medicine, Signal Transduction
Abstract: Tricyclic, bicyclic, and monocyclic compounds containing cyanoenones induce various anti-inflammatory and cytoprotective enzymes through activation of the Keap1/Nrf2/ARE (antioxidant response element) pathway. The potency of these compounds as Nrf2 activators was determined using a prototypic cytoprotective enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) in Hepa1c1c7 murine hepatoma cells. The electron affinity (EA) of the compounds, expressed as the energy of their lowest unoccupied molecular orbital [E (LUMO)], was evaluated using two types of quantum mechanical calculations: the semiempirical (AM1) and the density functional theory (DFT) methods. We observed striking linear correlations [r = 0.897 (AM1) and 0.936 (DFT)] between NQO1 inducer potency of these compounds and their E (LUMO) regardless of the molecule size. Importantly and interestingly, this finding demonstrates that the EA is the essentially important factor that determines the reactivity of the cyanoenones with Keap1.
Published: 2016

35. Potency of extracts from selected Egyptian plants as inducers of the Nrf2-dependent chemopreventive enzyme NQO1

Author: Albena T. Dinkova-Kostova, Tarik A. Mohamed, Nahla S. Abdel-Azim, Ahmed R. Hamed, Mohamed-Elamir F. Hegazy, Maureen Higgins, and Paul W. Paré
Subjects: NF-E2-Related Factor 2, Biology, Quinone oxidoreductase, Chemoprevention, 01 natural sciences, Mice, Botany, NAD(P)H Dehydrogenase (Quinone), medicine, Animals, Medicinal plants, chemistry.chemical_classification, Traditional medicine, Plant Extracts, 010405 organic chemistry, Euphorbiaceae, Cancer, biology.organism_classification, medicine.disease, 0104 chemical sciences, Heme oxygenase, 010404 medicinal & biomolecular chemistry, Enzyme, Phytochemical, chemistry, Molecular Medicine, Egypt, Lamiaceae
Abstract: Medicinal plants from the Egyptian Sinai Peninsula are widely used in traditional Bedouin medicine to treat a range of conditions including cancer, and as such are a promising resource for novel anti-cancer compounds. To achieve scientific justification of traditional use and/or to recommend the use of those plants as medicinal herbs for cancer chemoprevention, a group of 11 Sinai plants of different species that belong to 3 families (Asteraceae, Lamiaceae, and Euphorbiaceae) were biologically screened for cancer preventive activity using the chemoprevention marker enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1). Among the fractions assayed, a solvent extract from Pulicaria incisa had potent NQO1 inducing activity. Further analysis of the mechanism of induction revealed the concentration-dependent stabilization of the transcription factor NF-E2 p45-related factor 2 (Nrf2) and a coordinate upregulation of the Nrf2-dependent enzymes NQO1, heme oxygenase 1 and glutathione S-transferase-Pi. These results establish P. incisa as a promising target for future phytochemical characterization for cancer preventive components.
Published: 2016

36. Synthesis, molecular modeling and NAD(P)H:quinone oxidoreductase 1 inducer activity of novel 2-phenylquinazolin-4-amine derivatives

Author: Abdelaaty A. Shahat, Reem K. Arafa, Mansour S. Alsaid, Mostafa M. Ghorab, Maureen Higgins, Nehal H. Elghazawy, and Albena T. Dinkova-Kostova
Subjects: Models, Molecular, 0301 basic medicine, Molecular model, Stereochemistry, Proton Magnetic Resonance Spectroscopy, Quinone oxidoreductase, Mass Spectrometry, Mice, 03 medical and health sciences, 0302 clinical medicine, Cell Line, Tumor, Drug Discovery, NAD(P)H Dehydrogenase (Quinone), Animals, Inducer, Amines, Carbon-13 Magnetic Resonance Spectroscopy, Enzyme inducer, Pharmacology, chemistry.chemical_classification, biology, General Medicine, Amino acid, 030104 developmental biology, chemistry, Biochemistry, Docking (molecular), Enzyme Induction, 030220 oncology & carcinogenesis, Quinazolines, biology.protein, NAD+ kinase
Abstract: Reactive oxygen species (ROS) play an integral role in the pathogenesis of most diseases. This work presents the design and synthesis of novel 2-phenylquinazolin-4-amine derivatives (2–12) and evaluation of their NAD(P)H:quinone oxidoreductase 1 (NQO1) inducer activity in murine cells. Also, molecular docking of all the new compounds was performed to assess their ability to inhibit Keap1–Nrf2 protein–protein interaction through occupying the Keap1–Nrf2-binding domain which biologically leads to a consequent Nrf2 accumulation and enhanced gene expression of NQO1. Docking results showed that all compounds have the ability to interact with Keap1; however compound 7, the most active compound in this study, showed more interactions with key amino acids.
Published: 2016

37. Nrf2 activation in the treatment of neurodegenerative diseases: a focus on its role in mitochondrial bioenergetics and function

Author: Albena T. Dinkova-Kostova, Noemí Esteras, and Andrey Y. Abramov
Subjects: 0301 basic medicine, NF-E2-Related Factor 2, Clinical Biochemistry, Biology, Mitochondrion, medicine.disease_cause, Biochemistry, Glycogen Synthase Kinase 3, 03 medical and health sciences, GSK-3, medicine, Animals, Humans, Amyotrophic lateral sclerosis, Molecular Biology, Transcription factor, Neurodegeneration, Brain, Membrane Transport Proteins, Neurodegenerative Diseases, Lipid Metabolism, medicine.disease, KEAP1, Mitochondria, Cell biology, 030104 developmental biology, DNAJA3, Energy Metabolism, Oxidative stress
Abstract: The nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2) is a transcription factor well-known for its function in controlling the basal and inducible expression of a variety of antioxidant and detoxifying enzymes. As part of its cytoprotective activity, increasing evidence supports its role in metabolism and mitochondrial bioenergetics and function. Neurodegenerative diseases are excellent candidates for Nrf2-targeted treatments. Most neurodegenerative conditions such as Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis, frontotemporal dementia and Friedreich’s ataxia are characterized by oxidative stress, misfolded protein aggregates, and chronic inflammation, the common targets of Nrf2 therapeutic strategies. Together with them, mitochondrial dysfunction is implicated in the pathogenesis of most neurodegenerative disorders. The recently recognized ability of Nrf2 to regulate intermediary metabolism and mitochondrial function makes Nrf2 activation an attractive and comprehensive strategy for the treatment of neurodegenerative disorders. This review aims to focus on the potential therapeutic role of Nrf2 activation in neurodegeneration, with special emphasis on mitochondrial bioenergetics and function, metabolism and the role of transporters, all of which collectively contribute to the cytoprotective activity of this transcription factor.
Published: 2016

38. A Defective Pentose Phosphate Pathway Reduces Inflammatory Macrophage Responses during Hypercholesterolemia

Author: Luke A. J. O'Neill, Dave Speijer, Esther Lutgens, Michel van Weeghel, Annette E. Neele, Koen H.M. Prange, Saskia van der Velden, Albena T. Dinkova-Kostova, Menno P.J. de Winther, Rob C. I. Wüst, Jeroen Baardman, Maarten E. Witte, Simone Denis, Jan Van den Bossche, Elena V. Knatko, Dylan G. Ryan, Sanne G.S. Verberk, Riekelt H. Houtkooper, Molecular cell biology and Immunology, Physiology, Amsterdam Gastroenterology Endocrinology Metabolism, ACS - Atherosclerosis & ischemic syndromes, Graduate School, Medical Biochemistry, AII - Inflammatory diseases, Laboratory Genetic Metabolic Diseases, ACS - Diabetes & metabolism, ACS - Heart failure & arrhythmias, AMS - Ageing & Morbidty, ACS - Amsterdam Cardiovascular Sciences, AII - Amsterdam institute for Infection and Immunity, AGEM - Amsterdam Gastroenterology Endocrinology Metabolism, APH - Aging & Later Life, AGEM - Endocrinology, metabolism and nutrition, AGEM - Inborn errors of metabolism, and ARD - Amsterdam Reproduction and Development
Subjects: 0301 basic medicine, Lipopolysaccharides, Male, NF-E2-Related Factor 2, Citric Acid Cycle, immunometabolism, pentose phosphate pathway, Inflammation, Pentose phosphate pathway, medicine.disease_cause, General Biochemistry, Genetics and Molecular Biology, Nrf2, 03 medical and health sciences, 0302 clinical medicine, Immune system, SDG 3 - Good Health and Well-being, cardiovascular disease, medicine, Macrophage, Animals, lcsh:QH301-705.5, hypercholesterolemia, Chemistry, meta-inflammation, Metabolism, metabolic disease, foam cells, Cell biology, macrophages, Mice, Inbred C57BL, 030104 developmental biology, Cell metabolism, lcsh:Biology (General), inflammation, 030220 oncology & carcinogenesis, Cytokine secretion, Female, medicine.symptom, atherosclerosis, Glycolysis, Oxidative stress
Abstract: Summary: Metabolic reprogramming has emerged as a crucial regulator of immune cell activation, but how systemic metabolism influences immune cell metabolism and function remains to be investigated. To investigate the effect of dyslipidemia on immune cell metabolism, we performed in-depth transcriptional, metabolic, and functional characterization of macrophages isolated from hypercholesterolemic mice. Systemic metabolic changes in such mice alter cellular macrophage metabolism and attenuate inflammatory macrophage responses. In addition to diminished maximal mitochondrial respiration, hypercholesterolemia reduces the LPS-mediated induction of the pentose phosphate pathway (PPP) and the Nrf2-mediated oxidative stress response. Our observation that suppression of the PPP diminishes LPS-induced cytokine secretion supports the notion that this pathway contributes to inflammatory macrophage responses. Overall, this study reveals that systemic and cellular metabolism are strongly interconnected, together dictating macrophage phenotype and function. : The link between systemic and cellular metabolism is a neglected aspect in immunometabolism. Baardman et al. show that hypercholesterolemia alters macrophage metabolism and phenotype. The suppressed pentose phosphate pathway (PPP) in those “foam cell” macrophages attenuates inflammatory responses, signifying that systemic and cellular metabolism together regulate macrophage function. Keywords: immunometabolism, inflammation, macrophages, hypercholesterolemia, pentose phosphate pathway, Nrf2, meta-inflammation, foam cells, atherosclerosis, cardiovascular disease, metabolic disease
Published: 2018

39. Itaconate is an anti-inflammatory metabolite that activates Nrf2 via alkylation of KEAP1

Author: Evanna L. Mills, Dylan G. Ryan, Deepthi Menon, Michael P. Murphy, Anne F. McGettrick, Richard C. Hartley, Elena V. Knatko, Edward T. Chouchani, Marah C. Runtsch, Paul J. Meakin, Mark M. Hughes, Maureen Higgins, Richard G. Carroll, Lee M. Booty, Dina Dikovskaya, Padraic G. Fallon, Daniel C. Sévin, Mark P. Jedrychowski, Christian Frezza, Gino Brunori, Joanna F. McGouran, Roman Fischer, Michael L.J. Ashford, Emily Hams, Louise K. Modis, Martin S. King, Hiran A. Prag, John Szpyt, Stuart T. Caldwell, Edmund R.S. Kunji, Benedikt M. Kessler, Ana S. H. Costa, Albena T. Dinkova-Kostova, Zbigniew Zaslona, Luke A. J. O'Neill, Prag, Hiran [0000-0002-4753-8567], King, Martin [0000-0001-6030-5154], Kunji, Edmund [0000-0002-0610-4500], Frezza, Christian [0000-0002-3293-7397], Murphy, Mike [0000-0003-1115-9618], and Apollo - University of Cambridge Repository
Subjects: Lipopolysaccharides, 0301 basic medicine, Alkylation, Carboxy-Lyases, NF-E2-Related Factor 2, Metabolite, Anti-Inflammatory Agents, Article, Mice, 03 medical and health sciences, chemistry.chemical_compound, Animals, Humans, Cysteine, Rats, Wistar, Transcription factor, Hydro-Lyases, Cysteine metabolism, Feedback, Physiological, Inflammation, Kelch-Like ECH-Associated Protein 1, Multidisciplinary, Macrophages, Proteins, Succinates, Interferon-beta, KEAP1, Rats, HEK293 Cells, 030104 developmental biology, chemistry, Biochemistry, Cytokines, Aconitate decarboxylase, Cattle, Female, lipids (amino acids, peptides, and proteins)
Abstract: The endogenous metabolite itaconate has recently emerged as a regulator of macrophage function, but its precise mechanism of action remains poorly understood1,2,3. Here we show that itaconate is required for the activation of the anti-inflammatory transcription factor Nrf2 (also known as NFE2L2) by lipopolysaccharide in mouse and human macrophages. We find that itaconate directly modifies proteins via alkylation of cysteine residues. Itaconate alkylates cysteine residues 151, 257, 288, 273 and 297 on the protein KEAP1, enabling Nrf2 to increase the expression of downstream genes with anti-oxidant and anti-inflammatory capacities. The activation of Nrf2 is required for the anti-inflammatory action of itaconate. We describe the use of a new cell-permeable itaconate derivative, 4-octyl itaconate, which is protective against lipopolysaccharide-induced lethality in vivo and decreases cytokine production. We show that type I interferons boost the expression of Irg1 (also known as Acod1) and itaconate production. Furthermore, we find that itaconate production limits the type I interferon response, indicating a negative feedback loop that involves interferons and itaconate. Our findings demonstrate that itaconate is a crucial anti-inflammatory metabolite that acts via Nrf2 to limit inflammation and modulate type I interferons.
Published: 2018

40. Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Author: Albena T. Dinkova-Kostova, Holly Robertson, Stephen T. Durant, Steven Vitale, John D. Hayes, Trevor M. Penning, and Lauren E. Tebay
Subjects: biology, Carcinogenesis, NF-E2-Related Factor 2, mTORC1, Biochemistry, mTORC2, KEAP1, Article, Ubiquitin ligase, Oxidative Stress, Physiology (medical), Ubiquitin ligase complex, biology.protein, Animals, Humans, Thioredoxin, Signal transduction, Oxidation-Reduction, Protein kinase B, Signal Transduction
Abstract: Nuclear factor-erythroid 2 p45-related factor 2 (Nrf2) regulates the basal and stress-inducible expression of a battery of genes encoding key components of the glutathione-based and thioredoxin-based antioxidant systems, as well as aldo-keto reductase, glutathione S- transferase, and NAD(P)H:quinone oxidoreductase-1 drug-metabolizing isoenzymes along with multidrug-resistance-associated efflux pumps. It therefore plays a pivotal role in both intrinsic resistance and cellular adaptation to reactive oxygen species (ROS) and xenobiotics. Activation of Nrf2 can, however, serve as a double-edged sword because some of the genes it induces may contribute to chemical carcinogenesis by promoting futile redox cycling of polycyclic aromatic hydrocarbon metabolites or confer resistance to chemotherapeutic drugs by increasing the expression of efflux pumps, suggesting its cytoprotective effects will vary in a context-specific fashion. In addition to cytoprotection, Nrf2 also controls genes involved in intermediary metabolism, positively regulating those involved in NADPH generation, purine biosynthesis, and the β-oxidation of fatty acids, while suppressing those involved in lipogenesis and gluconeogenesis. Nrf2 is subject to regulation at multiple levels. Its ability to orchestrate adaptation to oxidants and electrophiles is due principally to stress-stimulated modification of thiols within one of its repressors, the Kelch-like ECH-associated protein 1 (Keap1), which is present in the cullin-3 RING ubiquitin ligase (CRL) complex CRL Keap1 . Thus modification of Cys residues in Keap1 blocks CRL Keap1 activity, allowing newly translated Nrf2 to accumulate rapidly and induce its target genes. The ability of Keap1 to repress Nrf2 can be attenuated by p62/sequestosome-1 in a mechanistic target of rapamycin complex 1 (mTORC1)-dependent manner, thereby allowing refeeding after fasting to increase Nrf2-target gene expression. In parallel with repression by Keap1, Nrf2 is also repressed by β-transducin repeat-containing protein (β-TrCP), present in the Skp1–cullin-1–F-box protein (SCF) ubiquitin ligase complex SCF β-TrCP . The ability of SCF β-TrCP to suppress Nrf2 activity is itself enhanced by prior phosphorylation of the transcription factor by glycogen synthase kinase-3 (GSK-3) through formation of a DSGIS-containing phosphodegron. However, formation of the phosphodegron in Nrf2 by GSK-3 is inhibited by stimuli that activate protein kinase B (PKB)/Akt. In particular, PKB/Akt activity can be increased by phosphoinositide 3-kinase and mTORC2, thereby providing an explanation of why antioxidant-responsive element-driven genes are induced by growth factors and nutrients. Thus Nrf2 activity is tightly controlled via CRL Keap1 and SCF β-TrCP by oxidative stress and energy-based signals, allowing it to mediate adaptive responses that restore redox homeostasis and modulate intermediary metabolism. Based on the fact that Nrf2 influences multiple biochemical pathways in both positive and negative ways, it is likely its dose–response curve, in terms of susceptibility to certain degenerative disease, is U-shaped. Specifically, too little Nrf2 activity will lead to loss of cytoprotection, diminished antioxidant capacity, and lowered β-oxidation of fatty acids, while conversely also exhibiting heightened sensitivity to ROS-based signaling that involves receptor tyrosine kinases and apoptosis signal-regulating kinase-1. By contrast, too much Nrf2 activity disturbs the homeostatic balance in favor of reduction, and so may have deleterious consequences including overproduction of reduced glutathione and NADPH, the blunting of ROS-based signal transduction, epithelial cell hyperplasia, and failure of certain cell types to differentiate correctly. We discuss the basis of a putative U-shaped Nrf2 dose–response curve in terms of potentially competing processes relevant to different stages of tumorigenesis.
Published: 2015

41. The emerging role of Nrf2 in mitochondrial function

Author: Dinkova-Kostova, Albena T. and Abramov, Andrey Y.
Subjects: Keap1, NF-E2-Related Factor 2, Free radicals, Bioenergetics, Biochemistry, Article, Nrf2, Mitochondria, Cytoprotection, Physiology (medical), Animals, Humans, Energy Metabolism, Oxidation-Reduction
Abstract: The transcription factor NF-E2 p45-related factor 2 (Nrf2; gene name NFE2L2) allows adaptation and survival under conditions of stress by regulating the gene expression of diverse networks of cytoprotective proteins, including antioxidant, anti-inflammatory, and detoxification enzymes as well as proteins that assist in the repair or removal of damaged macromolecules. Nrf2 has a crucial role in the maintenance of cellular redox homeostasis by regulating the biosynthesis, utilization, and regeneration of glutathione, thioredoxin, and NADPH and by controlling the production of reactive oxygen species by mitochondria and NADPH oxidase. Under homeostatic conditions, Nrf2 affects the mitochondrial membrane potential, fatty acid oxidation, availability of substrates (NADH and FADH2/succinate) for respiration, and ATP synthesis. Under conditions of stress or growth factor stimulation, activation of Nrf2 counteracts the increased reactive oxygen species production in mitochondria via transcriptional upregulation of uncoupling protein 3 and influences mitochondrial biogenesis by maintaining the levels of nuclear respiratory factor 1 and peroxisome proliferator-activated receptor γ coactivator 1α, as well as by promoting purine nucleotide biosynthesis. Pharmacological Nrf2 activators, such as the naturally occurring isothiocyanate sulforaphane, inhibit oxidant-mediated opening of the mitochondrial permeability transition pore and mitochondrial swelling. Curiously, a synthetic 1,4-diphenyl-1,2,3-triazole compound, originally designed as an Nrf2 activator, was found to promote mitophagy, thereby contributing to the overall mitochondrial homeostasis. Thus, Nrf2 is a prominent player in supporting the structural and functional integrity of the mitochondria, and this role is particularly crucial under conditions of stress., Highlights • Nrf2 has a crucial role in maintaining cellular redox homeostasis. • Nrf2 affects the mitochondrial membrane potential and ATP synthesis. • Nrf2 influences mitochondrial fatty acid oxidation. • Nrf2 supports the structural and functional integrity of the mitochondria. • Nrf2 activators have beneficial effects when mitochondrial function is compromised.
Published: 2015
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42. The spatiotemporal regulation of the Keap1–Nrf2 pathway and its importance in cellular bioenergetics

Author: Colin J. Meyer, Kira M. Holmström, Liam Baird, Albena T. Dinkova-Kostova, and Andrey Y. Abramov
Subjects: Models, Molecular, NF-E2-Related Factor 2, Oxidative phosphorylation, Mitochondrion, Biology, S2, digestive system, environment and public health, Biochemistry, The Keap1/Nrf2 Pathway in Health and Disease, S4, 03 medical and health sciences, 0302 clinical medicine, cytoprotection, Animals, Humans, Transcription factor, 030304 developmental biology, 0303 health sciences, Kelch-Like ECH-Associated Protein 1, PINK1, Intracellular Signaling Peptides and Proteins, respiratory system, KEAP1, Mitochondria, Cell biology, FRET/FLIM, Mitochondrial biogenesis, redox, Ubiquitin ligase complex, Signal transduction, Energy Metabolism, Oxidation-Reduction, Biochemical Society Focused Meetings, 030217 neurology & neurosurgery, Signal Transduction
Abstract: The Kelch-like ECH associated protein 1 (Keap1)–NF-E2 p45-related factor 2 (Nrf2) pathway regulates networks of proteins that protect against the cumulative damage of oxidants, electrophiles and misfolded proteins. The interaction between transcription factor Nrf2 and its main negative cytoplasmic regulator Keap1 follows a cycle whereby the protein complex sequentially adopts two conformations: ‘open’, in which Nrf2 binds to one monomer of Keap1, followed by ‘closed’, in which Nrf2 interacts with both members of the Keap1 dimer. Electrophiles and oxidants (inducers) are recognized by cysteine sensors within Keap1, disrupting its ability to target Nrf2 for ubiquitination and degradation. Consequently, the protein complex accumulates in the ‘closed’ conformation, free Keap1 is not regenerated and newly synthesized Nrf2 is stabilized to activate target-gene transcription. The prevailing view of the Keap1–Nrf2 pathway, for which there exists a wealth of experimental evidence, is that it lies at the heart of cellular defence, playing crucial roles in adaptation and survival under conditions of stress. More recently, the significance of Nrf2 in intermediary metabolism and mitochondrial physiology has also been recognized, adding another layer of cytoprotection to the repertoire of functions of Nrf2. One way by which Nrf2 influences mitochondrial activity is through increasing the availability of substrates (NADH and FADH2) for respiration. Another way is through accelerating fatty acid oxidation (FAO). These findings reinforce the reciprocal relationship between oxidative phosphorylation and the cellular redox state, and highlight the key role of Nrf2 in regulating this balance.
Published: 2015

43. Nrf2 Activation Protects against Solar-Simulated Ultraviolet Radiation in Mice and Humans

Author: James Ferguson, Paul Talalay, Ying Zhang, Jed W. Fahey, Albena T. Dinkova-Kostova, Sukirti Kalra, Akira Saito, Suqing Zheng, Maureen Higgins, Elena V. Knatko, Charlotte M. Proby, Robert S. Dawe, Sally H. Ibbotson, Jeffrey T.-J. Huang, Rosemary G. Clarke, Andrea L. Benedict, and Tadashi Honda
Subjects: Cancer Research, Skin erythema, Neoplasms, Radiation-Induced, Skin Neoplasms, NF-E2-Related Factor 2, Ultraviolet Rays, Blotting, Western, Biology, Real-Time Polymerase Chain Reaction, medicine.disease_cause, environment and public health, Article, Mice, Downregulation and upregulation, Solar Energy, medicine, Animals, Humans, RNA, Messenger, Carcinogen, Skin, Mice, Knockout, Mice, Hairless, Reverse Transcriptase Polymerase Chain Reaction, Activator (genetics), Interleukin, respiratory system, Healthy Volunteers, Hairless, Mice, Inbred C57BL, Oxidative Stress, Oncology, Immunology, Cancer research, Female, Carcinogenesis, Biomarkers, Oxidative stress
Abstract: The transcription factor Nrf2 determines the ability to adapt and survive under conditions of electrophilic, oxidative, and inflammatory stress by regulating the expression of elaborate networks comprising nearly 500 genes encoding proteins with versatile cytoprotective functions. In mice, disruption of Nrf2 increases susceptibility to carcinogens and accelerates disease pathogenesis. Paradoxically, Nrf2 is upregulated in established human tumors, but whether this upregulation drives carcinogenesis is not known. Here we show that the incidence, multiplicity, and burden of solar-simulated UV radiation–mediated cutaneous tumors that form in SKH-1 hairless mice in which Nrf2 is genetically constitutively activated are lower than those that arise in their wild-type counterparts. Pharmacologic Nrf2 activation by topical biweekly applications of small (40 nmol) quantities of the potent bis(cyano enone) inducer TBE-31 has a similar protective effect against solar-simulated UV radiation in animals receiving long-term treatment with the immunosuppressive agent azathioprine. Genetic or pharmacologic Nrf2 activation lowers the expression of the pro-inflammatory factors IL6 and IL1β, and COX2 after acute exposure of mice to UV radiation. In healthy human subjects, topical applications of extracts delivering the Nrf2 activator sulforaphane reduced the degree of solar-simulated UV radiation–induced skin erythema, a quantifiable surrogate endpoint for cutaneous damage and skin cancer risk. Collectively, these data show that Nrf2 is not a driver for tumorigenesis even upon exposure to a very potent and complete carcinogen and strongly suggest that the frequent activation of Nrf2 in established human tumors is a marker of metabolic adaptation. Cancer Prev Res; 8(6); 475–86. ©2015 AACR.
Published: 2015

44. Transcription factors Hsf1 and Nrf2 engage in crosstalk for cytoprotection

Author: Albena T. Dinkova-Kostova, Sharadha Dayalan Naidu, and Rumen V. Kostov
Subjects: Pharmacology, NF-E2-Related Factor 2, Activating transcription factor, Biology, Toxicology, Molecular biology, Cytoprotection, Mitochondria, Cell biology, DNA-Binding Proteins, Heat shock factor, Crosstalk (biology), Heat Shock Transcription Factors, Downregulation and upregulation, Heat shock protein, Animals, Humans, HSF1, Oxidation-Reduction, Transcription factor, Transcription Factors
Abstract: Transcription factors heat shock factor (Hsf)1 and nuclear factor-erythroid 2 p45-related factor (Nrf)2 are critical for adaptation and survival. Each is maintained at low basal levels, but is robustly activated by various stimuli, including cysteine-reactive small molecules (inducers). Although each is regulated by distinct mechanisms, it is emerging that these transcription factors engage in crosstalk by sharing overlapping transcriptional targets, such as heat shock protein (HSP)70, p62, and activating transcription factor (ATF)3, and in certain cases, compensating for each other. Critically, activation of Hsf1 or Nrf2 affects the cellular redox balance by promoting the reduced state. Conversely, deletion of Hsf1 or Nrf2 is associated with oxidative stress and impaired mitochondrial function. Transient activation of Hsf1 and Nrf2 is cytoprotective, but their persistent upregulation may be detrimental, causing cardiomyopathy or accelerating carcinogenesis, and should be considered when designing strategies for disease prevention and treatment.
Published: 2015

45. Metabolic and Homeostatic Changes in Seizures and Acquired Epilepsy-Mitochondria, Calcium Dynamics and Reactive Oxygen Species

Author: Ali Gorji, Albena T Dinkova Kostova, Stjepana Kovac, Nico Melzer, Sven G. Meuth, and Alexander M. Herrmann
Subjects: 0301 basic medicine, Review, Pharmacology, Mitochondrion, medicine.disease_cause, Endoplasmic Reticulum, Epileptogenesis, lcsh:Chemistry, Epilepsy, 0302 clinical medicine, Adenosine Triphosphate, Calcium dynamics, Homeostasis, lcsh:QH301-705.5, Spectroscopy, chemistry.chemical_classification, reactive oxygen species, Cell Death, Acquired epilepsy, General Medicine, Computer Science Applications, Mitochondria, NF-E2-Related Factor 2, Biology, Catalysis, Nrf2, Inorganic Chemistry, 03 medical and health sciences, Seizures, medicine, Animals, Humans, Physical and Theoretical Chemistry, Molecular Biology, Reactive oxygen species, calcium, Research, Organic Chemistry, Cell Membrane, medicine.disease, Oxidative Stress, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, chemistry, Calcium Channels, Energy Metabolism, Neuroscience, 030217 neurology & neurosurgery, Oxidative stress
Abstract: Acquired epilepsies can arise as a consequence of brain injury and result in unprovoked seizures that emerge after a latent period of epileptogenesis. These epilepsies pose a major challenge to clinicians as they are present in the majority of patients seen in a common outpatient epilepsy clinic and are prone to pharmacoresistance, highlighting an unmet need for new treatment strategies. Metabolic and homeostatic changes are closely linked to seizures and epilepsy, although, surprisingly, no potential treatment targets to date have been translated into clinical practice. We summarize here the current knowledge about metabolic and homeostatic changes in seizures and acquired epilepsy, maintaining a particular focus on mitochondria, calcium dynamics, reactive oxygen species and key regulators of cellular metabolism such as the Nrf2 pathway. Finally, we highlight research gaps that will need to be addressed in the future which may help to translate these findings into clinical practice.
Published: 2017

46. KEAP1-modifying small molecule reveals muted NRF2 signaling responses in neural stem cells from Huntington's disease patients

Author: Colúm Connolly, Clemens Steegborn, Donald C. Lo, Albena T. Dinkova-Kostova, Andrew Snyder, Vanita Chopra, Alexei Degterev, Michael A. Schwarzschild, Cho Low, Ulrike Träger, Leslie M. Thompson, Michael J. Van Kanegan, James R. Miller, Matthew Fuszard, Ningzhe Zhang, Ellen Sapp, Susanta Samajdar, Lisa Meisel, Kimberly B. Kegel-Gleason, Petr Vodicka, Adelaide Tousley, Lisa M. Ellerby, David Llères, Sébastien Moniot, Aleksey G. Kazantsev, Steven M. Hersch, Lisa A. Crawford, Ross S. Stein, Sarah J. Tabrizi, Eranthie Weerapana, Vijay Potluri, Linda S. Kaltenbach, Ruth Farmer, Blair R. Leavitt, Maureen Higgins, Luisa Quinti, Marian DiFiglia, Sharadha Dayalan Naidu, and Xiqun Chen
Subjects: 0301 basic medicine, Huntington's Disease, Male, Protein Conformation, Neurodegenerative, Inbred C57BL, environment and public health, Mice, Neural Stem Cells, NRF2 inducer, 2.1 Biological and endogenous factors, Aetiology, Cells, Cultured, Multidisciplinary, Cultured, Kelch-Like ECH-Associated Protein 1, biology, Microglia, Signal transducing adaptor protein, Brain, Middle Aged, respiratory system, Neural stem cell, Ubiquitin ligase, Cell biology, medicine.anatomical_structure, Huntington Disease, Neuroprotective Agents, Biochemistry, PNAS Plus, Cytokines, Female, Signal transduction, KEAP1/NRF2/ARE signaling, Huntington’s disease, Signal Transduction, Adult, antiinflammatory responses, NF-E2-Related Factor 2, Cells, 1.1 Normal biological development and functioning, digestive system, Proinflammatory cytokine, 03 medical and health sciences, Rare Diseases, Huntington's disease, Clinical Research, Underpinning research, medicine, Genetics, Animals, Humans, Transcription factor, Aged, Animal, Macrophages, Neurosciences, MPTP Poisoning, medicine.disease, Stem Cell Research, Brain Disorders, Rats, Mice, Inbred C57BL, Disease Models, Animal, 030104 developmental biology, human neural stem cells, HEK293 Cells, Disease Models, biology.protein
Abstract: The activity of the transcription factor nuclear factor-erythroid 2 p45-derived factor 2 (NRF2) is orchestrated and amplified through enhanced transcription of antioxidant and antiinflammatory target genes. The present study has characterized a triazole-containing inducer of NRF2 and elucidated the mechanism by which this molecule activates NRF2 signaling. In a highly selective manner, the compound covalently modifies a critical stress-sensor cysteine (C151) of the E3 ligase substrate adaptor protein Kelch-like ECH-associated protein 1 (KEAP1), the primary negative regulator of NRF2. We further used this inducer to probe the functional consequences of selective activation of NRF2 signaling in Huntington's disease (HD) mouse and human model systems. Surprisingly, we discovered a muted NRF2 activation response in human HD neural stem cells, which was restored by genetic correction of the disease-causing mutation. In contrast, selective activation of NRF2 signaling potently repressed the release of the proinflammatory cytokine IL-6 in primary mouse HD and WT microglia and astrocytes. Moreover, in primary monocytes from HD patients and healthy subjects, NRF2 induction repressed expression of the proinflammatory cytokines IL-1, IL-6, IL-8, and TNFα. Together, our results demonstrate a multifaceted protective potential of NRF2 signaling in key cell types relevant to HD pathology.
Published: 2017

47. Oxidative stress and chronic inflammation in osteoarthritis: can NRF2 counteract these partners in crime?

Author: Andrey S, Marchev, Petya A, Dimitrova, Andrew J, Burns, Rumen V, Kostov, Albena T, Dinkova-Kostova, and Milen I, Georgiev
Subjects: Inflammation, Oxidative Stress, Chondrocytes, Osteoblasts, NF-E2-Related Factor 2, Chronic Disease, Osteoarthritis, Animals, Humans, Protein Binding
Abstract: Osteoarthritis (OA) is an age-related joint degenerative disease associated with pain, joint deformity, and disability. The disease starts with cartilage damage but then progressively involves subchondral bone, causing an imbalance between osteoclast-driven bone resorption and osteoblast-driven remodeling. Here, we summarize the data for the role of oxidative stress and inflammation in OA pathology and discuss how these two processes are integrated during OA progression, as well as their contribution to abnormalities in cartilage/bone metabolism and integrity. At the cellular level, oxidative stress and inflammation are counteracted by transcription factor nuclear factor erythroid p45-related factor 2 (NRF2), and we describe the regulation of NRF2, highlighting its role in OA pathology. We also discuss the beneficial effect of some phytonutrients, including the therapeutic potential of NRF2 activation, in OA.
Published: 2017

48. Flavonolignan 2,3-dehydrosilydianin activates Nrf2 and upregulates NAD(P)H:quinone oxidoreductase 1 in Hepa1c1c7 cells

Author: Lenka, Roubalová, Albena T, Dinkova-Kostova, David, Biedermann, Vladimír, Křen, Jitka, Ulrichová, and Jiří, Vrba
Subjects: NF-E2-Related Factor 2, Glutamate-Cysteine Ligase, NQO1, NAD(P)H:quinone oxidoreductase 1, Gene Expression, ARE, antioxidant response element, Gapdh, glyceraldehyde-3-phosphate dehydrogenase, DMSO, dimethyl sulfoxide, SC, silychristin, Article, Nrf2, DHSD, 2,3-dehydrosilydianin, SB, silybin, Mice, MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, Silybum marianum, ROS, reactive oxygen species, Cell Line, Tumor, NAD(P)H Dehydrogenase (Quinone), Nrf2/NFE2L2, NF-E2 p45-related factor 2, Animals, Humans, Milk Thistle, DHSC, 2,3-dehydrosilychristin, SFN, sulforaphane, Molecular Structure, HMOX1, heme oxygenase-1, Membrane Proteins, SD, silydianin, GCLM, glutamate-cysteine ligase modifier subunit, Up-Regulation, Keap1, Kelch-like ECH-associated protein 1, Flavonolignans, Silybin, NQO1, DHSB, 2,3-dehydrosilybin, Heme Oxygenase-1, GCLC, glutamate-cysteine ligase catalytic subunit, Silymarin
Abstract: Silybum marianum (milk thistle) is a medicinal plant used for the treatment of various liver disorders. This study examined whether the main flavonolignans from S. marianum (i.e. silybin, silychristin, silydianin) and their 2,3-dehydro derivatives (i.e. 2,3-dehydrosilybin, 2,3-dehydrosilychristin, 2,3-dehydrosilydianin) activate the Nrf2 pathway, which regulates the expression of genes encoding many cytoprotective enzymes, including NAD(P)H:quinone oxidoreductase 1 (NQO1). After 48 h of exposure, 2,3-dehydrosilydianin at concentrations of 25 μM and higher significantly elevated the activity of NQO1 in murine hepatoma Hepa1c1c7 cells. In contrast, other tested compounds at non-cytotoxic concentrations had a mild or negligible effect on the NQO1 activity. Using a luciferase reporter assay, 2,3-dehydrosilydianin was found to significantly activate transcription via the antioxidant response element in stably transfected human AREc32 reporter cells. Moreover, 2,3-dehydrosilydianin caused the accumulation of Nrf2 and significantly induced the expression of the Nqo1 gene at both the mRNA and protein levels in Hepa1c1c7 cells. We found that 2,3-dehydrosilydianin also increased to some extent the expression of other Nrf2 target genes, namely of the heme oxygenase-1 gene (Hmox1) and the glutamate-cysteine ligase modifier subunit gene (Gclm). We conclude that 2,3-dehydrosilydianin activates Nrf2 and induces Nrf2-mediated gene expression in Hepa1c1c7 cells., Graphical abstract Image 1
Published: 2017

49. NRF2 as an Emerging Therapeutic Target

Author: Ian M. Copple, W. Christian Wigley, Albena T. Dinkova-Kostova, Thomas W. Kensler, and Karen T. Liby
Subjects: 0301 basic medicine, Aging, Article Subject, business.industry, lcsh:Cytology, NF-E2-Related Factor 2, MEDLINE, Cell Biology, General Medicine, Bioinformatics, Biochemistry, 03 medical and health sciences, Oxidative Stress, 030104 developmental biology, 0302 clinical medicine, Editorial, 030220 oncology & carcinogenesis, Optometry, Medicine, Animals, Humans, lcsh:QH573-671, business, Introductory Journal Article
Published: 2017

50. Nrf2 affects the efficiency of mitochondrial fatty acid oxidation

Author: Albena T. Dinkova-Kostova, Ying Zhang, Plamena R. Angelova, Andrey Y. Abramov, and Marthe H.R. Ludtmann
Subjects: NF-E2-Related Factor 2, Cellular respiration, Cell Respiration, Palmitic Acid, Mitochondria, Liver, Oxidative phosphorylation, Fatty Acids, Nonesterified, Mitochondrion, Biology, digestive system, environment and public health, Biochemistry, Mitochondria, Heart, Oxidative Phosphorylation, Article, Palmitic acid, Mice, chemistry.chemical_compound, Adenosine Triphosphate, Animals, adipocyte protein 2, Caproates, Molecular Biology, Beta oxidation, Cells, Cultured, Heart metabolism, Fatty acid synthesis, Adaptor Proteins, Signal Transducing, Mice, Knockout, Kelch-Like ECH-Associated Protein 1, Cell Biology, respiratory system, Embryo, Mammalian, Up-Regulation, Mice, Inbred C57BL, Cytoskeletal Proteins, Kinetics, chemistry, Flavin-Adenine Dinucleotide, biology.protein, Oxidation-Reduction
Abstract: Transcription factor Nrf2 (NF-E2 p45-related factor 2) regulates the cellular redox homoeostasis and cytoprotective responses, allowing adaptation and survival under conditions of stress. The significance of Nrf2 in intermediary metabolism is also beginning to be recognized. Thus this transcription factor negatively affects fatty acid synthesis. However, the effect of Nrf2 on fatty acid oxidation is currently unknown. In the present paper, we report that the mitochondrial oxidation of long-chain (palmitic) and short-chain (hexanoic) fatty acids is depressed in the absence of Nrf2 and accelerated when Nrf2 is constitutively active. Addition of fatty acids stimulates respiration in heart and liver mitochondria isolated from wild-type mice. This effect is significantly weaker when Nrf2 is deleted, whereas it is stronger when Nrf2 activity is constitutively high. In the absence of glucose, addition of fatty acids differentially affects the production of ATP in mouse embryonic fibroblasts from wild-type, Nrf2-knockout and Keap1 (Kelch-like ECH-associated protein 1)-knockout mice. In acute tissue slices, the rate of regeneration of FADH2 is reduced when Nrf2 is absent. This metabolic role of Nrf2 on fatty acid oxidation has implications for chronic disease conditions including cancer, metabolic syndrome and neurodegeneration.
Published: 2014

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