Author: "Cécile Coudy-Gandilhon" - Searchworks@Jio Institute Digital Library Search Results

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1. Knockout of the Muscle-Specific E3 Ligase MuRF1 Affects Liver Lipid Metabolism upon Dexamethasone Treatment in Mice

Author: Laurent Mosoni, Arno Germond, Cécile Coudy-Gandilhon, Mélodie Malige, Agnès Claustre, Coralie Delabrise, Mehdi Djelloul-Mazouz, Yoann Delorme, Julien Hermet, Pierre Fafournoux, Lydie Combaret, Cécile Polge, Anne-Catherine Maurin, and Daniel Taillandier
Subjects: Chemistry, QD1-999
Published: 2024
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2. GCN2 upregulates autophagy in response to short-term deprivation of a single essential amino acid

Author: Anne-Catherine Maurin, Laurent Parry, Wafa B’chir, Valérie Carraro, Cécile Coudy-Gandilhon, Ghita Chaouki, Cédric Chaveroux, Sylvie Mordier, Brigitte Martinie, Vanessa Reinhardt, Céline Jousse, Alain Bruhat, Patrice Codogno, Julien Averous, and Pierre Fafournoux
Subjects: atf4, eif2α, leucine, lysine, Cytology, QH573-671
Abstract: The ability to adapt the proteolysis rates based on fluctuations in essential amino acid (EAA) availability is essential for life. The GCN2-eIF2α-ATF4 signaling pathway is involved in the adaptive response to EAA deprivations. Our previous results demonstrated that activation of this pathway is involved in upregulating the expression of many autophagy genes at the transcriptional level thanks to the transcription factor ATF4. In the present study, we investigated whether the kinase GCN2 is also involved in early upregulation of the autophagic process in response to EAA deficiencies, thereby contributing to a rapid increase in the proteolysis rate. We observed that a one-hour leucine deprivation upregulated autophagy in both cultured cells and in vivo in mouse liver, as reflected by an increase in both [S278]-ATG16L1 phosphorylation and LC3B conversion, and decreased p62 protein level. Using cells and mice with genetic ablation of Gcn2 as well as genetic reconstitution experiments in vitro, data showed that GCN2 was required for this upregulation of autophagy. Downstream GCN2, the phosphorylation of eIF2α was necessary, while ATF4 was not. Overall, these findings revealed a major role of GCN2-eIF2α signaling in the regulation of autophagy in response to short-term EAA deprivation.
Published: 2022
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3. Induction of ATF4-Regulated Atrogenes Is Uncoupled from Muscle Atrophy during Disuse in Halofuginone-Treated Mice and in Hibernating Brown Bears

Author: Laura Cussonneau, Cécile Coudy-Gandilhon, Christiane Deval, Ghita Chaouki, Mehdi Djelloul-Mazouz, Yoann Delorme, Julien Hermet, Guillemette Gauquelin-Koch, Cécile Polge, Daniel Taillandier, Julien Averous, Alain Bruhat, Céline Jousse, Isabelle Papet, Fabrice Bertile, Etienne Lefai, Pierre Fafournoux, Anne-Catherine Maurin, and Lydie Combaret
Subjects: skeletal muscle, unloading, hindlimb suspension, halofuginone, ATF4, TGF-β/BMP signalling, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Activating transcription factor 4 (ATF4) is involved in muscle atrophy through the overexpression of some atrogenes. However, it also controls the transcription of genes involved in muscle homeostasis maintenance. Here, we explored the effect of ATF4 activation by the pharmacological molecule halofuginone during hindlimb suspension (HS)-induced muscle atrophy. Firstly, we reported that periodic activation of ATF4-regulated atrogenes (Gadd45a, Cdkn1a, and Eif4ebp1) by halofuginone was not associated with muscle atrophy in healthy mice. Secondly, halofuginone-treated mice even showed reduced atrophy during HS, although the induction of the ATF4 pathway was identical to that in untreated HS mice. We further showed that halofuginone inhibited transforming growth factor-β (TGF-β) signalling, while promoting bone morphogenetic protein (BMP) signalling in healthy mice and slightly preserved protein synthesis during HS. Finally, ATF4-regulated atrogenes were also induced in the atrophy-resistant muscles of hibernating brown bears, in which we previously also reported concurrent TGF-β inhibition and BMP activation. Overall, we show that ATF4-induced atrogenes can be uncoupled from muscle atrophy. In addition, our data also indicate that halofuginone can control the TGF-β/BMP balance towards muscle mass maintenance. Whether halofuginone-induced BMP signalling can counteract the effect of ATF4-induced atrogenes needs to be further investigated and may open a new avenue to fight muscle atrophy. Finally, our study opens the way for further studies to identify well-tolerated chemical compounds in humans that are able to fine-tune the TGF-β/BMP balance and could be used to preserve muscle mass during catabolic situations.
Published: 2022
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4. Activation of the eIF2α-ATF4 Pathway by Chronic Paracetamol Treatment Is Prevented by Dietary Supplementation with Cysteine

Author: Valérie Carraro, Lydie Combaret, Cécile Coudy-Gandilhon, Laurent Parry, Julien Averous, Anne-Catherine Maurin, Céline Jousse, Guillaume Voyard, Pierre Fafournoux, Isabelle Papet, and Alain Bruhat
Subjects: acetaminophen, eIF2α-ATF4 pathway, GCN2, cysteine, liver, skeletal muscle, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Chronic treatment with acetaminophen (APAP) induces cysteine (Cys) and glutathione (GSH) deficiency which leads to adverse metabolic effects including muscle atrophy. Mammalian cells respond to essential amino acid deprivation through the phosphorylation of the eukaryotic translation initiation factor 2α (eIF2α). Phosphorylated eIF2α leads to the recruitment of activating transcription factor 4 (ATF4) to specific CCAAT/enhancer-binding protein-ATF response element (CARE) located in the promoters of target genes. Our purpose was to study the activation of the eIF2α-ATF4 pathway in response to APAP-induced Cys deficiency, as well as the potential contribution of the eIF2α kinase GCN2 and the effect of dietary supplementation with Cys. Our results showed that chronic treatment with APAP activated both GCN2 and PERK eIF2α kinases and downstream target genes in the liver. Activation of the eIF2α-ATF4 pathway in skeletal muscle was accompanied by muscle atrophy even in the absence of GCN2. The dietary supplementation with cysteine reversed APAP-induced decreases in plasma-free Cys, liver GSH, muscle mass, and muscle GSH. Our new findings demonstrate that dietary Cys supplementation also reversed the APAP-induced activation of GCN2 and PERK and downstream ATF4-target genes in the liver.
Published: 2022
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5. A Single Bout of Ultra-Endurance Exercise Reveals Early Signs of Muscle Aging in Master Athletes

Author: Cécile Coudy-Gandilhon, Marine Gueugneau, Christophe Chambon, Daniel Taillandier, Lydie Combaret, Cécile Polge, Guillaume Y. Millet, Léonard Féasson, and Daniel Béchet
Subjects: aging, exercise, skeletal muscle, capillaries, lipid droplets, extracellular matrix, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Middle-aged and master endurance athletes exhibit similar physical performance and long-term muscle adaptation to aerobic exercise. Nevertheless, we hypothesized that the short-term plasticity of the skeletal muscle might be distinctly altered for master athletes when they are challenged by a single bout of prolonged moderate-intensity exercise. Six middle-aged (37Y) and five older (50Y) master highly-trained athletes performed a 24-h treadmill run (24TR). Vastus lateralis muscle biopsies were collected before and after the run and assessed for proteomics, fiber morphometry, intramyocellular lipid droplets (LD), mitochondrial oxidative activity, extracellular matrix (ECM), and micro-vascularisation. Before 24TR, muscle fiber type morphometry, intramyocellular LD, oxidative activity, ECM and micro-vascularisation were similar between master and middle-aged runners. For 37Y runners, 24TR was associated with ECM thickening, increased capillary-to-fiber interface, and an 89% depletion of LD in type-I fibers. In contrast, for 50Y runners, 24TR did not alter ECM and capillarization and poorly depleted LDs. Moreover, an impaired succinate dehydrogenase activity and functional class scoring of proteomes suggested reduced oxidative phosphorylation post-24TR exclusively in 50Y muscle. Collectively, our data support that middle-aged and master endurance athletes exhibit distinct transient plasticity in response to a single bout of ultra-endurance exercise, which may constitute early signs of muscle aging for master athletes.
Published: 2022
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6. Increased Serpina3n release into circulation during glucocorticoid‐mediated muscle atrophy

Author: Marine Gueugneau, Donatienne d'Hose, Caroline Barbé, Marie deBarsy, Pascale Lause, Dominique Maiter, Laure B. Bindels, Nathalie M. Delzenne, Laurent Schaeffer, Yann‐Gaël Gangloff, Christophe Chambon, Cécile Coudy‐Gandilhon, Daniel Béchet, and Jean‐Paul Thissen
Subjects: Serpina3n, Glucocorticoids, Muscle atrophy, Biomarker, Diseases of the musculoskeletal system, RC925-935, Human anatomy, QM1-695
Abstract: Abstract Background Glucocorticoids (GC) play a major role in muscle atrophy. As skeletal muscle is a secretory organ, characterization of the muscle secretome elicited by muscle atrophy should allow to better understand the cellular mechanisms and to identify circulating biomarkers of this condition. Our project aimed to identify the changes in the muscle secretome associated with GC‐induced muscle atrophy and susceptible to translate into circulation. Methods We have identified the GC‐induced changes in the secretome of C2C12 muscle cells by proteomic analysis, and then, we have determined how these changes translate into the circulation of mice or human subjects exposed to high concentrations of GC. Results This approach led us to identify Serpina3n as one of the most markedly secreted protein in response to GC. Our original in vitro results were confirmed in vivo by an increased expression of Serpina3n in skeletal muscle (3.9‐fold; P
Published: 2018
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7. A Mix of Dietary Fibres Changes Interorgan Nutrients Exchanges and Muscle-Adipose Energy Handling in Overfed Mini-Pigs

Author: Ahmed Ben Mohamed, Didier Rémond, Andreu Gual-Grau, Annick Bernalier-Donnadille, Frédéric Capel, Marie-Caroline Michalski, Fabienne Laugerette, Benoit Cohade, Noureddine Hafnaoui, Daniel Béchet, Cécile Coudy-Gandilhon, Marine Gueugneau, Jerome Salles, Carole Migné, Dominique Dardevet, Jérémie David, Sergio Polakof, and Isabelle Savary-Auzeloux
Subjects: overfeeding, dietary fibres, gene expression, SCFA, muscle metabolism, inter-organ metabolism, Nutrition. Foods and food supply, TX341-641
Abstract: This study evaluates the capacity of a bread enriched with fermentable dietary fibres to modulate the metabolism and nutrients handling between tissues, gut and peripheral, in a context of overfeeding. Net fluxes of glucose, lactate, urea, short chain fatty acids (SCFA), and amino acids were recorded in control and overfed female mini-pigs supplemented or not with fibre-enriched bread. SCFA in fecal water and gene expressions, but not protein levels or metabolic fluxes, were measured in muscle, adipose tissue, and intestine. Fibre supplementation increased the potential for fatty acid oxidation and mitochondrial activity in muscle (acox, ucp2, sdha and cpt1-m, p < 0.05) as well as main regulatory transcription factors of metabolic activity such as pparα, pgc-1α and nrf2. All these features were associated with a reduced muscle fibre cross sectional area, resembling to controls (i.e., lean phenotype). SCFA may be direct inducers of these cross-talk alterations, as their feces content (+52%, p = 0.05) was increased in fibre-supplemented mini-pigs. The SCFA effects could be mediated at the gut level by an increased production of incretins (increased gcg mRNA, p < 0.05) and an up-regulation of SCFA receptors (increased gpr41 mRNA, p < 0.01). Hence, consumption of supplemented bread with fermentable fibres can be an appropriate strategy to activate muscle energy catabolism and limit the establishment of an obese phenotype.
Published: 2021
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8. UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin

Author: Dulce Peris-Moreno, Mélodie Malige, Agnès Claustre, Andrea Armani, Cécile Coudy-Gandilhon, Christiane Deval, Daniel Béchet, Pierre Fafournoux, Marco Sandri, Lydie Combaret, Daniel Taillandier, and Cécile Polge
Subjects: MuRF1/TRIM63, skeletal muscle atrophy, glucocorticoids, UBE2L3/UbcH7, alpha-actin, myosin, Cytology, QH573-671
Abstract: The ubiquitin proteasome system (UPS) is the main player of skeletal muscle wasting, a common characteristic of many diseases (cancer, etc.) that negatively impacts treatment and life prognosis. Within the UPS, the E3 ligase MuRF1/TRIM63 targets for degradation several myofibrillar proteins, including the main contractile proteins alpha-actin and myosin heavy chain (MHC). We previously identified five E2 ubiquitin-conjugating enzymes interacting with MuRF1, including UBE2L3/UbcH7, that exhibited a high affinity for MuRF1 (KD = 50 nM). Here, we report a main effect of UBE2L3 on alpha-actin and MHC degradation in catabolic C2C12 myotubes. Consistently UBE2L3 knockdown in Tibialis anterior induced hypertrophy in dexamethasone (Dex)-treated mice, whereas overexpression worsened the muscle atrophy of Dex-treated mice. Using combined interactomic approaches, we also characterized the interactions between MuRF1 and its substrates alpha-actin and MHC and found that MuRF1 preferentially binds to filamentous F-actin (KD = 46.7 nM) over monomeric G-actin (KD = 450 nM). By contrast with actin that did not alter MuRF1–UBE2L3 affinity, binding of MHC to MuRF1 (KD = 8 nM) impeded UBE2L3 binding, suggesting that differential interactions prevail with MuRF1 depending on both the substrate and the E2. Our data suggest that UBE2L3 regulates contractile proteins levels and skeletal muscle atrophy.
Published: 2021
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9. Magnesium Deficiency Alters Expression of Genes Critical for Muscle Magnesium Homeostasis and Physiology in Mice

Author: Dominique Bayle, Cécile Coudy-Gandilhon, Marine Gueugneau, Sara Castiglioni, Monica Zocchi, Magdalena Maj-Zurawska, Adriana Palinska-Saadi, André Mazur, Daniel Béchet, and Jeanette A. Maier
Subjects: skeletal muscle, magnesium, magnesium transporters, transcriptome, Nutrition. Foods and food supply, TX341-641
Abstract: Chronic Mg2+ deficiency is the underlying cause of a broad range of health dysfunctions. As 25% of body Mg2+ is located in the skeletal muscle, Mg2+ transport and homeostasis systems (MgTHs) in the muscle are critical for whole-body Mg2+ homeostasis. In the present study, we assessed whether Mg2+ deficiency alters muscle fiber characteristics and major pathways regulating muscle physiology. C57BL/6J mice received either a control, mildly, or severely Mg2+-deficient diet (0.1%; 0.01%; and 0.003% Mg2+ wt/wt, respectively) for 14 days. Mg2+ deficiency slightly decreased body weight gain and muscle Mg2+ concentrations but was not associated with detectable variations in gastrocnemius muscle weight, fiber morphometry, and capillarization. Nonetheless, muscles exhibited decreased expression of several MgTHs (MagT1, CNNM2, CNNM4, and TRPM6). Moreover, TaqMan low-density array (TLDA) analyses further revealed that, before the emergence of major muscle dysfunctions, even a mild Mg2+ deficiency was sufficient to alter the expression of genes critical for muscle physiology, including energy metabolism, muscle regeneration, proteostasis, mitochondrial dynamics, and excitation–contraction coupling.
Published: 2021
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10. Muscle Proteomic and Transcriptomic Profiling of Healthy Aging and Metabolic Syndrome in Men

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Christophe Chambon, Julien Verney, Daniel Taillandier, Lydie Combaret, Cécile Polge, Stéphane Walrand, Frédéric Roche, Jean-Claude Barthélémy, Léonard Féasson, and Daniel Béchet
Subjects: skeletal muscle, aging, sarcopenia, metabolic syndrome, proteome, transcriptome, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: (1) Background: Aging is associated with a progressive decline in muscle mass and function. Aging is also a primary risk factor for metabolic syndrome, which further alters muscle metabolism. However, the molecular mechanisms involved remain to be clarified. Herein we performed omic profiling to decipher in muscle which dominating processes are associated with healthy aging and metabolic syndrome in old men. (2) Methods: This study included 15 healthy young, 15 healthy old, and 9 old men with metabolic syndrome. Old men were selected from a well-characterized cohort, and each vastus lateralis biopsy was used to combine global transcriptomic and proteomic analyses. (3) Results: Over-representation analysis of differentially expressed genes (ORA) and functional class scoring of pathways (FCS) indicated that healthy aging was mainly associated with upregulations of apoptosis and immune function and downregulations of glycolysis and protein catabolism. ORA and FCS indicated that with metabolic syndrome the dominating biological processes were upregulation of proteolysis and downregulation of oxidative phosphorylation. Proteomic profiling matched 586 muscle proteins between individuals. The proteome of healthy aging revealed modifications consistent with a fast-to-slow transition and downregulation of glycolysis. These transitions were reduced with metabolic syndrome, which was more associated with alterations in NADH/NAD+ shuttle and β-oxidation. Proteomic profiling further showed that all old muscles overexpressed protein chaperones to preserve proteostasis and myofiber integrity. There was also evidence of aging-related increases in reactive oxygen species but better detoxifications of cytotoxic aldehydes and membrane protection in healthy than in metabolic syndrome muscles. (4) Conclusions: Most candidate proteins and mRNAs identified herein constitute putative muscle biomarkers of healthy aging and metabolic syndrome in old men.
Published: 2021
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11. Mitophagy and Mitochondria Biogenesis Are Differentially Induced in Rat Skeletal Muscles during Immobilization and/or Remobilization

Author: Christiane Deval, Julie Calonne, Cécile Coudy-Gandilhon, Emilie Vazeille, Daniel Bechet, Cécile Polge, Daniel Taillandier, Didier Attaix, and Lydie Combaret
Subjects: immobilization, recovery, mitophagy, microtubules, physical inactivity, skeletal muscle, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Mitochondria alterations are a classical feature of muscle immobilization, and autophagy is required for the elimination of deficient mitochondria (mitophagy) and the maintenance of muscle mass. We focused on the regulation of mitochondrial quality control during immobilization and remobilization in rat gastrocnemius (GA) and tibialis anterior (TA) muscles, which have very different atrophy and recovery kinetics. We studied mitochondrial biogenesis, dynamic, movement along microtubules, and addressing to autophagy. Our data indicated that mitochondria quality control adapted differently to immobilization and remobilization in GA and TA muscles. Data showed i) a disruption of mitochondria dynamic that occurred earlier in the immobilized TA, ii) an overriding role of mitophagy that involved Parkin-dependent and/or independent processes during immobilization in the GA and during remobilization in the TA, and iii) increased mitochondria biogenesis during remobilization in both muscles. This strongly emphasized the need to consider several muscle groups to study the mechanisms involved in muscle atrophy and their ability to recover, in order to provide broad and/or specific clues for the development of strategies to maintain muscle mass and improve the health and quality of life of patients.
Published: 2020
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12. Erratum: Polge, C., et al. UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment. Cells 2018, 7, 214

Author: Cécile Polge, Julien Aniort, Andrea Armani, Agnès Claustre, Cécile Coudy-Gandilhon, Clara Tournebize, Christiane Deval, Lydie Combaret, Daniel Béchet, Marco Sandri, Didier Attaix, and Daniel Taillandier
Subjects: n/a, Cytology, QH573-671
Abstract: Change in author names (order). [...]
Published: 2018
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13. A Proof of Concept to Bridge the Gap between Mass Spectrometry Imaging, Protein Identification and Relative Quantitation: MSI~LC-MS/MS-LF

Author: Laëtitia Théron, Delphine Centeno, Cécile Coudy-Gandilhon, Estelle Pujos-Guillot, Thierry Astruc, Didier Rémond, Jean-Claude Barthelemy, Frédéric Roche, Léonard Feasson, Michel Hébraud, Daniel Béchet, and Christophe Chambon
Subjects: MALDI mass spectrometry imaging, protein identification, label-free quantitation, skeletal muscle, Microbiology, QR1-502
Abstract: Mass spectrometry imaging (MSI) is a powerful tool to visualize the spatial distribution of molecules on a tissue section. The main limitation of MALDI-MSI of proteins is the lack of direct identification. Therefore, this study focuses on a MSI~LC-MS/MS-LF workflow to link the results from MALDI-MSI with potential peak identification and label-free quantitation, using only one tissue section. At first, we studied the impact of matrix deposition and laser ablation on protein extraction from the tissue section. Then, we did a back-correlation of the m/z of the proteins detected by MALDI-MSI to those identified by label-free quantitation. This allowed us to compare the label-free quantitation of proteins obtained in LC-MS/MS with the peak intensities observed in MALDI-MSI. We managed to link identification to nine peaks observed by MALDI-MSI. The results showed that the MSI~LC-MS/MS-LF workflow (i) allowed us to study a representative muscle proteome compared to a classical bottom-up workflow; and (ii) was sparsely impacted by matrix deposition and laser ablation. This workflow, performed as a proof-of-concept, suggests that a single tissue section can be used to perform MALDI-MSI and protein extraction, identification, and relative quantitation.
Published: 2016
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14. When idiopathic male infertility is rooted in maternal malnutrition during the perinatal period in mice

Author: Yuki Muranishi, Laurent Parry, Mélanie Vachette-Dit-Martin, Fabrice Saez, Cécile Coudy-Gandilhon, Pierre Sauvanet, David H Volle, Jérémy Tournayre, Serge Bottari, Francesca Carpentiero, Guillaume Martinez, Jana Muroňová, Jessica Escoffier, Alain Bruhat, Anne-Catherine Maurin, Julien Averous, Christophe Arnoult, Pierre Fafournoux, Céline Jousse, Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Obihiro University of Agriculture and Veterinary Medicine, Génétique, Reproduction et Développement (GReD), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA), 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), CHU Clermont-Ferrand, Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Université Grenoble Alpes (UGA), Service de Chirurgie Digestive et Hépatobiliaire [CHU Clermont-Ferrand], CHU Estaing [Clermont-Ferrand], CHU Clermont-Ferrand-CHU Clermont-Ferrand, Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Centre Hospitalier Universitaire de Grenoble, UM de Génétique Chromosomique, VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])
Subjects: Adult, Male, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, male fertility, sperm capacitation, 03 medical and health sciences, Mice, 0302 clinical medicine, Pregnancy, Animals, Humans, Lactation, [SDV.BDD]Life Sciences [q-bio]/Development Biology, Infertility, Male, 030304 developmental biology, 0303 health sciences, 030219 obstetrics & reproductive medicine, Malnutrition, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology, Cell Biology, General Medicine, Spermatozoa, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Fertility, Reproductive Medicine, Sperm Motility, Female, nutritional programming, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Abstract: Infertility represents a growing burden worldwide, with one in seven couples presenting difficulties conceiving. Among these, 10–15% of the men have idiopathic infertility that does not correlate with any defect in the classical sperm parameters measured. In the present study, we used a mouse model to investigate the effects of maternal undernutrition on fertility in male progeny. Our results indicate that mothers fed on a low-protein diet during gestation and lactation produce male offspring with normal sperm morphology, concentration, and motility but exhibiting an overall decrease of fertility when they reach adulthood. Particularly, in contrast to control, sperm from these offspring show a remarkable lower capacity to fertilize oocytes when copulation occurs early in the estrus cycle relative to ovulation, due to an altered sperm capacitation. Our data demonstrate for the first time that maternal nutritional stress can have long-term consequences on the reproductive health of male progeny by affecting sperm physiology, especially capacitation, with no observable impact on spermatogenesis and classical quantitative and qualitative sperm parameters. Moreover, our experimental model could be of major interest to study, explain, and ultimately treat certain categories of infertilities.
Published: 2022

15. A Mix of Dietary Fibres Changes Interorgan Nutrients Exchanges and Muscle-Adipose Energy Handling in Overfed Mini-Pigs

Author: Savary-Auzeloux, Ahmed Ben Mohamed, Didier Rémond, Andreu Gual-Grau, Annick Bernalier-Donnadille, Frédéric Capel, Marie-Caroline Michalski, Fabienne Laugerette, Benoit Cohade, Noureddine Hafnaoui, Daniel Béchet, Cécile Coudy-Gandilhon, Marine Gueugneau, Jerome Salles, Carole Migné, Dominique Dardevet, Jérémie David, Sergio Polakof, and Isabelle
Subjects: digestive, oral, and skin physiology, overfeeding, dietary fibres, gene expression, SCFA, muscle metabolism, inter-organ metabolism, obesity, food and beverages
Abstract: This study evaluates the capacity of a bread enriched with fermentable dietary fibres to modulate the metabolism and nutrients handling between tissues, gut and peripheral, in a context of overfeeding. Net fluxes of glucose, lactate, urea, short chain fatty acids (SCFA), and amino acids were recorded in control and overfed female mini-pigs supplemented or not with fibre-enriched bread. SCFA in fecal water and gene expressions, but not protein levels or metabolic fluxes, were measured in muscle, adipose tissue, and intestine. Fibre supplementation increased the potential for fatty acid oxidation and mitochondrial activity in muscle (acox, ucp2, sdha and cpt1-m, p < 0.05) as well as main regulatory transcription factors of metabolic activity such as pparα, pgc-1α and nrf2. All these features were associated with a reduced muscle fibre cross sectional area, resembling to controls (i.e., lean phenotype). SCFA may be direct inducers of these cross-talk alterations, as their feces content (+52%, p = 0.05) was increased in fibre-supplemented mini-pigs. The SCFA effects could be mediated at the gut level by an increased production of incretins (increased gcg mRNA, p < 0.05) and an up-regulation of SCFA receptors (increased gpr41 mRNA, p < 0.01). Hence, consumption of supplemented bread with fermentable fibres can be an appropriate strategy to activate muscle energy catabolism and limit the establishment of an obese phenotype.
Published: 2021
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16. Maternal nutritional stress alters sperm competence in male mice offspring leading to reduced fertility

Author: Serge Bottari, Francesca Carpentiero, Anne-Catherine Maurin, Christophe Arnoult, Cécile Coudy-Gandilhon, Mélanie Vachette-dit-Martin, Fabrice Saez, Pierre Fafournoux, Yuki Muranishi, Jessica Escoffier, Céline Jousse, Alain Bruhat, David Volle, Laurent Parry, Julien Averous, Pierre Sauvanet, Jérémy Tournayre, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), and VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Subjects: Infertility, Offspring, media_common.quotation_subject, Fertility, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Andrology, 03 medical and health sciences, 0302 clinical medicine, Capacitation, Lactation, medicine, Ovulation, [SDV.BDD]Life Sciences [q-bio]/Development Biology, 030304 developmental biology, media_common, 0303 health sciences, 030219 obstetrics & reproductive medicine, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology, medicine.disease, Sperm, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], medicine.anatomical_structure, Spermatogenesis, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Abstract: Infertility represents a growing burden worldwide, with one in seven couples presenting difficulties conceiving. Amongst these, 10-15% of the men have idiopathic infertility that does not correlate with any defect in the classical sperm parameters measured. In the present study, we used a mouse model to investigate the effects of maternal undernutrition on fertility in male progeny. Our results indicate that mothers fed on a low protein diet during gestation and lactation produce male offspring with normal sperm morphology, concentration and motility but exhibiting an overall decrease of fertility when they reach adulthood. Particularly, sperm from these offspring show a remarkable lower capacity to fertilize oocytes when copulation occurs early in the estrus cycle relative to ovulation, due to an altered sperm capacitation.Our data demonstrate for the first time that maternal nutritional stress can have long-term consequences on the reproductive health of male progeny by affecting sperm physiology, especially capacitation, with no observable impact on spermatogenesis and classical quantitative and qualitative sperm parameters. Moreover, our experimental model could be of major interest to study, explain, and ultimately treat certain categories of infertilities.
Published: 2021

17. UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin

Author: Polge, Dulce Peris-Moreno, Mélodie Malige, Agnès Claustre, Andrea Armani, Cécile Coudy-Gandilhon, Christiane Deval, Daniel Béchet, Pierre Fafournoux, Marco Sandri, Lydie Combaret, Daniel Taillandier, and Cécile
Subjects: MuRF1/TRIM63, skeletal muscle atrophy, glucocorticoids, UBE2L3/UbcH7, alpha-actin, myosin, ubiquitinating enzymes, contractile proteins, MicroScale-Thermophoresis, macromolecular substances
Abstract: The ubiquitin proteasome system (UPS) is the main player of skeletal muscle wasting, a common characteristic of many diseases (cancer, etc.) that negatively impacts treatment and life prognosis. Within the UPS, the E3 ligase MuRF1/TRIM63 targets for degradation several myofibrillar proteins, including the main contractile proteins alpha-actin and myosin heavy chain (MHC). We previously identified five E2 ubiquitin-conjugating enzymes interacting with MuRF1, including UBE2L3/UbcH7, that exhibited a high affinity for MuRF1 (KD = 50 nM). Here, we report a main effect of UBE2L3 on alpha-actin and MHC degradation in catabolic C2C12 myotubes. Consistently UBE2L3 knockdown in Tibialis anterior induced hypertrophy in dexamethasone (Dex)-treated mice, whereas overexpression worsened the muscle atrophy of Dex-treated mice. Using combined interactomic approaches, we also characterized the interactions between MuRF1 and its substrates alpha-actin and MHC and found that MuRF1 preferentially binds to filamentous F-actin (KD = 46.7 nM) over monomeric G-actin (KD = 450 nM). By contrast with actin that did not alter MuRF1–UBE2L3 affinity, binding of MHC to MuRF1 (KD = 8 nM) impeded UBE2L3 binding, suggesting that differential interactions prevail with MuRF1 depending on both the substrate and the E2. Our data suggest that UBE2L3 regulates contractile proteins levels and skeletal muscle atrophy.
Published: 2021
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18. Association Between Physical Activity, Quadriceps Muscle Performance, and Biological Characteristics of Very Old Men and Women

Author: Léonard Féasson, Thomas Lapole, Frédéric Roche, Jean-Claude Barthélémy, Giorgio Varesco, Marine Gueugneau, Alice Decourt, Cécile Coudy-Gandilhon, Vianney Rozand, Daniel Béchet, Université de Lyon, Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), and Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)
Subjects: Male, Total work, Aging, Vastus lateralis muscle, Physical activity, Physiology, Isometric exercise, Quadriceps Muscle, Oldest old, Isometric Contraction, Medicine, Humans, Knee, Muscle, Skeletal, Exercise, Fatigue, Knee extensors, business.industry, [SDV.MHEP.GEG]Life Sciences [q-bio]/Human health and pathology/Geriatry and gerontology, Quadriceps muscle, Myosin heavy chain 1, Physical activity level, Muscle Fatigue, Female, Geriatrics and Gerontology, business, Force steadiness
Abstract: The aim of the study was to evaluate the association between physical activity, knee extensors (KE) performance (ie, isometric strength and fatigability), and biological parameters (ie, muscle structural, microvascular, and metabolic properties) in healthy very old men and women. Thirty very old adults (82 ± 1 years, 15 women) performed an isometric Quadriceps Intermittent Fatigue (QIF) test for the assessment of KE maximal force, total work (index of absolute performance), and fatigability. Muscle biopsies from the vastus lateralis muscle were collected to assess muscle fibers type and morphology, microvasculature, and enzymes activity. Correlation analyses were used to investigate the relationships between physical activity (steps/day, actimetry), KE performance, and biological data for each sex separately. Men, compared to women, showed greater total work at the QIF test (44 497 ± 8 629 Ns vs 26 946 ± 4 707 Ns; p < .001). Steps per day were correlated with total work only for women (r = 0.73, p = .011). In men, steps per day were correlated with the percentage (r = 0.57, p = .033), shape factor (r = 0.75, p = .002), and capillary tortuosity of type IIX fibers (r = 0.59, p = .035). No other relevant correlations were observed for men or women between steps per day and biological parameters. Physical activity level was positively associated with the capacity of very old women to perform a fatiguing test, but not maximal force production capacity of the KE. Physical activity of very old men was not correlated with muscle performance. We suggest that very old women could be at higher risk of autonomy loss and increasing the steps per day count could provide a sufficient stimulus for adaptations in less active women.
Published: 2021

19. Lipid accumulation and mitochondrial abnormalities are associated with fiber atrophy in skeletal muscle of rats with collagen-induced arthritis

Author: Frédéric Capel, Gaëlle Vial, Fabien Wauquier, Carole Chevenet, Alexandre Pinel, Martin Soubrier, Cécile Coudy-Gandilhon, Yohan Wittrant, Daniel Béchet, Anne Tournadre, Véronique Coxam, Service de rhumatologie, CHU Clermont-Ferrand, Unité de Nutrition Humaine (UNH), Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Laboratoire d'Anatomie et de Cytologie Pathologique, Groupe Hospitalier de l'Institut Catholique de Lille (GHICL), public grant (ARTH-INNOV project) from the European Regional Development Fund (ERDF/FEDER-Region Auvergne), Groupement des Hôpitaux de l'Institut Catholique de Lille (GHICL), Université catholique de Lille (UCL)-Université catholique de Lille (UCL), Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), and Groupement hospitalier de l'Institut Catholique de Lille
Subjects: 0301 basic medicine, Male, medicine.medical_specialty, Sarcopenia, Ubiquitin-Protein Ligases, Freund's Adjuvant, Muscle Fibers, Skeletal, Adipose tissue, Arthritis, Muscle Proteins, Arthritis, Rheumatoid, Rats, Sprague-Dawley, Tripartite Motif Proteins, 03 medical and health sciences, Gastrocnemius muscle, 0302 clinical medicine, Atrophy, Tibialis anterior muscle, Internal medicine, medicine, Animals, Humans, Rats, Wistar, Molecular Biology, Collagen Type II, Triglycerides, SKP Cullin F-Box Protein Ligases, Myogenesis, business.industry, Skeletal muscle, Cell Biology, medicine.disease, Arthritis, Experimental, Lipids, Rats, Mitochondria, PPAR gamma, Muscular Atrophy, 030104 developmental biology, Endocrinology, medicine.anatomical_structure, Adipose Tissue, Muscle, business, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery
Abstract: Epub ahead of print; Rheumatoid arthritis (RA) has a negative impact on muscle mass, and reduces patient's mobility and autonomy. Furthermore, RA is associated with metabolic comorbidities, notably in lipid homeostasis by unknown mechanisms. To understand the links between the loss in muscle mass and the metabolic abnormalities, arthritis was induced in male Sprague Dawley rats (n=11) using the collagen-induced arthritis model. Rats immunized with bovine type II collagen were compared to a control group of animals (n=11) injected with acetic acid and complete Freund's adjuvant. The clinical severity of the ensuing arthritis was evaluated weekly by a semi-quantitative score. Skeletal muscles from the hind limb were used for the histological analysis and exploration of mitochondrial activity, lipid accumulation, metabolism and regenerative capacities A significant atrophy in tibialis anterior muscle fibers was observed in rats with arthritis despite a non-significant decrease in the weight of the muscles. Despite moderate inflammation, accumulation of triglycerides (P
Published: 2020

20. Increased Serpina3n release into circulation during glucocorticoid-mediated muscle atrophy

Author: Dominique Maiter, Donatienne d'Hose, Yann-Gaël Gangloff, Laure B. Bindels, Caroline Barbé, Laurent Schaeffer, Christophe Chambon, Marine Gueugneau, Nathalie M. Delzenne, Daniel Béchet, Cécile Coudy-Gandilhon, Pascale Lause, Marie de Barsy, and Jean-Paul Thissen
Subjects: 0301 basic medicine, medicine.medical_specialty, Myostatin, Muscle hypertrophy, 03 medical and health sciences, Physiology (medical), Internal medicine, Diabetes mellitus, medicine, Myocyte, Orthopedics and Sports Medicine, biology, business.industry, Skeletal muscle, medicine.disease, Muscle atrophy, 3. Good health, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, biology.protein, Biomarker (medicine), medicine.symptom, business, Glucocorticoid, medicine.drug
Abstract: BACKGROUND: Glucocorticoids (GC) play a major role in muscle atrophy. As skeletal muscle is a secretory organ, characterization of the muscle secretome elicited by muscle atrophy should allow to better understand the cellular mechanisms and to identify circulating biomarkers of this condition. Our project aimed to identify the changes in the muscle secretome associated with GC-induced muscle atrophy and susceptible to translate into circulation. METHODS: We have identified the GC-induced changes in the secretome of C2 C12 muscle cells by proteomic analysis, and then, we have determined how these changes translate into the circulation of mice or human subjects exposed to high concentrations of GC. RESULTS: This approach led us to identify Serpina3n as one of the most markedly secreted protein in response to GC. Our original in vitro results were confirmed in vivo by an increased expression of Serpina3n in skeletal muscle (3.9-fold; P < 0.01) and in the serum (two-fold; P < 0.01) of mice treated with GC. We also observed increased levels of the human orthologue Serpina3 in the serum of Cushing's syndrome patients compared with healthy controls matched for age and sex (n = 9/group, 2.5-fold; P < 0.01). An increase of Serpina3n was also demonstrated in muscle atrophy models mediated by GC such as cancer cachexia (four-fold; P < 0.01), sepsis (12.5-fold; P < 0.001), or diabetes (two-fold; P < 0.01). In contrast, levels of Serpina3n both in skeletal muscle and in the circulation were reduced in several models of muscle hypertrophy induced by myostatin inhibition (P < 0.01). Furthermore, a cluster of data suggests that the regulation of muscle Serpina3n involves mTOR, an essential determinant of the muscle cell size. CONCLUSIONS: Taken together, these data suggest that Serpina3n may represent a circulating biomarker of muscle atrophy associated to GC and, broadly, a reflection of dynamic changes in muscle mass.
Published: 2018

21. Muscle loss associated changes of oxylipin signatures during biological aging: an exploratory study from the PROOF cohort

Author: Alice Decourt, Cécile Coudy-Gandilhon, Annika I. Ostermann, Thade Konrad, Cécile Gladine, Daniel Béchet, Nils Helge Schebb, Céline Dalle, Léonard Féasson, Frédéric Roche, André Mazur, Jean-Claude Barthélémy, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Faculty of Mathematics and Natural Sciences, University of Wuppertal, University of Veterinary Medicine Hanover, Service de Physiologie Clinique et de l'Exercice, Faculté de Médecine Jacques Lisfranc, PRES Université de Lyon, Université Jean Monnet (Saint-Etienne), Université de Lyon, Service de Neurologie, Centre Hospitalier du Pays d'Aix, Laboratoire Interuniversitaire de Biologie de la Motricité (LIBM ), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), German Resaerch Foundation SCHE 1801Fondation Caisse d'Epargne Rhone-Alpes (CERA) 30French government IDEX-ISITE initiative 16-IDEX-0001 CAP 20-25French Ministry of Health, ProdInra, Archive Ouverte, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Institute for Food Toxicology, University of Veterinary Medicine, Chair of Food Chemistry, Faculty of Mathematics and Natural Sciences, service de chirurgie cardiaque, Centre Hospitalier Universitaire Gabriel Montpied, Service de Physiologie Clinique et de l'Exercice, CHU Nord, Faculté de Médecine Jacques Lisfranc, Unité de Myologie, Centre Référent Maladies Neuromusculaires Rares Rhône-Alpes, Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Institute for Food Toxicology and Analytical Chemistry, University of Veterinary Medicine Hannover, Unité de Myologie, Centre Hospitalier Universitaire de Saint-Etienne, Service de Physiologie Clinique et de l'Exercice [CHU de Saint-Etienne], Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)-Université Jean Monnet - Saint-Étienne (UJM), Université Jean Monnet - Saint-Étienne (UJM), Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), Université Catholique de Louvain (UCLouvain). BEL., CHU Gabriel Montpied [Clermont-Ferrand], CHU Clermont-Ferrand-CHU Clermont-Ferrand, Institut Multidisciplinaire de Biochimie des Lipides (IMBL). FRA., Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), ANR-16-IDEX-0001,CAP 20-25,CAP 20-25(2016), Unité de Nutrition Humaine - Clermont Auvergne ( UNH ), Université Clermont Auvergne ( UCA ) -Institut national de la recherche agronomique [Auvergne/Rhône-Alpes] ( INRA Auvergne/Rhône-Alpes ), and Centre Hospitalier Universitaire de Saint-Etienne ( CHU de Saint-Etienne )
Subjects: 0301 basic medicine, Male, Aging, Sarcopenia, [CHIM.ANAL] Chemical Sciences/Analytical chemistry, [ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition, Lipid mediators, Inflammation, medicine.disease_cause, Bioinformatics, analyse métabolomique, 03 medical and health sciences, 0302 clinical medicine, Metabolomics, Absorptiometry, Photon, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, medicine, Humans, Longitudinal Studies, Oxylipins, Prospective Studies, perte de muscle, Aged, 80 and over, business.industry, Lipid signaling, vieillissement, Oxylipin, medicine.disease, [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition, 030104 developmental biology, oxylipine, Ageing, ageing, Cohort, Eicosanoids, Female, Geriatrics and Gerontology, medicine.symptom, business, étude de cohorte, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress, Biomarkers
Abstract: L’Unité de Nutrition Humaine (UNH - Clermont-Ferrand) organise cette année avec l’aide du laboratoire CarMeN (Lyon) la 18ème éditionL’Unité de Nutrition Humaine (UNH - Clermont-Ferrand) organise cette année avec l’aide du laboratoire CarMeN (Lyon) la 18ème édition; Characterizations of the multiple mechanisms determining biological aging are required tobetter understand the etiology and identify early biomarkers of sarcopenia. Oxylipins are a largefamily of signaling lipids involved in the regulation of various biological processes that becomedysregulated during aging.To investigate whether comprehensive oxylipin profiling could provide an integrated and finecharacterisation of the early phases of sarcopenia, we performed a quantitative targetedmetabolomics of oxylipins in plasma of 81-year old subjects from the PROOF cohort withdecreased (n=12), stable (n=16) or increased appendicular muscle mass (n=14).Multivariate and univariate analyses identified significant and concordant changes of oxylipinprofiles according to the muscle status. Of note, 90% of the most discriminant oxylipins werederived from EPA and DHA and were increased in the sarcopenic subjects. The oxylipinssignatures of sarcopenic subjects revealed subtle activation of inflammatory resolutionpathways, coagulation processes and oxidative stress and the inhibition of angiogenesis. Heatmaps highlighted relationships between oxylipins and the cardiometabolic health parameterswhich were mainly lost in sarcopenic subjects.This exploratory study supports that targeted metabolomics of oxylipins could provide relevantand subtle characterization of early disturbances associated with muscle-loss during aging.
Published: 2019

22. A mix of dietary fermentable fibers improves lipids handling by the liver of overfed minipigs

Author: Daniel Béchet, Didier Rémond, Jérémie David, Michel Hébraud, Isabelle Savary-Auzeloux, Noureddine Hafnaoui, Benoit Cohade, Ahmed Ben Mohamed, Sergio Polakof, Christophe Chambon, Frédéric Capel, Dominique Dardevet, Joël Doré, Carole Migné, Thierry Sayd, Cécile Coudy-Gandilhon, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Microbiologie Environnement Digestif Santé - Clermont Auvergne (MEDIS), INRA Clermont-Ferrand-Theix-Université Clermont Auvergne (UCA), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Microbiologie Environnement Digestif Santé (MEDIS), INRA Clermont-Ferrand-Theix-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), INRA, France (AlimH research department), INRA, France (CEPIA research department), and INRA, France (MICA research department)
Subjects: 0301 basic medicine, Sucrose, Endocrinology, Diabetes and Metabolism, Clinical Biochemistry, fibre alimentaire, Biochemistry, chemistry.chemical_compound, Overnutrition, 0302 clinical medicine, Nonalcoholic fatty liver disease, mini-pig proteomic, Resistant starch, protéomique, 2. Zero hunger, Nutrition and Dietetics, Short-chain fatty acid, dietary fibre, Inulin, dietary fiber, foie, Lipogenesis, Pectins, Swine, Miniature, Female, medicine.medical_specialty, food.ingredient, short chain fatty acid, 030209 endocrinology & metabolism, Carbohydrate metabolism, Diet, High-Fat, liver, acide gras à chaîne courte, 03 medical and health sciences, food, proteomics, lipid, Internal medicine, medicine, Animals, Molecular Biology, lipide, Cholesterol, Proteins, swine, Metabolism, Fatty Acids, Volatile, Lipid Metabolism, medicine.disease, fibre fermentescible, 030104 developmental biology, Endocrinology, Gene Expression Regulation, chemistry, Fermentation, liver function tests, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, porc
Abstract: Obesity induced by overfeeding ultimately can lead to nonalcoholic fatty liver disease, whereas dietary fiber consumption is known to have a beneficial effect. We aimed to determine if a supplementation of a mix of fibers (inulin, resistant starch and pectin) could limit or alleviate overfeeding-induced metabolic perturbations. Twenty female minipigs were fed with a control diet (C) or an enriched fat/sucrose diet supplemented (O + F) or not (O) with fibers. Between 0 and 56 days of overfeeding, insulin (+88%), HOMA (+102%), cholesterol (+45%) and lactate (+63%) were increased, without any beneficial effect of fibers supplementation. However, fibers supplementation limited body weight gain (vs. O, −15% at D56) and the accumulation of hepatic lipids droplets induced by overfeeding. This could be explained by a decreased lipids transport potential (−50% FABP1 mRNA, O + F vs. O) inducing a down-regulation of regulatory elements of lipids metabolism / lipogenesis (−36% SREBP1c mRNA, O + F vs. O) but not to an increased oxidation (O + F not different from O and C for proteins and mRNA measured). Glucose metabolism was also differentially regulated by fibers supplementation, with an increased net hepatic release of glucose in the fasted state (diet × time effect, P
Published: 2019

23. Beneficial effects of endurance exercise training on skeletal muscle microvasculature in sickle cell disease patients

Author: Pablo Bartolucci, Frédéric Galactéros, Léonard Féasson, Thomas Rupp, Cécile Coudy-Gandilhon, Laurent Messonnier, Barnabas Gellen, Daniel Béchet, Angèle N. Merlet, Laboratoire Interuniversitaire de Biologie de la Motricité, Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), ELSAN-Polyclinique de Poitiers, CHU Henri Mondor, CHU Henri Mondor AP-HP/UPEC, CHU de St Etienne, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), CHU Henri Mondor [Créteil], and Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)
Subjects: medicine.medical_specialty, Vastus lateralis muscle, Anemia, Immunology, education, 030204 cardiovascular system & hematology, Biochemistry, law.invention, Incremental exercise, 03 medical and health sciences, 0302 clinical medicine, Randomized controlled trial, Endurance training, law, Internal medicine, Biopsy, medicine, 030304 developmental biology, 0303 health sciences, medicine.diagnostic_test, business.industry, Skeletal muscle, Cell Biology, Hematology, medicine.disease, 3. Good health, Hemoglobinopathy, medicine.anatomical_structure, Cardiology, business, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Epub ahead of print; Sickle cell disease (SCD) is a genetic hemoglobinopathy leading to two major clinical manifestations: severe chronic hemolytic anemia and iterative vaso-occlusive crises. SCD is also accompanied by profound muscle microvascular remodeling. The beneficial effects of endurance training on microvasculature are widely known. The aim of this study was to evaluate the effects of an endurance training program on microvasculature of skeletal muscle in SCD patients. A biopsy of the vastus lateralis muscle and submaximal incremental exercise were performed before and after the training period. Of the forty randomized SCD patients, complete data sets from 32 were obtained. The training group (n=15) followed a personalized moderate-intensity endurance training program, while the non-training (n=17) group maintained a normal lifestyle. Training consisted of three 40-minute cycle ergometer exercise sessions per week for 8 weeks. Histological analysis highlighted microvascular benefits in the training SCD patients compared to non-training patients, including increases in capillary density (CD) (P = .003), number of capillaries around a fiber (CAF) (P = .015) and functional exchange surface (LC/PF) (P < .0001). Conversely, no significant between-group difference was found in the morphology of capillaries. Indexes of physical ability also improved in the training patients. The moderate-intensity endurance exercise training program improved the muscle capillary network and partly reversed the microvascular defects commonly observed in skeletal muscle of SCD patients. This trial was registered at www.clinicaltrials.gov as #NCT02571088.
Published: 2019

24. Abstracts of the 7th Cachexia Conference, Kobe/Osaka, Japan, December 9-11, 2013 (Part 2)

Author: Cécile Polge, Didier Attaix, Huijuan Wang, Lydie Combaret, Anne Listrat, Daniel Taillandier, Cécile Coudy-Gandilhon, Kijoon Lee, Claire Lethias, Bruno Meunier, Daniel Béchet, Marine Gueugneau, and Kheng Lim Goh
Subjects: 0303 health sciences, Stromal cell, TUNEL assay, Angiogenesis, Chemistry, Skeletal muscle, 030204 cardiovascular system & hematology, musculoskeletal system, medicine.disease, Article, Cell biology, 03 medical and health sciences, Gastrocnemius muscle, 0302 clinical medicine, Atrophy, medicine.anatomical_structure, Apoptosis, Physiology (medical), Sarcopenia, medicine, Orthopedics and Sports Medicine, 030304 developmental biology
Abstract: Summary The age-related loss of skeletal muscle mass and function (sarcopenia) is a consistent hallmark of ageing. Apoptosis plays an importantroleinmuscleatrophy,andtheintentofthisstudywasto specify whether apoptosis is restricted to myofibre nuclei (myonuclei)oroccursinsatellitecellsorstromalcellsofextracellularmatrix (ECM). Sarcopenia in mouse gastrocnemius muscle was characterized by myofibre atrophy, oxidative type grouping, delocalization of myonuclei and ECM fibrosis. Terminal deoxynucleotidyl transferase-mediated dUTP nick end-labelling (TUNEL) indicated a sharp rise in apoptosis during ageing. TUNEL coupled with immunostaining for dystrophin, paired box protein-7 (Pax7) or laminin-2a, respectively, was used to identify apoptosis in myonuclei, satellite cells and stromal cells. In adult muscle, apoptosis was not detected inmyofibres,butwasrestrictedtostromalcells.Moreover,theagerelated rise in apoptotic nuclei was essentially due to stromal cells. Myofibre-associatedapoptosisneverthelessoccurredinoldmuscle, but represented < 20% of the total muscle apoptosis. Specifically, apoptosis in old muscle affected a small proportion (0.8%) of the myonuclei, buta large part (46%)of the Pax7 + satellite cells. TUNEL coupled with CD31 immunostaining further attributed stromal apoptosis to capillary endothelial cells. Age-dependent rise in apoptotic capillary endothelial cells was concomitant with altered levelsofkeyangiogenicregulators,perlecanandaperlecandomain V (endorepellin) proteolytic product. Collectively, our results indicate that sarcopenia is associated with apoptosis of satellite cells and impairment of capillary functions, which is likely to contribute to the decline in muscle mass and functionality during ageing.
Published: 2014

25. A Proof of Concept to Bridge the Gap between Mass Spectrometry Imaging, Protein Identification and Relative Quantitation: MSI~LC-MS/MS-LF

Author: Michel Hébraud, Frédéric Roche, Thierry Astruc, Christophe Chambon, Cécile Coudy-Gandilhon, Laetitia Théron, Delphine Centeno, Léonard Féasson, Didier Rémond, Jean-Claude Barthélémy, Estelle Pujos-Guillot, Daniel Béchet, Tissus animaux, nutrition, digestion, écosystème et métabolisme (TANDEM), Institut National de la Recherche Agronomique (INRA)-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-INP. Ecole Nationale Supérieure Agronomique de Toulouse, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Service de Physiologie Clinique et de l’Exercice, Faculté de Médecine Jacques Lisfranc, Biologie, Ingénierie et Imagerie de la Greffe de Cornée (EA 2521, JE2521, IFR143), Université Jean Monnet [Saint-Étienne] (UJM), Laboratoire Interuniversitaire de Biologie de la Motricité (LIBM ), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Microbiologie Equipe Qualité et Sécurité des Aliments (INRA), Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Plateforme d'Exploration du Métabolisme, Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM), Plateforme Exploration du Métabolisme (PFEM), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-MetaboHUB-Clermont, MetaboHUB-MetaboHUB, Service de Physiologie Clinique et de l'Exercice [CHU de Saint-Etienne], Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)-Université Jean Monnet - Saint-Étienne (UJM), Biologie, Ingénierie et Imagerie pour l'Ophtalmologie (BIIO), Université Jean Monnet - Saint-Étienne (UJM), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), SECurité des ALIments et Microbiologie, and Institut National de la Recherche Agronomique (INRA)-École nationale d'ingénieurs des techniques des industries agricoles et alimentaires (ENITIAA)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)
Subjects: 0301 basic medicine, [SDV]Life Sciences [q-bio], Clinical Biochemistry, MALDI mass spectrometry imaging, protein identification, label-free quantitation, skeletal muscle, lcsh:QR1-502, Biochemistry, Article, Mass spectrometry imaging, lcsh:Microbiology, Matrix (chemical analysis), 03 medical and health sciences, Structural Biology, spectrométrie de masse, Lc ms ms, Protein purification, Molecular Biology, neoplasms, ComputingMilieux_MISCELLANEOUS, Chromatography, Laser ablation, Chemistry, muscle squelettique, digestive system diseases, quantification, Label-free quantification, 030104 developmental biology, Tissue sections, protéine, identification, Protein identification
Abstract: International audience; Mass spectrometry imaging (MSI) is a powerful tool to visualize the spatial distribution of molecules on a tissue section. The main limitation of MALDI-MSI of proteins is the lack of direct identification. Therefore, this study focuses on a MSI~LC-MS/MS-LF workflow to link the results from MALDI-MSI with potential peak identification and label-free quantitation, using only one tissue section. At first, we studied the impact of matrix deposition and laser ablation on protein extraction from the tissue section. Then, we did a back-correlation of the m/z of the proteins detected by MALDI-MSI to those identified by label-free quantitation. This allowed us to compare the label-free quantitation of proteins obtained in LC-MS/MS with the peak intensities observed in MALDI-MSI. We managed to link identification to nine peaks observed by MALDI-MSI. The results showed that the MSI~LC-MS/MS-LF workflow (i) allowed us to study a representative muscle proteome compared to a classical bottom-up workflow; and (ii) was sparsely impacted by matrix deposition and laser ablation. This workflow, performed as a proof-of-concept, suggests that a single tissue section can be used to perform MALDI-MSI and protein extraction, identification, and relative quantitation.
Published: 2016

26. Lower skeletal muscle capillarization in hypertensive elderly men

Author: Frédéric Roche, Léonard Féasson, Bruno Meunier, Daniel Béchet, Daniel Taillandier, Cécile Coudy-Gandilhon, Marine Gueugneau, Lydie Combaret, Cécile Polge, Jean-Claude Barthélémy, Didier Attaix, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Unité Mixte de Recherches sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA), Service de Physiologie Clinique et de l Exercice, CHU Nord, Faculté de Medecine Jacques Lisfranc, Université Jean Monnet (Saint-Etienne), Centre de Référence des Maladies Neuromusculaires Rares, Unité de Myologie, Centre Hospitalier Universitaire (CHU), Laboratoire de Physiologie de l'Exercice EA4338 (LPE), Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Institut de recherche Expérimentale et Clinique-Pôle d'Endocrinologie, Diabétologie, et Nutrition (EDIN), Université Catholique de Louvain (UCL), Laboratoire Interuniversitaire de Biologie de la Motricité (LIBM ), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Fondation Caisse d'Epargne Rhone-Alpes 30, European Union Collaborative Project MyoAge EC-Fp7 CT-223576, Region Auvergne, Fonds Europeens de Developpement Regional (FEDER) 23000422, Unité de Nutrition Humaine ( UNH ), Institut National de la Recherche Agronomique ( INRA ) -Université d'Auvergne - Clermont-Ferrand I ( UdA ) -Clermont Université, Unité Mixte de Recherches sur les Herbivores ( UMR 1213 Herbivores ), VetAgro Sup ( VAS ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique ( INRA ), Centre Hospitalier Universitaire ( CHU ), Laboratoire de Physiologie de l'Exercice, Université de Lyon, Université Catholique de Louvain ( UCL ), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Université Catholique de Louvain = Catholic University of Louvain (UCL), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Service de Physiologie Clinique et de l'Exercice [CHU de Saint-Etienne], Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)-Université Jean Monnet - Saint-Étienne (UJM), Laboratoire de Physiologie de l'Exercice (LPE), Université Jean Monnet - Saint-Étienne (UJM), and Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])
Subjects: Male, Biopsy, [ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition, Muscle Fibers, Skeletal, 030204 cardiovascular system & hematology, Biochemistry, capillary, Extracellular matrix, 0302 clinical medicine, Endocrinology, Fibrosis, medicine.diagnostic_test, [SDV.MHEP.GEG]Life Sciences [q-bio]/Human health and pathology/Geriatry and gerontology, Age Factors, muscle fiber, Extracellular Matrix, medicine.anatomical_structure, Lower Extremity, medicine.medical_specialty, hypertension, Neovascularization, Physiologic, [ SDV.MHEP.GEG ] Life Sciences [q-bio]/Human health and pathology/Geriatry and gerontology, metabolic syndrome, Electron Transport Complex IV, sarcopenia, 03 medical and health sciences, Young Adult, Sex Factors, Internal medicine, Genetics, medicine, Humans, Risk factor, Muscle, Skeletal, Molecular Biology, Aged, business.industry, aging, Skeletal muscle, Cell Biology, medicine.disease, Endomysium, Capillaries, Sarcopenia, Metabolic syndrome, business, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery
Abstract: The authors wish to gratefully acknowledge Professor Philippe Courpron for his central role in initiating this work. The authors are grateful to the Fondation pour l'Université de Lyon for assistance with obtaining reagents; Aging strongly affects the skeletal muscle and is associated with microvascular dysfunctions. Age is also a primary risk factor for the metabolic syndrome, which is a cluster of metabolic and cardiovascular symptoms. Among the metabolic syndrome components, hypertension is the most prevalent in elderly subjects and has a central role in vascular alterations. Despite critical clinical outcomes, the effects of hypertension and metabolic syndrome on skeletal muscle capillarization have poorly been investigated during aging. In the present study, muscle biopsies from normotensive young (YO) and elderly (ELc) men, and elderly men with hypertension (EL-HT) or metabolic syndrome (EL-MS) were assessed for the number of capillaries around a fiber (CAF), capillary-to-fiber perimeter exchange (CFPE), length of contact to perimeter of fiber ratio (LC/PF), capillary tortuosity, and for extracellular matrix (ECM) embedding capillaries. As capillarization and muscle mitochondrial oxidative capacity may be associated, we also investigated cytochrome c oxidase (COX) content. Our findings indicate that capillarization and COX did not change between normotensive adult and old individuals. They further reveal that hypertension in elderly men is associated with reduced CAF (ELc: 5.2 +/- 0.4, EL-HT: 4.1 +/- 0.2, P < 0.02 for type I fibers; ELc: 4.1 +/- 0.2, EL-HT: 3.1 +/- 0.3, P < 0.03 for type IIA fibers), CFPE (ELc: 7.9 +/- 0.7, EL-HT: 6.4 +/- 0.4 capillaries/1000 mu m, P < 0.03 for type I fibers; ELc: 6.5 +/- 0.4, EL-HT: 5.2 +/- 0.4 capillaries/1000 mu m, P < 0.03 for type IIA fibers), LC/PF (ELc: 23.3 +/- 1.2, EL-HT: 17.8 +/- 0.6%, P < 0.01 for type I fibers; ELc: 19.8 +/- 1.1, EL-HT: 15.6 +/- 0.8%, P < 0.01 for type IIA fibers) and capillary tortuosity, and with ECM endomysium fibrosis. Capillary rarefaction also correlated with lower COX content in the old hypertensive muscle. No further modification occurred with metabolic syndrome in elderly men. Collectively, our results suggest that hypertension plays a central role in muscle capillarization during aging, and that the other components of metabolic syndrome do not make major additional changes in the aged skeletal muscle capillary network
Published: 2016

27. Les fibres alimentaires limitent le stockage de lipides hépatiques en situation de surnutrition : quels mécanismes et quels médiateurs ?

Author: Hubert Chiron, Sergio Polakof, Daniel Béchet, Dominique Dardevet, Didier Rémond, Isabelle Savary-Auzeloux, B. Cohade, Cécile Coudy-Gandilhon, A.B. Mohamed, G. Della-valle, Joël Doré, and J. David
Subjects: Nutrition and Dietetics, Endocrinology, Diabetes and Metabolism, Internal Medicine
Abstract: Introduction et but de l’etude Alors que l’obesite peut s’expliquer par une surnutrition et l’ingestion de regimes riches en graisses et sucres, l’ingestion de fibres alimentaires est connue pour favoriser la perte de poids [1] . Notre etude vise a determiner si, en situation d’apport alimentaire superieur aux besoins (alimentation de type occidentale generant de l’obesite), les fibres alimentaires peuvent limiter l’apparition des deregulations metaboliques via notamment une reorganisation de l’utilisation des nutriments dans l’aire splanchnique (ASP : foie + tube digestif [TD]). Materiel et methodes Quatorze Miniporcs sont multicatheterises en artere, veine porte et veine sus-hepatique pour mesurer les flux nets de nutriments au travers de l’ASP. Les animaux ont ete nourris 60 jours avec un regime en surnutrition (14 911 kJ/j EM) supplemente en pain enrichi (F) (+ 2291 kj/j EM) ou non (T) (+ 2438 kj/j EM) en fibres (inuline, pectine, amidon resistant). Des prelevements sanguins ont ete realises a jeun apres 1, 14 et 60 jours de regime T ou F, ainsi que des prelevements tissulaires a l’euthanasie. Des analyses plasmatiques (AGCC, glucose, lactate, acides amines) et hepatiques (histologie : red oil) ont ete effectuees. Les flux nets des nutriments par l’ASP ont ete calcules par difference arterioveineuse. Les effets regimes/cinetiques ont ete evaluees par ANOVA a mesures repetees, signification p Resultats et analyse statistique A j60, le contenu lipidique dans le foie est inferieur chez F vs T (−33,6 % ; p Parmi les facteurs pouvant expliquer les changements dans l’utilisation des nutriments energetiques entre T et F, on constate une emission des AGCC par le TD superieure chez F vs T uniquement a j14, liee a la degradation des fibres solubles dans le colon. Or, les AGCC sont connus pour reguler les voies du metabolisme energetique via une action sur GPR41-43 [2] . Neanmoins, l’effet des fibres perdurant a j60, des mediateurs relais ou des regulations a long terme doivent s’etre mis en place. Conclusion La supplementation en fibres alimentaires limite le stockage des lipides dans le foie en situation de surnutrition. Cet effet pourrait etre medie dans les phases precoces du developpement des deregulations metaboliques par les AGCC via une alteration de la repartition des nutriments energetiques entre le foie et les tissus peripheriques. Pour analyser cette hypothese, des expressions de genes, des analyses de proteomique et des activites enzymatiques du metabolisme energetico-azote (foie, muscle, tissu adipeux) sont en cours.
Published: 2018

28. Skeletal muscle lipid content and oxidative activity in relation to muscle fiber type in aging and metabolic syndrome

Author: Cécile Polge, Daniel Béchet, Léonard Féasson, Daniel Taillandier, Frédéric Roche, Bruno Meunier, Brigitte Picard, Lydie Combaret, Didier Attaix, Cécile Coudy-Gandilhon, Jean-Claude Barthélémy, Christiane Barboiron, Julien Verney, Laetitia Théron, Marine Gueugneau, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Centre de Recherche en Nutrition Humaine, Unité Mixte de Recherches sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Centre Référent Maladies Neuromusculaires Rares Rhône-Alpes, Unité de Myologie, Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Laboratoire de Physiologie de l'Exercice EA4338 (LPE), Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Université de Lyon, Hôpital Nord - Faculté de MédecineJacques Lisfranc, Service de Physiologie Clinique et de l'Exercice, PRES Université de Lyon, Université Jean Monnet (Saint-Etienne), Hôpital Nord - Faculté de Médecine Jacques Lisfranc, Service de Physiologie Clinique et de l'Exercice, Unité de Nutrition Humaine (UNH), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Unité de Nutrition Humaine - Clermont Auvergne ( UNH ), Université Clermont Auvergne ( UCA ) -Institut national de la recherche agronomique [Auvergne/Rhône-Alpes] ( INRA Auvergne/Rhône-Alpes ), Unité Mixte de Recherches sur les Herbivores ( UMR 1213 Herbivores ), VetAgro Sup ( VAS ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique ( INRA ), Institut d'Enseignement Supérieur et de Recherche en Alimentation, Santé Animale, Sciences Agronomiques et de l'Environnement, Centre Hospitalier Universitaire de Saint-Etienne ( CHU de Saint-Etienne ), Laboratoire de Physiologie de l'Exercice EA4338, Université de Lyon (COMUE), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), Laboratoire de Physiologie de l'Exercice (LPE), Université Jean Monnet - Saint-Étienne (UJM), Service de Physiologie Clinique et de l'Exercice [CHU de Saint-Etienne], and Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)-Université Jean Monnet - Saint-Étienne (UJM)
Subjects: Male, Sarcopenia, medicine.medical_specialty, masse musculaire, [ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition, Biopsy, lipid droplets, Muscle Fibers, Skeletal, metabolic syndrome, Electron Transport Complex IV, Young Adult, Absorptiometry, Photon, Atrophy, Internal medicine, Lipid droplet, Humans, Medicine, Cytochrome c oxidase, Muscle Strength, Intramyocellular lipids, skeletal muscle, Aged, syndrome métabolique, biology, business.industry, aging, fiber types, Skeletal muscle, metabolic x syndrome, vieillissement, Lipid Metabolism, medicine.disease, Endocrinology, medicine.anatomical_structure, muscle mass, Ageing, ageing, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Body Composition, biology.protein, teneur en lipides, oil content, Geriatrics and Gerontology, Metabolic syndrome, Energy Metabolism, business, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Abstract: One of the most noticeable effects of aging is the reduction in skeletal muscle mass and strength (sarcopenia). The metabolic syndrome (MS) is also prevalent in old subjects, but its relevance to skeletal muscle characteristics has poorly been investigated. Immunohistochemical studies were performed with muscle biopsies from young (22 years) and old (73 years) men with and without MS to reveal age-dependent and MS-associated modifications of fiber-type characteristics. Atrophy of type II fibers and altered fiber shape characterized muscle aging in lean healthy men. In contrast, increased cross-sectional area of the most abundant type I and type IIA fibers, and reduced cytochrome c oxidase content in all fiber types, characterized MS. Aging and particularly MS were associated with accumulation of intramyocellular lipid droplets. Although lipids mostly accumulated in type I fibers, matrix-assisted laser desorption/ionization–mass spectrometry imaging of intramyocellular lipids did not distinguish fiber types, but clearly separated young, old, and MS subjects. In conclusion, our study suggests that MS in the elderly persons is associated with alterations in skeletal muscle at a fiber-type specific level. Overall, these fiber type-specific modifications may be important both for the age-related loss of muscle mass and strength and for the increased prevalence of MS in elderly subjects.
Published: 2015

29. Proteomics of muscle chronological ageing in post-menopausal women

Author: Cécile Polge, Gillian Butler-Browne, Lydie Combaret, Christophe Chambon, Cécile Coudy-Gandilhon, Daniel Taillandier, Marine Gueugneau, Daniel Béchet, Ophélie Gourbeyre, Andrea B. Maier, Didier Attaix, Bertrand Friguet, Vieillissement Cellulaire Intégré et Inflammation (VCII), Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), European Union Collaborative Project MyoAge [EC Fp7 CT-223576], Fondation Caisse d'Epargne Rhone-Alpes (CERA Sarcopenie) [30], Region Auvergne, Fonds Europeens de Developpement Regional (FEDER) [23000422], FEDER [35380 T2a 2011 Prenusa], European Project: 223576,EC:FP7:HEALTH,FP7-HEALTH-2007-B,MYOAGE(2009), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Béchet, Daniel, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Internal medicine, MOVE Research Institute, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: Proteomics, Sarcopenia, Aging, Cytoplasm, Skeletal muscle, Sarcomere, Myosin, protéome, Cytotoxins, Muscles, muscle squelettique, Blood Proteins, Middle Aged, Muscle atrophy, atrophie musculaire, Cell biology, Mitochondria, Postmenopause, medicine.anatomical_structure, Alimentation et Nutrition, femme menopausée, Female, medicine.symptom, biomarqueur, Biotechnology, Muscle contraction, Research Article, Human, Signal Transduction, Sarcomeres, Ageing, Biomarkers, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, sarcopenie, Genetics, medicine, Food and Nutrition, Humans, Muscle, Skeletal, Aged, Lipid Metabolism, Electrophoreses, Cytoskeletal Proteins, Oxidative Stress, Proteostasis, Proteolysis, Myofibril, Energy Metabolism, Transcriptome
Abstract: International audience; Background: Muscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the mechanisms involved are complex and likely result from the alteration of a variety of interrelated functions. In order to better understand the molecular mechanisms underlying muscle chronological ageing in human, we have undertaken a top-down differential proteomic approach to identify novel biomarkers after the fifth decade of age. Results: Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. Overall, 1919 protein spots were matched between all individuals, 95 were differentially expressed and identified by mass spectrometry, and they corresponded to 67 different proteins. Our results suggested important modifications in cytosolic, mitochondrial and lipid energy metabolism, which may relate to dysfunctions in old muscle force generation. A fraction of the differentially expressed proteins were linked to the sarcomere and cytoskeleton (myosin light-chains, troponin T, ankyrin repeat domain-containing protein-2, vinculin, four and a half LIM domain protein-3), which may account for alterations in contractile properties. In line with muscle contraction, we also identified proteins related to calcium signal transduction (calsequestrin-1, sarcalumenin, myozenin-1, annexins). Muscle ageing was further characterized by the differential regulation of several proteins implicated in cytoprotection (catalase, peroxiredoxins), ion homeostasis (carbonic anhydrases, selenium-binding protein 1) and detoxification (aldo-keto reductases, aldehyde dehydrogenases). Notably, many of the differentially expressed proteins were central for proteostasis, including heat shock proteins and proteins involved in proteolysis (valosin-containing protein, proteasome subunit beta type-4, mitochondrial elongation factor-Tu). Conclusions: This study describes the most extensive proteomic analysis of muscle ageing in humans, and identified 34 new potential biomarkers. None of them were previously recognized as differentially expressed in old muscles, and each may represent a novel starting point to elucidate the mechanisms of muscle chronological ageing in humans.
Published: 2014

30. Sarcopénie : définitions et contradictions - Approches histologique et moléculaire

Author: Daniel Bechet, Marine Gueugneau, Cécile Coudy-Gandilhon, Laetitia Theron, Unité de Nutrition Humaine (UNH), and Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université
Subjects: [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract: National audience
Published: 2014

31. Apoptosis in capillary endothelial cells in ageing skeletal muscle

Author: Claire Lethias, Cécile Coudy-Gandilhon, Daniel Béchet, Kijoon Lee, Lydie Combaret, Anne Listrat, Didier Attaix, Huijuan Wang, Bruno Meunier, Cécile Polge, Marine Gueugneau, Kheng Lim Goh, Daniel Taillandier, Unité de Nutrition Humaine (UNH), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305 (LBTI), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), School of Chemical and Biomedical Engineering, Nanyang Technological University [Singapour], School of Mechanical and Systems Engineering, Newcastle University International Singapore (NUIS), NTU Academic Research Fund (AcRF) Tier 1 [RG37/07], Egide Merlion [5.03.07], European Commission MyoAge [EC Fp7 CT-223756], Fondation Caisse d'Epargne Rhone Alpes (CERA), Fondation Rhone Alpes Futur, NTU, Conseil Regional Auvergne, Fonds Europeens de Developpement Regional (FEDER), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Unité Mixte de Recherches sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Unité de Nutrition Humaine ( UNH ), Clermont Université-Université d'Auvergne - Clermont-Ferrand I ( UdA ) -Institut National de la Recherche Agronomique ( INRA ), Unité Mixte de Recherches sur les Herbivores ( UMR 1213 Herbivores ), VetAgro Sup ( VAS ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique ( INRA ), Laboratoire de Biologie Tissulaire et d'ingénierie Thérapeutique UMR 5305 ( LBTI ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Newcastle University International Singapore ( NUIS ), and Béchet, Daniel
Subjects: Male, Pathology, Aging, satellite stem cell, Angiogenesis, Muscle Fibers, Skeletal, souris, [ SDV.BA ] Life Sciences [q-bio]/Animal biology, angiogenesis, 0302 clinical medicine, Animal biology, 0303 health sciences, TUNEL assay, [SDV.BA]Life Sciences [q-bio]/Animal biology, digestive, oral, and skin physiology, apoptosis, Tenascin, vieillissement, musculoskeletal system, Cell biology, atrophie musculaire, medicine.anatomical_structure, muscle mass, muscular atrophy, dystrophine, hormones, hormone substitutes, and hormone antagonists, medicine.medical_specialty, Stromal cell, mice, Satellite Cells, Skeletal Muscle, myofibre, masse musculaire, activité anti apoptotique, matrice extracellulaire, Médecine humaine et pathologie, Biology, sarcopenia, 03 medical and health sciences, Gastrocnemius muscle, Atrophy, sarcopenie, cellule satellite, [ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathology, Biologie animale, fonctionnement, medicine, Animals, Muscle, Skeletal, 030304 developmental biology, Cell Nucleus, cellule stromale, Engineering::Bioengineering [DRNTU], Skeletal muscle, Endothelial Cells, Cell Biology, Original Articles, medicine.disease, Mice, Inbred C57BL, Apoptosis, ageing, Sarcopenia, Human health and pathology, Stromal Cells, Extracellular Space, cellule endotheliale, 030217 neurology & neurosurgery, Heparan Sulfate Proteoglycans, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, squelette
Abstract: International audience; The age-related loss of skeletal muscle mass and function (sarcopenia) is a consistent hallmark of ageing. Apoptosis plays an important role in muscle atrophy, and the intent of this study was to specify whether apoptosis is restricted to myofibre nuclei (myonuclei) or occurs in satellite cells or stromal cells of extracellular matrix (ECM). Sarcopenia in mouse gastrocnemius muscle was characterized by myofibre atrophy, oxidative type grouping, delocalization of myonuclei and ECM fibrosis. Terminal deoxynucleotidyl transferase-mediated dUTP nick end-labelling (TUNEL) indicated a sharp rise in apoptosis during ageing. TUNEL coupled with immunostaining for dystrophin, paired box protein-7 (Pax7) or laminin-2α, respectively, was used to identify apoptosis in myonuclei, satellite cells and stromal cells. In adult muscle, apoptosis was not detected in myofibres, but was restricted to stromal cells. Moreover, the age-related rise in apoptotic nuclei was essentially due to stromal cells. Myofibre-associated apoptosis nevertheless occurred in old muscle, but represented < 20% of the total muscle apoptosis. Specifically, apoptosis in old muscle affected a small proportion (0.8%) of the myonuclei, but a large part (46%) of the Pax7(+) satellite cells. TUNEL coupled with CD31 immunostaining further attributed stromal apoptosis to capillary endothelial cells. Age-dependent rise in apoptotic capillary endothelial cells was concomitant with altered levels of key angiogenic regulators, perlecan and a perlecan domain V (endorepellin) proteolytic product. Collectively, our results indicate that sarcopenia is associated with apoptosis of satellite cells and impairment of capillary functions, which is likely to contribute to the decline in muscle mass and functionality during ageing.
Published: 2013

32. Etude protéomique du vieillissement musculaire chez la femme post-ménopausée

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Christophe Chambon, Brigitte Picard, Bijislma, A., Maier, A., Didier Attaix, Butler-Browne, G., Daniel Bechet, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Department of Gerontology and Geriatrics, Leiden University Medical Center (LUMC), UMRS974, Université Pierre et Marie Curie - Paris 6 (UPMC), U974, Institut National de la Santé et de la Recherche Médicale (INSERM), UMR7215, Centre National de la Recherche Scientifique (CNRS), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre de recherche en Myologie – U974 SU-INSERM, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), ProdInra, Migration, and Universiteit Leiden-Universiteit Leiden
Subjects: [SDV] Life Sciences [q-bio], sarcopenie, [SDV]Life Sciences [q-bio], femme menopausée, [INFO]Computer Science [cs], [SHS] Humanities and Social Sciences, vieillissement, [INFO] Computer Science [cs], protéomique, [SHS]Humanities and Social Sciences
Abstract: Organisateurs : Laboratoire de recherche en Cardiovasculaire, Mét abolisme, Diabétologie et Nutrition ( CarMeN) ; Unité de Nutrition Humaine ( UNH ) ; Laboratoire de Bioénergétique Fondamentale et Appliquée ( LBFA); National audience; Introduction et Méthodes : Une approche protéomique a été développée afin identifier de nouveaux biomarqueurs du vieillissement musculaire (sarcopénie). Des extraits totaux et sarcoplasmiques ont été préparés à partir de femmes ménopausées matures (54 ans) et âgées (78 ans). Sur un total de 1919 spots, 133 sont exprimés de façon différentielle chez les femmes âgées par rapport aux femmes matures, et la spectrométrie de masse (nanoLC-MS/MS) a permis d’identifier 74 protéines différentes. Résultats : On observe d'importantes modifications du métabolisme énergétique cytosolique (TPIS, PYGM, GPDA, créatine-kinase) et mitochondrial (pyruvate-déshydrogénase, aconitase, COX, NADH-déshydrogénase). Certaines protéines différentiellement exprimées correspondent à des protéines myofibrillaires (myosine light-chaînes, troponines T, myozenin). Tout ceci peut expliquer les modifications des propriétés contractiles chez la personne âgée. Les autres protéines montrent des perturbations dans les processus de cytoprotection et de détoxification, comme une régulation différentielle de plusieurs chaperons moléculaires (HSPA9, HSPA1A), l'homéostasie ionique (sélénium-binding protein) et le stress du réticulum endoplasmique (sarcalumenin, calséquestrine). De plus, l’expression de protéines impliquées dans la protéolyse est augmentée (VCP, UBA1, Calpain Small subunit-1). Nous avons aussi remarqué une régulation négative des protéines impliquées dans l’édition de l’ARN (apobec2) et la traduction mitochondriale (TuFM). Conclusion : Plusieurs biomarqueurs identifiés dans cette analyse étaient auparavant non reconnus comme différentiellement exprimés dans le muscle âgé, et peuvent représenter de nouveaux points de départ pour élucider certains des mécanismes de la sarcopénie.
Published: 2013

33. Effets du syndrome métabolique sur les fibres musculaires chez l'homme âgé

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Bruno Meunier, Christiane Barboiron, Anne Listrat, Jean-Claude Barthelemy, Léonard Feasson, Brigitte Picard, Daniel Bechet, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Physiologie Clinique et Exercice, Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), Université Jean Monnet - Saint-Étienne (UJM), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Université Jean Monnet [Saint-Étienne] (UJM), and VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
Subjects: [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, ComputingMilieux_MISCELLANEOUS
Abstract: National audience
Published: 2012

34. Etude protéomique du vieillissement musculaire chez la femme post-ménopausée

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Christophe Chambon, Bijislma, A., Maier, A., Cécile Polge, Lydie Combaret, Daniel Taillandier, Didier Attaix, Gillian Butler-Browne, Brigitte Picard, Daniel Bechet, Unité de Nutrition Humaine (UNH), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Department of Gerontology and Geriatrics, Leiden University Medical Center (LUMC), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Universiteit Leiden-Universiteit Leiden, Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), and VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
Subjects: [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, ComputingMilieux_MISCELLANEOUS
Abstract: National audience
Published: 2012

35. Proteomics of skeletal muscle aging in women

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Christophe Chambon, Astrid Bijlsma, Andrea Maier, Gillian Butler- Browne, Brigitte Picard, Daniel Béchet, ProdInra, Archive Ouverte, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Qualité des Produits Animaux (QuaPA), Institut National de la Recherche Agronomique (INRA), Unité Mixte de Recherches sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA), Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, and Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
Subjects: [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition, education, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, reproductive and urinary physiology, health care economics and organizations, humanities
Abstract: Proteomics of skeletal muscle aging in women. 2nd MYOAGE symposium: The aging human muscle: An integrated machinery
Published: 2012

36. Age-related variation in the Framework and composition of skeletal muscle ECM

Author: Huijuan Wang, Daniel Bechet, Bruno Meunier, Cécile Coudy-Gandilhon, Lee, K., Kheng Lim Goh, Lethias, C., Anne Listrat, Unité de Recherches sur les Herbivores (URH), Institut National de la Recherche Agronomique (INRA), Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Société Française de Biologie de la Matrice Extracellulaire (SFBME). FRA., Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université-Institut National de la Recherche Agronomique (INRA), and ProdInra, Migration
Subjects: [SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], [INFO]Computer Science [cs], [SHS] Humanities and Social Sciences, [INFO] Computer Science [cs], ComputingMilieux_MISCELLANEOUS, [SHS]Humanities and Social Sciences
Abstract: National audience

37. Cellular and functional mechanisms underlying muscle aging and associated diseases

Author: Marine Gueugneau, Cécile Coudy-Gandilhon, Frédéic Roche, Jean-Claude Barthélémy, Léonard Féasson, Daniel Béchet, Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Service de Physiologie Clinique et de l’Exercice, Faculté de Médecine Jacques Lisfranc, Université Jean Monnet (Saint-Etienne), Unité de Myologie, Centre Référent Maladies Neuromusculaires Rares Rhône-Alpes, Laboratoire de Physiologie de l'Exercice EA4338 (LPE), Université Jean Monnet [Saint-Étienne] (UJM)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry]), Université de Lyon, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Service de Physiologie Clinique et de l'Exercice [CHU de Saint-Etienne], Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E)-Université Jean Monnet - Saint-Étienne (UJM), Université Jean Monnet - Saint-Étienne (UJM), and Laboratoire de Physiologie de l'Exercice (LPE)
Subjects: body regions, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, musculoskeletal system, human activities, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Abstract: The loss of skeletal muscle mass and function during the aging process (sarcopenia) has a major impact on muscle function and is a key component of frailty. A clear understanding of the mechanisms of sarcopenia through the identification of selective biomarkers, and thus of potential therapeutic targets, is of paramount importance in ensuring quality of life in old age. This presentation will provide an overview of the studies associating immunohistology and omics investigations during sarcopenia and associated pathologies in humans.

38. UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment.

Author: Cécile P, Julien A, Andrea A, Agnès C, Cécile CG, Clara T, Christiane D, Lydie C, Daniel B, Marco S, Didier A, and Daniel T
Abstract: Skeletal muscle mass is reduced during many diseases or physiological situations (disuse, aging), which results in decreased strength and increased mortality. Muscle mass is mainly controlled by the ubiquitin-proteasome system (UPS), involving hundreds of ubiquitinating enzymes (E2s and E3s) that target their dedicated substrates for subsequent degradation. We recently demonstrated that MuRF1, an E3 ubiquitin ligase known to bind to sarcomeric proteins (telethonin, α-actin, myosins) during catabolic situations, interacts with 5 different E2 enzymes and that these E2-MuRF1 couples are able to target telethonin, a small sarcomeric protein, for degradation. Amongst the E2s interacting with MuRF1, E2E1 was peculiar as the presence of the substrate was necessary for optimal MuRF1-E2E1 interaction. In this work, we focused on the putative role of E2E1 during skeletal muscle atrophy. We found that E2E1 expression was restricted to type I and type IIA muscle fibers and was not detectable in type IIB fibers. This strongly suggests that E2E1 targets are fiber-specific and may be strongly linked to the contractile and metabolic properties of the skeletal muscle. However, E2E1 knockdown was not sufficient for preserving the protein content in C2C12 myotubes subjected to a catabolic state (dexamethasone treatment), suggesting that E2E1 is not involved in the development of muscle atrophy. By contrast, E2E1 knockdown aggravated the atrophying process in both catabolic C2C12 myotubes and the Tibialis anterior muscle of mice, suggesting that E2E1 has a protective effect on muscle mass.
Published: 2018
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