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13 results on '"Mayeuf-Louchart A"'

1. MuscleJ2: a rebuilding of MuscleJ with new features for high-content analysis of skeletal muscle immunofluorescence slides.

Author

Danckaert A, Trignol A, Le Loher G, Loubens S, Staels B, Duez H, Shorte SL, and Mayeuf-Louchart A

Subjects
Fluorescent Antibody Technique, Muscle Fibers, Skeletal, Software, Muscle, Skeletal, Satellite Cells, Skeletal Muscle
Abstract

Histological analysis of skeletal muscle is of major interest for understanding its behavior in different pathophysiological conditions, such as the response to different environments or myopathies. In this context, many software programs have been developed to perform automated high-content analysis. We created MuscleJ, a macro that runs in ImageJ/Fiji on batches of images. MuscleJ is a multianalysis tool that initially allows the analysis of muscle fibers, capillaries, and satellite cells. Since its creation, it has been used in many studies, and we have further developed the software and added new features, which are presented in this article. We converted the macro into a Java-language plugin with an improved user interface. MuscleJ2 provides quantitative analysis of fibrosis, vascularization, and cell phenotype in whole muscle sections. It also performs analysis of the peri-myonuclei, the individual capillaries, and any staining in the muscle fibers, providing accurate quantification within regional sublocalizations of the fiber. A multicartography option allows users to visualize multiple results simultaneously. The plugin is freely available to the muscle science community., (© 2023. BioMed Central Ltd., part of Springer Nature.)

Published
2023
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2. NR1D1 controls skeletal muscle calcium homeostasis through myoregulin repression.

Author

Boulinguiez A, Duhem C, Mayeuf-Louchart A, Pourcet B, Sebti Y, Kondratska K, Montel V, Delhaye S, Thorel Q, Beauchamp J, Hebras A, Gimenez M, Couvelaere M, Zecchin M, Ferri L, Prevarskaya N, Forand A, Gentil C, Ohana J, Piétri-Rouxel F, Bastide B, Staels B, Duez H, and Lancel S

Subjects
Animals, Homeostasis, Mice, Mice, Inbred mdx, Nuclear Receptor Subfamily 1, Group D, Member 1 genetics, Sarcoplasmic Reticulum metabolism, Calcium metabolism, Muscle, Skeletal metabolism
Abstract

The sarcoplasmic reticulum (SR) plays an important role in calcium homeostasis. SR calcium mishandling is described in pathological conditions, such as myopathies. Here, we investigated whether the nuclear receptor subfamily 1 group D member (NR1D1, also called REV-ERBα) regulates skeletal muscle SR calcium homeostasis. Our data demonstrate that NR1D1 deficiency in mice impaired sarco/endoplasmic reticulum calcium ATPase-dependent (SERCA-dependent) SR calcium uptake. NR1D1 acts on calcium homeostasis by repressing the SERCA inhibitor myoregulin through direct binding to its promoter. Restoration of myoregulin counteracted the effects of NR1D1 overexpression on SR calcium content. Interestingly, myoblasts from patients with Duchenne muscular dystrophy displayed lower NR1D1 expression, whereas pharmacological NR1D1 activation ameliorated SR calcium homeostasis and improved muscle structure and function in dystrophic mdx/Utr+/- mice. Our findings demonstrate that NR1D1 regulates muscle SR calcium homeostasis, pointing to its therapeutic potential for mitigating myopathy.

Published
2022
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3. [The muscle biological clock].

Author

Mayeuf-Louchart A

Subjects
Animals, Circadian Clocks drug effects, Circadian Rhythm drug effects, Circadian Rhythm physiology, Energy Metabolism drug effects, Energy Metabolism physiology, Exercise physiology, Glucocorticoids pharmacology, Humans, Muscle, Skeletal drug effects, Muscle, Skeletal metabolism, Regeneration physiology, Sarcopenia etiology, Sarcopenia physiopathology, Circadian Clocks physiology, Muscle, Skeletal physiology
Abstract

The biological clock plays an essential role in the control of muscle activity, by dissociating temporally the metabolic functions of skeletal muscle. Exercise capacity also displays a circadian rhythm. Alterations in biological rhythm, as in shift workers, alter muscle function and are associated with the development of sarcopenia., (© 2020 médecine/sciences – Inserm.)

Published
2020
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4. Endospanin-2 enhances skeletal muscle energy metabolism and running endurance capacity.

Author

Lancel S, Hesselink MK, Woldt E, Rouillé Y, Dorchies E, Delhaye S, Duhem C, Thorel Q, Mayeuf-Louchart A, Pourcet B, Montel V, Schaart G, Beton N, Picquet F, Briand O, Salles JP, Duez H, Schrauwen P, Bastide B, Bailleul B, Staels B, and Sebti Y

Subjects
Adaptor Proteins, Signal Transducing genetics, Adaptor Proteins, Signal Transducing physiology, Animals, Autophagy, Caloric Restriction, Cell Plasticity genetics, Cells, Cultured, Extracellular Signal-Regulated MAP Kinases metabolism, Female, Humans, Intracellular Signaling Peptides and Proteins, MAP Kinase Signaling System, Male, Membrane Proteins genetics, Mice, Mitochondria metabolism, Muscle Fibers, Fast-Twitch physiology, Muscle Fibers, Slow-Twitch physiology, Muscle, Skeletal cytology, Muscle, Skeletal physiology, Oxidative Stress, Phenotype, Phosphorylation, Physical Exertion, RNA, Messenger metabolism, Energy Metabolism, Membrane Proteins physiology, Muscle, Skeletal metabolism, Physical Endurance physiology
Abstract

Metabolic stresses such as dietary energy restriction or physical activity exert beneficial metabolic effects. In the liver, endospanin-1 and endospanin-2 cooperatively modulate calorie restriction-mediated (CR-mediated) liver adaptations by controlling growth hormone sensitivity. Since we found CR to induce endospanin protein expression in skeletal muscle, we investigated their role in this tissue. In vivo and in vitro endospanin-2 triggers ERK phosphorylation in skeletal muscle through an autophagy-dependent pathway. Furthermore, endospanin-2, but not endospanin-1, overexpression decreases muscle mitochondrial ROS production, induces fast-to-slow fiber-type switch, increases skeletal muscle glycogen content, and improves glucose homeostasis, ultimately promoting running endurance capacity. In line, endospanin-2-/- mice display higher lipid peroxidation levels, increased mitochondrial ROS production under mitochondrial stress, decreased ERK phosphorylation, and reduced endurance capacity. In conclusion, our results identify endospanin-2 as a potentially novel player in skeletal muscle metabolism, plasticity, and function.

Published
2018
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5. Skeletal muscle functions around the clock.

Author

Mayeuf-Louchart A, Staels B, and Duez H

Subjects
Animals, Eating physiology, Exercise physiology, Humans, Muscle Development physiology, Muscle, Skeletal metabolism, Transcription Factors metabolism, Circadian Clocks physiology, Circadian Rhythm physiology, Muscle, Skeletal physiology, Transcription Factors physiology
Abstract

In mammals, the central clock localized in the central nervous system imposes a circadian rhythmicity to all organs. This is achieved thanks to a well-conserved molecular clockwork, involving interactions between several transcription factors, whose pace is conveyed to peripheral tissues through neuronal and humoral signals. The molecular clock plays a key role in the control of numerous physiological processes and takes part in the regulation of metabolism and energy balance. Skeletal muscle is one of the peripheral organs whose function is under the control of the molecular clock. However, although skeletal muscle metabolism and performances display circadian rhythmicity, the role of the molecular clock in the skeletal muscle has remained unappreciated for years. Peripheral organs such as skeletal muscle, and the liver, among others, can be desynchronized from the central clock by external stimuli, such as feeding or exercise, which impose a new rhythm at the organism level. In this review, we discuss our current understanding of the clock in skeletal muscle circadian physiology, focusing on the control of myogenesis and skeletal muscle metabolism., (© 2015 John Wiley & Sons Ltd.)

Published
2015
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6. Itm2a is a Pax3 target gene, expressed at sites of skeletal muscle formation in vivo.

Author

Lagha M, Mayeuf-Louchart A, Chang T, Montarras D, Rocancourt D, Zalc A, Kormish J, Zaret KS, Buckingham ME, and Relaix F

Subjects
Animals, Cell Nucleus metabolism, Female, Male, Membrane Proteins metabolism, Mice, Mice, Inbred C57BL, Mice, Transgenic, Muscle Development, Muscle, Skeletal cytology, Muscle, Skeletal metabolism, Myogenic Regulatory Factor 5 metabolism, PAX3 Transcription Factor, Satellite Cells, Skeletal Muscle metabolism, Gene Expression Regulation, Developmental, Membrane Proteins genetics, Muscle, Skeletal embryology, Paired Box Transcription Factors metabolism
Abstract

The paired-box homeodomain transcription factor Pax3 is a key regulator of the nervous system, neural crest and skeletal muscle development. Despite the important role of this transcription factor, very few direct target genes have been characterized. We show that Itm2a, which encodes a type 2 transmembrane protein, is a direct Pax3 target in vivo, by combining genetic approaches and in vivo chromatin immunoprecipitation assays. We have generated a conditional mutant allele for Itm2a, which is an imprinted gene, by flanking exons 2-4 with loxP sites and inserting an IRESnLacZ reporter in the 3' UTR of the gene. The LacZ reporter reproduces the expression profile of Itm2a, and allowed us to further characterize its expression at sites of myogenesis, in the dermomyotome and myotome of somites, and in limb buds, in the mouse embryo. We further show that Itm2a is not only expressed in adult muscle fibres but also in the satellite cells responsible for regeneration. Itm2a mutant mice are viable and fertile with no overt phenotype during skeletal muscle formation or regeneration. Potential compensatory mechanisms are discussed.

Published
2013
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7. NR1D1 controls skeletal muscle calcium homeostasis through myoregulin repression

Author

Alexis Boulinguiez, Christian Duhem, Alicia Mayeuf-Louchart, Benoit Pourcet, Yasmine Sebti, Kateryna Kondratska, Valérie Montel, Stéphane Delhaye, Quentin Thorel, Justine Beauchamp, Aurore Hebras, Marion Gimenez, Marie Couvelaere, Mathilde Zecchin, Lise Ferri, Natalia Prevarskaya, Anne Forand, Christel Gentil, Jessica Ohana, France Piétri-Rouxel, Bruno Bastide, Bart Staels, Helene Duez, Steve Lancel, CHU Lille, Récepteurs Nucléaires, Maladies Métaboliques et Cardiovasculaires (RNMCD - U1011), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), European Genomic Institute for Diabetes - FR 3508 (EGID), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U 1003 (PHYCELL), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 (URePSSS), Université d'Artois (UA)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille, Centre de recherche en Myologie – U974 SU-INSERM, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Piétri-Rouxel, France, Récepteurs Nucléaires, Maladies Métaboliques et Cardiovasculaires - U1011 (RNMCD), Institut Européen de Génomique du Diabète - European Genomic Institute for Diabetes - FR 3508 (EGID), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), ANR-16-IDEX-0004,ULNE,ULNE(2016), Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD], Récepteurs Nucléaires, Maladies Métaboliques et Cardiovasculaires [RNMCD - U1011], Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U 1003 [PHYCELL], Inovarion, and Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 (RNMCD)

Subjects
[SDV]Life Sciences [q-bio], Cell Biology, General Medicine, [SDV] Life Sciences [q-bio], Mice, Sarcoplasmic Reticulum, Nuclear Receptor Subfamily 1, Group D, Member 1, Mice, Inbred mdx, Muscle Biology, Animals, Homeostasis, Muscle, Calcium, Muscle, Skeletal
Abstract

International audience; The sarcoplasmic reticulum (SR) plays an important role in calcium homeostasis. SR calcium mishandling is described in pathological conditions, such as myopathies. Here, we investigated whether the nuclear receptor subfamily 1 group D member (NR1D1, also called REV-ERBα) regulates skeletal muscle SR calcium homeostasis. Our data demonstrate that NR1D1 deficiency in mice impaired sarco/endoplasmic reticulum calcium ATPase-dependent (SERCA-dependent) SR calcium uptake. NR1D1 acts on calcium homeostasis by repressing the SERCA inhibitor myoregulin through direct binding to its promoter. Restoration of myoregulin counteracted the effects of NR1D1 overexpression on SR calcium content. Interestingly, myoblasts from patients with Duchenne muscular dystrophy displayed lower NR1D1 expression, whereas pharmacological NR1D1 activation ameliorated SR calcium homeostasis and improved muscle structure and function in dystrophic mdx/Utr+/- mice. Our findings demonstrate that NR1D1 regulates muscle SR calcium homeostasis, pointing to its therapeutic potential for mitigating myopathy.

Published
2022

8. [The muscle biological clock]

Author

Mayeuf-Louchart, Alicia, Récepteurs Nucléaires, Maladies Métaboliques et Cardiovasculaires (RNMCD - U1011), Institut Pasteur de Lille, and Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)

Subjects
Sarcopenia, [SDV]Life Sciences [q-bio], Circadian Clocks, Animals, Humans, Regeneration, Energy Metabolism, Muscle, Skeletal, Exercise, Glucocorticoids, Circadian Rhythm
Abstract

The biological clock plays an essential role in the control of muscle activity, by dissociating temporally the metabolic functions of skeletal muscle. Exercise capacity also displays a circadian rhythm. Alterations in biological rhythm, as in shift workers, alter muscle function and are associated with the development of sarcopenia.L'horloge biologique du muscle.L’horloge biologique joue un rôle essentiel dans le contrôle de l’activité musculaire, en dissociant temporellement les fonctions métaboliques du muscle squelettique. Les capacités musculaires en réponse à l’exercice sont également circadiennes. Des perturbations des rythmes biologiques, telles que celles retrouvées chez les travailleurs postés affectent la fonction musculaire et sont associées au développement de la sarcopénie.

Published
2021

9. Endospanin-2 enhances skeletal muscle energy metabolism and running endurance capacity

Author

Lancel, S. (Steve), Hesselink, M.K. (Matthijs Kc), Woldt, E. (Estelle), Rouille, Y. (Yves), Dorchies, E. (Emilie), Delhaye, S. (Stephane), Duhem, C. (Christian), Thorel, Q. (Quentin), Mayeuf-Louchart, A. (Alicia), Pourcet, B. (Benoit), Montel, V. (Valerie), Schaart, G. (Gert), Beton, N. (Nicolas), Picquet, F. (Florence), Briand, O. (Olivier), Salles, J.P. (Jean Pierre), Duez, H. (Helene), Schrauwen, P. (Patrick), Bastide, B. (Bruno), Bailleul, B. (Bernard), Staels, B. (Bart), Sebti, Y. (Yasmine), Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 (RNMCD), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM), Maastricht University [Maastricht], Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 (URePSSS), Université d'Artois (UA)-Université de Lille-Université du Littoral Côte d'Opale (ULCO), Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), European Project: 694717,H2020-EU.1.1. - EXCELLENT SCIENCE - European Research Council (ERC) ,ImmunoBile(2016), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Université d'Artois (UA)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille, Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Récepteurs nucléaires, maladies cardiovasculaires et diabète (EGID), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Maastricht University Medical Center (MUMC), Centre d’Infection et d’Immunité de Lille (CIIL) - INSERM U1019 - UMR 9017 (CIIL), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - EA 7369 (URePSSS), Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Université d'Artois (UA), Centre de Physiopathologie Toulouse Purpan ex IFR 30 et IFR 150 (CPTP), This research was supported by the European Genomic Institute for Diabetes (EGID, ANR-10-LABX-46) and European Commission, Lille Métropole Communauté Urbaine (to YS), Région Nord Pas-de-Calais/FEDER (to BS), CPER 2011-R3-P12A (to B. Bailleul), a joint Société Francophone du Diabète (SFD)/Menarini research fellowship (to B. Bailleul), EFSD/Lilly research grant and CPER emerging team (to HD), Eurhythdia (to BS and HD), ERC Région Haut de France (to HD), and Pfizer France and Ipsen Beaufour (to JPS). BS hold an ERC advanced grant (no. 694717)., ANR-10-LABX-0046/10-LABX-0046,EGID,EGID Diabetes Pole(2010), Nutrition and Movement Sciences, RS: NUTRIM - R1 - Obesity, diabetes and cardiovascular health, Ondersteunend personeel NTM, Université de Lille, Univ. Artois, Univ. Littoral Côte d’Opale, Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD], Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS], and Centre de Physiopathologie Toulouse Purpan [CPTP]

Subjects
Male, [SDV]Life Sciences [q-bio], Cell Plasticity, Messenger, Skeletal muscle, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], MOUSE, STAT3, Mice, Phosphorylation, Extracellular Signal-Regulated MAP Kinases, Cells, Cultured, Glucose metabolism, Cultured, ACTIVATED PROTEIN-KINASE, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, MITOCHONDRIAL BIOGENESIS, Skeletal, Mitochondria, ERK, Muscle Fibers, Slow-Twitch, Phenotype, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Muscle Fibers, Fast-Twitch, Muscle, Female, PHENOTYPIC ANALYSIS, Research Article, PERMEABILITY TRANSITION, MAP Kinase Signaling System, Cells, Physical Exertion, EXERCISE, Slow-Twitch, Muscle Fibers, Signal Transducing, Animals, Autophagy, Caloric Restriction, Energy Metabolism, Humans, Membrane Proteins, Fast-Twitch, Oxidative Stress, Physical Endurance, RNA, Metabolism, Muscle Biology, RNA, Messenger, Muscle, Skeletal, Adaptor Proteins, Signal Transducing, ELECTRON-TRANSPORT CHAIN
Abstract

International audience; Metabolic stresses such as dietary energy restriction or physical activity exert beneficial metabolic effects. In the liver, endospanin-1 and endospanin-2 cooperatively modulate calorie restriction-mediated (CR-mediated) liver adaptations by controlling growth hormone sensitivity. Since we found CR to induce endospanin protein expression in skeletal muscle, we investigated their role in this tissue. In vivo and in vitro endospanin-2 triggers ERK phosphorylation in skeletal muscle through an autophagy-dependent pathway. Furthermore, endospanin-2, but not endospanin-1, overexpression decreases muscle mitochondrial ROS production, induces fast-to-slow fiber-type switch, increases skeletal muscle glycogen content, and improves glucose homeostasis, ultimately promoting running endurance capacity. In line, endospanin-2-/- mice display higher lipid peroxidation levels, increased mitochondrial ROS production under mitochondrial stress, decreased ERK phosphorylation, and reduced endurance capacity. In conclusion, our results identify endospanin-2 as a potentially novel player in skeletal muscle metabolism, plasticity, and function.

Published
2018

10. Skeletal muscle functions around the clock

Author

Alicia Mayeuf-Louchart, Hélène Duez, and Bart Staels

Subjects
medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, Central nervous system, Circadian clock, Clockwork, Biology, Muscle Development, Eating, Endocrinology, Circadian Clocks, Internal medicine, Internal Medicine, medicine, Animals, Humans, Circadian rhythm, Muscle, Skeletal, Molecular clock, Exercise, Transcription factor, Myogenesis, Skeletal muscle, Circadian Rhythm, medicine.anatomical_structure, Neuroscience, Transcription Factors
Abstract

In mammals, the central clock localized in the central nervous system imposes a circadian rhythmicity to all organs. This is achieved thanks to a well-conserved molecular clockwork, involving interactions between several transcription factors, whose pace is conveyed to peripheral tissues through neuronal and humoral signals. The molecular clock plays a key role in the control of numerous physiological processes and takes part in the regulation of metabolism and energy balance. Skeletal muscle is one of the peripheral organs whose function is under the control of the molecular clock. However, although skeletal muscle metabolism and performances display circadian rhythmicity, the role of the molecular clock in the skeletal muscle has remained unappreciated for years. Peripheral organs such as skeletal muscle, and the liver, among others, can be desynchronized from the central clock by external stimuli, such as feeding or exercise, which impose a new rhythm at the organism level. In this review, we discuss our current understanding of the clock in skeletal muscle circadian physiology, focusing on the control of myogenesis and skeletal muscle metabolism.

Published
2015

11. Rev-erb-α regulates atrophy-related genes to control skeletal muscle mass

Author

Alicia Mayeuf-Louchart, Quentin Thorel, Stéphane Delhaye, Justine Beauchamp, Christian Duhem, Anne Danckaert, Steve Lancel, Benoit Pourcet, Estelle Woldt, Alexis Boulinguiez, Lise Ferri, Mathilde Zecchin, Bart Staels, Yasmine Sebti, and Hélène Duez

Subjects
Mice, Knockout, Transcriptional Activation, Adipogenesis, viruses, lcsh:R, lcsh:Medicine, Cell Differentiation, Article, body regions, Repressor Proteins, Mice, Muscular Atrophy, Liver, Muscular Diseases, Nuclear Receptor Subfamily 1, Group D, Member 1, Autophagy, Animals, lcsh:Q, lcsh:Science, skin and connective tissue diseases, Muscle, Skeletal
Abstract

The nuclear receptor Rev-erb-α modulates hepatic lipid and glucose metabolism, adipogenesis and thermogenesis. We have previously demonstrated that Rev-erb-α is also an important regulator of skeletal muscle mitochondrial biogenesis and function, and autophagy. As such, Rev-erb-α over-expression in skeletal muscle or its pharmacological activation improved mitochondrial respiration and enhanced exercise capacity. Here, in gain- and loss-of function studies, we show that Rev-erb-α also controls muscle mass. Rev-erb-α-deficiency in skeletal muscle leads to increased expression of the atrophy-related genes (atrogenes), associated with reduced muscle mass and decreased fiber size. By contrast, in vivo and in vitro Rev-erb-α over-expression results in reduced atrogenes expression and increased fiber size. Finally, Rev-erb-α pharmacological activation blocks dexamethasone-induced upregulation of atrogenes and muscle atrophy. This study identifies Rev-erb-α as a promising pharmacological target to preserve muscle mass.

Published
2017

12. Notch regulation of myogenic versus endothelial fates of cells that migrate from the somite to the limb

Author

Anne Danckaert, Didier Rocancourt, Frédéric Relaix, Alicia Mayeuf-Louchart, Stéphane D. Vincent, Mounia Lagha, Margaret Buckingham, Bases Génétiques, Moléculaires et Cellulaires du Développement (BGMCD), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Imagerie Dynamique (Plate-Forme) (PFID), Institut Pasteur [Paris] (IP), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Département de Biologie du Développement et Cellules souches - Department of Developmental and Stem Cell Biology, Institut Pasteur [Paris], and VINCENT, Stéphane

Subjects
Male, Cellular differentiation, Genetic Vectors, PAX3, Notch signaling pathway, Mice, Transgenic, [SDV.GEN.GA] Life Sciences [q-bio]/Genetics/Animal genetics, Biology, Muscle Development, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Mice, Skeletal muscle cell differentiation, Cell Movement, medicine, Animals, Paired Box Transcription Factors, Cell Lineage, Progenitor cell, Muscle, Skeletal, PAX3 Transcription Factor, Alleles, Multidisciplinary, Receptors, Notch, Endothelial Cells, Gene Expression Regulation, Developmental, [SDV.BDD.EO] Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Skeletal muscle, Cell Differentiation, Extremities, Forkhead Transcription Factors, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Biological Sciences, musculoskeletal system, Cell biology, Somite, [SDV.GEN.GA]Life Sciences [q-bio]/Genetics/Animal genetics, medicine.anatomical_structure, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Somites, embryonic structures, Immunology, Female, Signal transduction, Signal Transduction
Abstract

Multipotent Pax3-positive (Pax3(+)) cells in the somites give rise to skeletal muscle and to cells of the vasculature. We had previously proposed that this cell-fate choice depends on the equilibrium between Pax3 and Foxc2 expression. In this study, we report that the Notch pathway promotes vascular versus skeletal muscle cell fates. Overactivating the Notch pathway specifically in Pax3(+) progenitors, via a conditional Pax3(NICD) allele, results in an increase of the number of smooth muscle and endothelial cells contributing to the aorta. At limb level, Pax3(+) cells in the somite give rise to skeletal muscles and to a subpopulation of endothelial cells in blood vessels of the limb. We now demonstrate that in addition to the inhibitory role of Notch signaling on skeletal muscle cell differentiation, the Notch pathway affects the Pax3:Foxc2 balance and promotes the endothelial versus myogenic cell fate, before migration to the limb, in multipotent Pax3(+) cells in the somite of the mouse embryo.

Published
2014

13. Itm2a is a Pax3 target gene, expressed at sites of skeletal muscle formation in vivo

Author

Mounia Lagha, Didier Montarras, Antoine Zalc, Kenneth S. Zaret, Jay D. Kormish, Margaret Buckingham, Alicia Mayeuf-Louchart, Didier Rocancourt, Frédéric Relaix, Ted Hung-Tse Chang, Biologie du Développement, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Groupe Myologie, Institut de Myologie, Université Pierre et Marie Curie - Paris 6 (UPMC)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Association française contre les myopathies (AFM-Téléthon)-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)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Association française contre les myopathies (AFM-Téléthon)-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), University of Pennsylvania, This project was supported by funding to FR from the INSERM Avenir Program, Association Française Contre les Myopathies (AFM), Association Institut de Myologie, the Ligue Nationale Contre le Cancer (LNCC), Association pour la Recherche Contre le Cancer (ARC), Fondation pour la Recherche Médicale, Institut National du Cancer (INCa), and from the European Union Seventh Framework Programme in the project ENDOSTEM (grant agreement number 241440). MB’s laboratory was supported by the Pasteur Institute and the CNRS (URA 2578) and by grants from the AFM and the EU 7th PCRD programmes, EuroSyStem (grant agreement number 200720) and Optistem (grant agreement number 223098). ML is currently the recipient of a Human Frontier Science Program (HFSP) fellowship., European Project: 241440,EC:FP7:HEALTH,FP7-HEALTH-2009-single-stage,ENDOSTEM(2010), European Project: 200720,EC:FP7:HEALTH,FP7-HEALTH-2007-A,EUROSYSTEM(2008), European Project: 223098,EC:FP7:HEALTH,FP7-HEALTH-2007-B,OPTISTEM(2009), Institut Pasteur [Paris]-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)-Association française contre les myopathies (AFM-Téléthon)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-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)-Association française contre les myopathies (AFM-Téléthon)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), University of Pennsylvania [Philadelphia], Adele, Sarah, Activation of vasculature associated stem cells and muscle stem cells for the repair and maintenance of muscle tissue - ENDOSTEM - - EC:FP7:HEALTH2010-01-01 - 2014-12-31 - 241440 - VALID, European Consortium for Systematic Stem Cell Biology - EUROSYSTEM - - EC:FP7:HEALTH2008-03-01 - 2012-08-31 - 200720 - VALID, and Optimization of stem cell therapy for clinical trials of degenerative skin and muscle diseases - OPTISTEM - - EC:FP7:HEALTH2009-01-01 - 2013-12-31 - 223098 - VALID

Subjects
Male, Embryology, Mouse, Mutant, PAX3, lcsh:Medicine, Gene Expression, Muscle Development, Cell Fate Determination, Mice, 0302 clinical medicine, Molecular Cell Biology, Paired Box Transcription Factors, lcsh:Science, 0303 health sciences, Multidisciplinary, Myogenesis, Stem Cells, Gene Expression Regulation, Developmental, Animal Models, medicine.anatomical_structure, 030220 oncology & carcinogenesis, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Female, Myogenic Regulatory Factor 5, Research Article, Satellite Cells, Skeletal Muscle, Cre recombinase, Mice, Transgenic, Biology, 03 medical and health sciences, Model Organisms, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Genetics, Animals, Muscle, Skeletal, Transcription factor, PAX3 Transcription Factor, 030304 developmental biology, Cell Nucleus, lcsh:R, Skeletal muscle, Membrane Proteins, Molecular biology, Mice, Inbred C57BL, lcsh:Q, Genomic imprinting, Chromatin immunoprecipitation, Organism Development, Animal Genetics, Developmental Biology
Abstract

International audience; The paired-box homeodomain transcription factor Pax3 is a key regulator of the nervous system, neural crest and skeletal muscle development. Despite the important role of this transcription factor, very few direct target genes have been characterized. We show that Itm2a, which encodes a type 2 transmembrane protein, is a direct Pax3 target in vivo, by combining genetic approaches and in vivo chromatin immunoprecipitation assays. We have generated a conditional mutant allele for Itm2a, which is an imprinted gene, by flanking exons 2-4 with loxP sites and inserting an IRESnLacZ reporter in the 3' UTR of the gene. The LacZ reporter reproduces the expression profile of Itm2a, and allowed us to further characterize its expression at sites of myogenesis, in the dermomyotome and myotome of somites, and in limb buds, in the mouse embryo. We further show that Itm2a is not only expressed in adult muscle fibres but also in the satellite cells responsible for regeneration. Itm2a mutant mice are viable and fertile with no overt phenotype during skeletal muscle formation or regeneration. Potential compensatory mechanisms are discussed.

Published
2012

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