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5. Rev-erb-α controls skeletal muscle calcium homeostasis through myoregulin repression: implications in Duchenne Muscular Dystrophy

Author

Benoit Pourcet, Mathilde Zecchin, Kondratska K, Stéphane Delhaye, Piétri-Rouxel F, Montel, Alicia Mayeuf-Louchart, Bastide B, Lise Ferri, Alexis Boulinguiez, Quentin Thorel, Forand A, Hebras A, Natalia Prevarskaya, Christian Duhem, Yasmine Sebti, Steve Lancel, Bart Staels, Justine Beauchamp, Hélène Duez, Couvelaere M, Matías Giménez, and Christel Gentil

Subjects
Calcium metabolism, SERCA, Chemistry, Duchenne muscular dystrophy, chemistry.chemical_element, Skeletal muscle, Calcium, medicine.disease, Cell biology, medicine.anatomical_structure, Nuclear receptor, medicine, Myocyte, medicine.symptom, Myopathy
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 Rev-erb-α regulates skeletal muscle SR calcium homeostasis. Our data demonstrate that Rev-erbα invalidation in mice impairs SERCA-dependent SR calcium uptake. Rev-erb-α acts on calcium homeostasis by repressing the SERCA inhibitor Myoregulin, through direct binding to its promoter. Restoration of Myoregulin counteracts the effects of REV-ERB-α overexpression on SR calcium content. Interestingly, myoblasts from Duchenne myopathy patients display downregulated REV-ERBα expression, whereas pharmacological Rev-erb activation ameliorates SR calcium homeostasis, and improves muscle structure and function in dystrophic mdx/Utr+/- mice. Our findings demonstrate that Rev-erb-α regulates muscle SR calcium homeostasis, pointing to its therapeutic interest for mitigating myopathy.

Published
2021

8. Expression and functional properties of four slow skeletal troponin T isoforms in rat muscles

Author

Kischel, P., Bastide, B., Muller, M., Dubail, F., Offredi, F., Jin, J.P., Mounier, Y., and Martial, J.

Subjects
Atrophy, Muscular -- Research, Atrophy, Muscular -- Physiological aspects, Muscle cells -- Research, Muscle cells -- Physiological aspects, Biological sciences
Abstract

We investigated the expression and functional properties of slow skeletal troponin T (sTnT) isoforms in rat skeletal muscles. Four sTnT cDNAs were cloned from the slow soleus muscle. Three isoforms were found to be similar to sTnT1, sTnT2, and sTnT3 isoforms described in mouse muscles. A new rat isoform, with a molecular weight slightly higher than that of sTnT3, was discovered. This fourth isoform had never been detected previously in any skeletal muscle and was therefore called sTnTx. From both expression pattern and functional measurements, it appears that sTnT isoforms can be separated into two classes, high-molecular-weight (sTnT1, sTnT2) and low-molecular-weight (sTnTx, sTnT3) isoforms. By comparison to the apparent migration pattern of the four recombinant sTnT isoforms, the newly described low-molecular-weight sTnTx isoform appeared predominantly and typically expressed in fast skeletal muscles, whereas the higher-molecular-weight isoforms were more abundant in slow soleus muscle. The relative proportion of the sTnT isoforms in the soleus was not modified after exposure to hindlimb unloading (HU), known to induce a functional atrophy and a slow-to-fast isoform transition of several myofibrillar proteins. Functional data gathered from replacement of endogenous troponin complexes in skinned muscle fibers showed that the sTnT isoforms modified the [Ca.sup.2+] activation characteristics of single skeletal muscle fibers, with sTnT2 and sTnT1 conferring a similar increase in [Ca.sup.2+] affinity higher than that caused by low-molecular-weight isoforms sTnTx and sTnT3. Thus we show for the first time the presence of sTnT in fast muscle fibers, and our data show that the changes in neuromuscular activity on HU are insufficient to alter the sTnT expression pattern. skinned fibers; skeletal muscle; troponin subunit exchange; hindlimb unloading; atrophy

Published
2005

22. 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

25. Characterizing Coherent Wind Structures using Large-Scale Particle Tracking Velocimetry: A Proof-of-Principle Study

Author

Rosi, G. A., Bastide, B. la, Gäbler, Julia, Kinzel, M., and Rival, D. E.

Subjects
ddc:530
Abstract

The following study proposes a two-dimensional large-scale particle tracking velocimetry (LS-PTV) system to characterize coherent wind structures. Seven minutes of LS-PTV data is collected via an apparatus that seeds fog-filled soap bubbles into the wind at a height of 6m from the ground. The LS-PTV data is compared to 20 minutes of data collected concurrently from a wind mast at the same site. The LS-PTV system recorded a mean streamwise velocity of 1.35m/s with a standard deviation of 0.23m/s at a mean height of 2.50m with a standard deviation of 0.7m, which agrees well with the velocity profile measured by the wind mast. Furthermore, the Reynolds stresses measured by the LS-PTV system are found to compare to those measured by the wind mast and by Klebanoff [1] for a canonical turbulent boundary layer. The current study assumes that the centre-of-curvature trajectories of the particle pathlines are representative of the trajectories followed by the spanwise vortices. As a proof-of-principle study, this work has been successful in accurately describing the vortex distribution very near to the ground. However, the trajectories followed by the centres-of- curvat.ure belonging to pathlines concurrently passing through the field-of-view were sporadic and uncorrelated.

Published
2014

26. A feasability study of color flow doppler vectorization for automated blood flow monitoring.

Author

Schorer, R., Badoual, A., Bastide, B., Vandebrouck, A., Licker, M., and Sage, D.

Abstract

An ongoing issue in vascular medicine is the measure of the blood flow. Catheterization remains the gold standard measurement method, although non-invasive techniques are an area of intense research. We hereby present a computational method for real-time measurement of the blood flow from color flow Doppler data, with a focus on simplicity and monitoring instead of diagnostics. We then analyze the performance of a proof-of-principle software implementation. We imagined a geometrical model geared towards blood flow computation from a color flow Doppler signal, and we developed a software implementation requiring only a standard diagnostic ultrasound device. Detection performance was evaluated by computing flow and its determinants (flow speed, vessel area, and ultrasound beam angle of incidence) on purposely designed synthetic and phantom-based arterial flow simulations. Flow was appropriately detected in all cases. Errors on synthetic images ranged from nonexistent to substantial depending on experimental conditions. Mean errors on measurements from our phantom flow simulation ranged from 1.2 to 40.2% for angle estimation, and from 3.2 to 25.3% for real-time flow estimation. This study is a proof of concept showing that accurate measurement can be done from automated color flow Doppler signal extraction, providing the industry the opportunity for further optimization using raw ultrasound data. [ABSTRACT FROM AUTHOR]

Published
2017
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31. The role of the Ca2+ regulatory sites of skeletal troponin C in modulating muscle fibre reactivity to the Ca2+ sensitizer bepridil

Author

Kischel, P, Bastide, B, Potter, J D, and Mounier, Y

Subjects
Male, Binding Sites, Dose-Response Relationship, Drug, Vasodilator Agents, Bepridil, Muscle Fibers, Skeletal, DNA, Recombinant, In Vitro Techniques, musculoskeletal system, Rats, Mice, Muscle Fibers, Slow-Twitch, Strontium, Papers, Muscle Fibers, Fast-Twitch, Mutation, Animals, Protein Isoforms, Calcium, Rabbits, Rats, Wistar, Muscle, Skeletal, Troponin C
Abstract

1. The Ca(2+)-sensor protein troponin C (TnC) exerts a key role in the regulation of muscle contraction, and constitutes a target for Ca(2+) sensitizer compounds, such as bepridil, known to increase its apparent Ca(2+) affinity. Moreover, bepridil has been reported to exert a differential effect in slow and fast skeletal muscle fibres, which express the slow/cardiac and fast TnC isoform, respectively. 2. The role of the TnC isoform in establishing the differential effect of bepridil was assessed in slow soleus and fast tibialis rat skinned fibres, by extraction of endogenous TnC and consecutive reconstitution with either slow or fast recombinant TnC. A mutant (VG2), lacking the regulatory site II, was also used to distinguish the role of each regulatory site. 3. Fast tibialis fibres reconstituted with cardiac TnC exhibited a typical slow bepridil reactivity, while slow soleus fibres reincorporated with fast TnC displayed a typically fast reactivity to bepridil. These results indicated that the differential effect of bepridil in slow and fast fibres is related to the TnC isoform predominantly expressed in a fibre. 4. Experiments with the VG2 mutant demonstrated that BPD can achieve an increase in the Ca(2+) affinity in the absence of a functional site II. Thus, site I was necessary for the BPD effect to be independent of the Ca(2+) concentration. Moreover, the amplitude of the reinforcement in the Ca(2+) affinity, induced by the binding of bepridil to the TnC molecule, is dependent on the number of functional regulatory sites, the larger affinity reinforcement being detected when only one regulatory site (either site I or II) is functional.

Published
2000

43. Gap junction protein connexin40 is preferentially expressed in vascular endothelium and conductive bundles of rat myocardium and is increased under hypertensive conditions.

Author

Bastide, B., Neyses, Ludwig, Ganten, D., Paul, M., Willecke, K., Traub, O., Bastide, B., Neyses, Ludwig, Ganten, D., Paul, M., Willecke, K., and Traub, O.

Abstract

Gap junction channels consisting of connexin protein mediate electrical coupling between cardiac cells. Expression of two connexins, connexin40 (Cx40) and connexin43 (Cx43), has been studied in ventricular myocytes from normal and hypertensive rats. Polyclonal affinity-purified rabbit antibodies to Cx43 and Cx40 have been used for immunohistochemical analysis on frozen sections from rat heart. These studies revealed coexpression of Cx43 and Cx40 in ventricular myocytes. In addition, Cx40 is preferentially expressed in three distinct regions: first, in the endothelial layer of the heart blood vessels but not in the smooth muscle layer of the arteries; second, in the ventricular conductive myocardium, particularly in the atrioventricular bundle and bundle branches, where Cx43 is not observed; and third, in the myocyte layers close to the ventricular cavities. These results suggest that Cx40 is preferentially expressed in the fast conducting areas of myocardial tissue. Expression of both Cx40 and Cx43 was also found in immunoblots from normal and hypertensive rat myocardiocytes. Under hypertensive conditions (ie, in spontaneous hypertensive rats and in transgenic rats that exhibit hypertension due to expression of an exogenous renin gene), we found a 3.1-fold increase in Cx40 expression, compared with normal myocardium. Furthermore, we detected a 3.3-fold decrease in Cx43 protein level in transgenic hypertensive rats. The coexpression of Cx40 and Cx43 proteins in rat myocytes, their spatial distribution, and the increased amount of Cx40 protein during cardiac hypertrophy suggest that Cx40 may be involved in mediating fast conduction under normal and pathological conditions. The increased expression of Cx40 in hypertrophic heart may be a compensatory mechanism to increase conduction velocity.

Published
1993

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