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2. Peptide-conjugated oligonucleotides evoke long-lasting myotonic dystrophy correction in patient-derived cells and mice

Author

Klein, Arnaud F., Varela, Miguel A., Arandel, Ludovic, Holland, Ashling, Naouar, Naira, Arzumanov, Andrey, Seoane, David, Revillod, Lucile, Bassez, Guillaume, Ferry, Arnaud, Jauvin, Dominic, Gourdon, Genevieve, Puymirat, Jack, Gait, Michael J., Furling, Denis, and Wood, Matthew J.A.

Subjects
Myotonic dystrophy -- Genetic aspects -- Health aspects, Skeletal muscle -- Health aspects, Peptides -- Health aspects, RNA -- Health aspects, Arginine, Protein kinases, Phenotypes, Health care industry
Abstract

Antisense oligonucleotides (ASOs) targeting pathologic RNAs have shown promising therapeutic corrections for many genetic diseases including myotonic dystrophy (DM1). Thus, ASO strategies for DM1 can abolish the toxic RNA gain-of-function mechanism caused by nucleus-retained mutant DMPK (DM1 protein kinase) transcripts containing CUG expansions (CUGexps). However, systemic use of ASOs for this muscular disease remains challenging due to poor drug distribution to skeletal muscle. To overcome this limitation, we test an arginine-rich Pip6a cell-penetrating peptide and show that Pip6aconjugated morpholino phosphorodiamidate oligomer (PMO) dramatically enhanced ASO delivery into striated muscles of DM1 mice following systemic administration in comparison with unconjugated PMO and other ASO strategies. Thus, low-dose treatment with Pip6a-PMO-CAG targeting pathologic expansions is sufficient to reverse both splicing defects and myotonia in DM1 mice and normalizes the overall disease transcriptome. Moreover, treated DM1 patient-derived muscle cells showed that Pip6a-PMO-CAG specifically targets mutant CUGexp-DMPK transcripts to abrogate the detrimental sequestration of MBNL1 splicing factor by nuclear RNA foci and consequently MBNL1 functional loss, responsible for splicing defects and muscle dysfunction. Our results demonstrate that Pip6a-PMO-CAG induces long- lasting correction with high efficacy of DM1-associated phenotypes at both molecular and functional levels, and strongly support the use of advanced peptide conjugates for systemic corrective therapy in DM1., Introduction Myotonic dystrophy (DM1), one of the most common muscular dystrophies in adults (1), is an RNA-dominant disorder caused by the expression of expanded microsatellite repeats located in the 3' [...]

Published
2019
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3. Analysis of Exonic Regions Involved in Nuclear Localization, Splicing Activity, and Dimerization of Muscleblind-like-1 Isoforms

Author

Tran, Hélène, Gourrier, Nathalie, Lemercier-Neuillet, Camille, Dhaenens, Claire-Marie, Vautrin, Audrey, Fernandez-Gomez, Francisco José, Arandel, Ludovic, Carpentier, Céline, Obriot, Hélène, Eddarkaoui, Sabiha, Delattre, Lucie, Van Brussels, Edwige, Holt, Ian, Morris, Glenn E., Sablonnière, Bernard, Buée, Luc, Charlet-Berguerand, Nicolas, Schraen-Maschke, Susanna, Furling, Denis, Behm-Ansmant, Isabelle, Branlant, Christiane, Caillet-Boudin, Marie-Laure, and Sergeant, Nicolas

Published
2011
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5. Transduction Efficiency of Adeno-Associated Virus Serotypes After Local Injection in Mouse and Human Skeletal Muscle

Author

Muraine, Laura, primary, Bensalah, Mona, additional, Dhiab, Jamila, additional, Cordova, Gonzalo, additional, Arandel, Ludovic, additional, Marhic, Alix, additional, Chapart, Maud, additional, Vasseur, Stéphane, additional, Benkhelifa-Ziyyat, Sofia, additional, Bigot, Anne, additional, Butler-Browne, Gillian, additional, Mouly, Vincent, additional, Negroni, Elisa, additional, and Trollet, Capucine, additional

Published
2020
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6. FISH protocol for Myotonic Dystrophy type 1 cells

Author

Klein, Arnaud F., Arandel, Ludovic, Marie, Joëlle, Furling, Denis, Furling, Denis, Centre de recherche en Myologie – U974 SU-INSERM, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Sorbonne Université (SU), Institut National de la Santé et de la Recherche Médicale (INSERM), Association Institut de Myologie [Paris], and Centre de Recherche en Myologie

Subjects
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019
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7. Myostatin is a key mediator between energy metabolism and\ud endurance capacity of skeletal muscle

Author

Mouisel, Etienne, Relizani, Karima, Mille-Hamard, Laurence, Denis, Raphael, Hourde, Christophe, Agbulut, Onnik, Patel, Ketan, Arandel, Ludovic, Morales-Gonzalez, Susanne, Vignaud, Alban, Garcia, Luis, Ferry, Arnaud, Luquet, Serge, Billat, Veronique, Ventura-Clapier, Renee, Schuelke, Markus, and Amthor, Helge

Subjects
musculoskeletal system
Abstract

Myostatin (Mstn) participates in the regulation of skeletal muscle size and has emerged as a regulator of muscle metabolism. Here, we hypothesized that lack of myostatin profoundly depresses oxidative phosphorylation-dependent muscle function. Toward this end, we explored Mstn/ mice as a model for the constitutive absence of myostatin and AAV-mediated overexpression of myostatin propeptide as a model of myostatin blockade in adult wild-type mice. We show that muscles from Mstn/ mice, although larger and stronger, fatigue extremely rapidly. Myostatin deficiency shifts muscle from aerobic toward anaerobic energy metabolism, as evidenced by decreased mitochondrial respiration, reduced expression of PPAR transcriptional regulators, increased enolase activity, and exercise-induced lactic acidosis. As a consequence, constitutively reduced myostatin signaling diminishes exercise capacity, while the hypermuscular state of Mstn/ mice increases oxygen consumption and the energy cost of running. We wondered whether these results are the mere consequence of the congenital fiber-type switch toward a glycolytic phenotype of constitutive Mstn/ mice. Hence, we overexpressed myostatin propeptide in adult mice, which did not affect fiber-type distribution, while nonetheless causing increased muscle fatigability, diminished exercise capacity, and decreased Pparb/d and Pgc1a expression. In conclusion, our results suggest that myostatin endows skeletal muscle with high oxidative capacity and low fatigability, thus regulating the delicate balance between muscle mass, muscle force, energy metabolism, and endurance capacity.

Published
2014

8. Splicing misregulation of SCN5A contributes to cardiac-conduction delay and heart arrhythmia in myotonic dystrophy

Author

Freyermuth, Fernande, primary, Rau, Frédérique, additional, Kokunai, Yosuke, additional, Linke, Thomas, additional, Sellier, Chantal, additional, Nakamori, Masayuki, additional, Kino, Yoshihiro, additional, Arandel, Ludovic, additional, Jollet, Arnaud, additional, Thibault, Christelle, additional, Philipps, Muriel, additional, Vicaire, Serge, additional, Jost, Bernard, additional, Udd, Bjarne, additional, Day, John W., additional, Duboc, Denis, additional, Wahbi, Karim, additional, Matsumura, Tsuyoshi, additional, Fujimura, Harutoshi, additional, Mochizuki, Hideki, additional, Deryckere, François, additional, Kimura, Takashi, additional, Nukina, Nobuyuki, additional, Ishiura, Shoichi, additional, Lacroix, Vincent, additional, Campan-Fournier, Amandine, additional, Navratil, Vincent, additional, Chautard, Emilie, additional, Auboeuf, Didier, additional, Horie, Minoru, additional, Imoto, Keiji, additional, Lee, Kuang-Yung, additional, Swanson, Maurice S., additional, de Munain, Adolfo Lopez, additional, Inada, Shin, additional, Itoh, Hideki, additional, Nakazawa, Kazuo, additional, Ashihara, Takashi, additional, Wang, Eric, additional, Zimmer, Thomas, additional, Furling, Denis, additional, Takahashi, Masanori P., additional, and Charlet-Berguerand, Nicolas, additional

Published
2016
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9. Abnormal splicing switch of DMD’s penultimate exon compromises muscle fibre maintenance in myotonic dystrophy

Author

Rau, Frédérique, primary, Lainé, Jeanne, additional, Ramanoudjame, Laetitita, additional, Ferry, Arnaud, additional, Arandel, Ludovic, additional, Delalande, Olivier, additional, Jollet, Arnaud, additional, Dingli, Florent, additional, Lee, Kuang-Yung, additional, Peccate, Cécile, additional, Lorain, Stéphanie, additional, Kabashi, Edor, additional, Athanasopoulos, Takis, additional, Koo, Taeyoung, additional, Loew, Damarys, additional, Swanson, Maurice S., additional, Le Rumeur, Elisabeth, additional, Dickson, George, additional, Allamand, Valérie, additional, Marie, Joëlle, additional, and Furling, Denis, additional

Published
2015
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10. Correction:Impaired adaptive response to mechanical overloading in dystrophic skeletal muscle (PLoS ONE)

Author

Joanne, Pierre, Hourdé, Christophe, Ochala, Julien, Caudéran, Yvain, Medja, Fadia, Vignaud, Alban, Mouisel, Etienne, Hadj-Said, Wahiba, Arandel, Ludovic, Garcia, Luis, Goyenvalle, Aurélie, Mounier, Rémi, Zibroba, Daria, Sakamato, Kei, Butler-Browne, Gillian, Agbulut, Onnik, Ferry, Arnaud, Joanne, Pierre, Hourdé, Christophe, Ochala, Julien, Caudéran, Yvain, Medja, Fadia, Vignaud, Alban, Mouisel, Etienne, Hadj-Said, Wahiba, Arandel, Ludovic, Garcia, Luis, Goyenvalle, Aurélie, Mounier, Rémi, Zibroba, Daria, Sakamato, Kei, Butler-Browne, Gillian, Agbulut, Onnik, and Ferry, Arnaud

Published
2013

11. Impaired Adaptive Response to Mechanical Overloading in Dystrophic Skeletal Muscle

Author

Joanne, Pierre, Hourdé, Christophe, Ochala, Julien, Caudéran, Yvain, Medja, Fadia, Vignaud, Alban, Mouisel, Etienne, Hadj-Said, Wahiba, Arandel, Ludovic, Garcia, Luis, Goyenvalle, Aurelie, Mounier, Remi, Zibroba, Daria, Sakamato, Kei, Butler-Browne, Gillian, Agbulut, Onnik, Ferry, Arnaud, Joanne, Pierre, Hourdé, Christophe, Ochala, Julien, Caudéran, Yvain, Medja, Fadia, Vignaud, Alban, Mouisel, Etienne, Hadj-Said, Wahiba, Arandel, Ludovic, Garcia, Luis, Goyenvalle, Aurelie, Mounier, Remi, Zibroba, Daria, Sakamato, Kei, Butler-Browne, Gillian, Agbulut, Onnik, and Ferry, Arnaud

Abstract

Dystrophin contributes to force transmission and has a protein-scaffolding role for a variety of signaling complexes in skeletal muscle. In the present study, we tested the hypothesis that the muscle adaptive response following mechanical overloading (ML) would be decreased in MDX dystrophic muscle lacking dystrophin. We found that the gains in muscle maximal force production and fatigue resistance in response to ML were both reduced in MDX mice as compared to healthy mice. MDX muscle also exhibited decreased cellular and molecular muscle remodeling (hypertrophy and promotion of slower/oxidative fiber type) in response to ML, and altered intracellular signalings involved in muscle growth and maintenance (mTOR, myostatin, follistatin, AMPK alpha 1, REDD1, atrogin-1, Bnip3). Moreover, dystrophin rescue via exon skipping restored the adaptive response to ML. Therefore our results demonstrate that the adaptive response in response to ML is impaired in dystrophic MDX muscle, most likely because of the dystrophin crucial role.

Published
2012
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12. Correction: Impaired Adaptive Response to Mechanical Overloading in Dystrophic Skeletal Muscle

Author

Joanne, Pierre, primary, Hourdé, Christophe, additional, Ochala, Julien, additional, Caudéran, Yvain, additional, Medja, Fadia, additional, Vignaud, Alban, additional, Mouisel, Etienne, additional, Hadj-Said, Wahiba, additional, Arandel, Ludovic, additional, Garcia, Luis, additional, Goyenvalle, Aurélie, additional, Mounier, Rémi, additional, Zibroba, Daria, additional, Sakamato, Kei, additional, Butler-Browne, Gillian, additional, Agbulut, Onnik, additional, and Ferry, Arnaud, additional

Published
2013
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13. Impaired Adaptive Response to Mechanical Overloading in Dystrophic Skeletal Muscle

Author

Joanne, Pierre, primary, Hourdé, Christophe, additional, Ochala, Julien, additional, Caudéran, Yvain, additional, Medja, Fadia, additional, Vignaud, Alban, additional, Mouisel, Etienne, additional, Hadj-Said, Wahiba, additional, Arandel, Ludovic, additional, Garcia, Luis, additional, Goyenvalle, Aurélie, additional, Mounier, Rémi, additional, Zibroba, Daria, additional, Sakamato, Kei, additional, Butler-Browne, Gillian, additional, Agbulut, Onnik, additional, and Ferry, Arnaud, additional

Published
2012
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14. Immortalized human myotonic dystrophy muscle cell lines to assess therapeutic compounds

Author

Arandel, Ludovic, Polay Espinoza, Micaela, Matloka, Magdalena, Bazinet, Audrey, De Dea Diniz, Damily, Naouar, Naïra, Rau, Frédérique, Jollet, Arnaud, Edom-Vovard, Frédérique, Mamchaoui, Kamel, Tarnopolsky, Mark, Puymirat, Jack, Battail, Christophe, Boland, Anne, Deleuze, Jean-Francois, Mouly, Vincent, Klein, Arnaud F., and Furling, Denis

Abstract

Myotonic dystrophy type 1 (DM1) and type 2 (DM2) are autosomal dominant neuromuscular diseases caused by microsatellite expansions and belong to the family of RNA-dominant disorders. Availability of cellular models in which the DM mutation is expressed within its natural context is essential to facilitate efforts to identify new therapeutic compounds. Here, we generated immortalized DM1 and DM2 human muscle cell lines that display nuclear RNA aggregates of expanded repeats, a hallmark of myotonic dystrophy. Selected clones of DM1 and DM2 immortalized myoblasts behave as parental primary myoblasts with a reduced fusion capacity of immortalized DM1 myoblasts when compared with control and DM2 cells. Alternative splicing defects were observed in differentiated DM1 muscle cell lines, but not in DM2 lines. Splicing alterations did not result from differentiation delay because similar changes were found in immortalized DM1 transdifferentiated fibroblasts in which myogenic differentiation has been forced by overexpression of MYOD1. As a proof-of-concept, we show that antisense approaches alleviate disease-associated defects, and an RNA-seq analysis confirmed that the vast majority of mis-spliced events in immortalized DM1 muscle cells were affected by antisense treatment, with half of them significantly rescued in treated DM1 cells. Immortalized DM1 muscle cell lines displaying characteristic disease-associated molecular features such as nuclear RNA aggregates and splicing defects can be used as robust readouts for the screening of therapeutic compounds. Therefore, immortalized DM1 and DM2 muscle cell lines represent new models and tools to investigate molecular pathophysiological mechanisms and evaluate the in vitro effects of compounds on RNA toxicity associated with myotonic dystrophy mutations.

Published
2017
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16. Myostatin is a key mediator between energy metabolism and endurance capacity of skeletal muscle.

Author

Vignaud, Alban, Mouisel, Etienne, Ventura-Clapier, Renée, Arandel, Ludovic, Ferry, Arnaud, Amthor, Helge, Hourdé, Christophe, Morales-Gonzalez, Susanne, Schuelke, Markus, Relizani, Karima, Garcia, Luis, Mille-Hamard, Laurence, Billat, Véronique, Denis, Raphaël, Luquet, Serge, Agbulut, Onnik, and Patel, Ketan

Subjects
MYOSTATIN, AEROBIC exercises, MUSCLE fatigue, OXIDATIVE phosphorylation, MITOCHONDRIA, PEROXISOME proliferator-activated receptors
Abstract

Myostatin (Mstn) participates in the regulation of skeletal muscle size and has emerged as a regulator of muscle metabolism. Here, we hypothesized that lack of myostatin profoundly depresses oxidative phosphorylation-dependent muscle function. Toward this end, we explored Mstn-/- mice as a model for the constitutive absence of myostatin and AAV-mediated overexpression of myostatin propeptide as a model of myostatin blockade in adult wild-type mice. We show that muscles from Mstn-/- mice, although larger and stronger, fatigue extremely rapidly. Myostatin deficiency shifts muscle from aerobic toward anaerobic energy metabolism, as evidenced by decreased mitochondrial respiration, reduced expression of PPAR transcriptional regulators, increased enolase activity, and exercise-induced lactic acidosis. As a consequence, constitutively reduced myostatin signaling diminishes exercise capacity, while the hypermuscular state of Mstn-/- mice increases oxygen consumption and the energy cost of running. We wondered whether these results are the mere consequence of the congenital fiber-type switch toward a glycolytic phenotype of constitutive Mstn-/- mice. Hence, we overexpressed myostatin propeptide in adult mice, which did not affect fiber-type distribution, while nonetheless causing increased muscle fatigability, diminished exercise capacity, and decreased Pparb/d and Pgc1a expression. In conclusion, our results suggest that myostatin endows skeletal muscle with high oxidative capacity and low fatigability, thus regulating the delicate balance between muscle mass, muscle force, energy metabolism, and endurance capacity. [ABSTRACT FROM AUTHOR]

Published
2014
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