Cited by 248Muscle Physiology and DisordersTGF-β signaling in diseasesMeat and Animal Product Quality

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Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin

Gilson, Hélène, Schakman, Olivier, Kalista, Stéphanie, Lause, Pascale, Tsuchida, Kunihiro, Thissen, Jean-Paul·2009·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00193.2009

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Abstract

Follistatin (FS) inhibits several members of the TGF-beta superfamily, including myostatin (Mstn), a negative regulator of muscle growth. Mstn inhibition by FS represents a potential therapeutic approach of muscle atrophy. The aim of our study was to investigate the mechanisms of the FS-induced muscle hypertrophy. To test the role of satellite cells in the FS effect, we used irradiation to destroy their proliferative capacity. FS overexpression increased the muscle weight by about 37% in control animals, but the increase reached only 20% in irradiated muscle, supporting the role of cell proliferation in the FS-induced hypertrophy. Surprisingly, the muscle hypertrophy caused by FS reached the same magnitude in Mstn-KO as in WT mice, suggesting that Mstn might not be the only ligand of FS involved in the regulation of muscle mass. To assess the role of activin (Act), another FS ligand, in the FS-induced hypertrophy, we electroporated FSI-I, a FS mutant that does not bind Act with high affinity. Whereas FS electroporation increased muscle weight by 32%, the muscle weight gain induced by FSI-I reached only 14%. Furthermore, in Mstn-KO mice, FSI-I overexpression failed to induce hypertrophy, in contrast to FS. Therefore, these results suggest that Act inhibition may contribute to FS-induced hypertrophy. Finally, the role of Act as a regulator of muscle mass was supported by the observation that ActA overexpression induced muscle weight loss (-15%). In conclusion, our results show that satellite cell proliferation and both Mstn and Act inhibition are involved in the FS-induced muscle hypertrophy.

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RETRACTED: Follistatin induction by nitric oxide through cyclic GMP: a tightly regulated signaling pathway that controls myoblast fusion
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Authors: Gilson, H., Schakman, O., Kalista, S., Lause, P., Tsuchida, K., & Thissen, J.-P.
Affiliations: UCLouvain (BE)
ORCID: Schakman, Olivier
Tsuchida, Kunihiro
Thissen, Jean-Paul
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2009-07
Volume: 297
Issue: 1
Pages: E157-E164
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00193.2009
OpenAlex: W2169876318
Cited by: 248
References: 48
Citations by year: 2026: 6 · 2025: 12 · 2024: 6 · 2023: 13 · 2022: 11 · 2021: 14 · 2020: 16 · 2019: 13 · 2018: 19 · 2017: 17 · 2016: 13 · 2015: 17 · 2014: 22 · 2013: 17 · 2012: 17
FWCI: 6.95
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Digital Access to Libraries (submittedVersion)
Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion)
Funders: Fonds Spéciaux de Recherche
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
Keywords: follistatin, muscle hypertrophy, satellite cells, satellite cell proliferation, myostatin, activin, TGF-beta superfamily, muscle atrophy, muscle mass regulation
MeSH terms: Animals, Hypertrophy, Male, Muscular Atrophy, Up-Regulation, Rats, Wistar, Mice, Knockout, Activins, Satellite Cells, Skeletal Muscle, Follistatin, Cell Proliferation, Mice, Rats, Myostatin, Rats, Transgenic

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Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin

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