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Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin
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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“Follistatin might enhance SkM hypertrophy due to its ability to bind and neutralize myostatin [184,199], increasing the mass of SkM available for glucose and FFA uptake and oxidation.”
In the citing paper
“FGF21 was determined to increase glucocorticoid action [164] and the secretion of adiponectin [165], while follistatin was found to bind and inactivate myostatin [184] (8), further inhibiting its proinflammatory effects.”
In the citing paper
“Follistatin, on the other hand, by inhibiting myostatin [184] (5), might also contribute to continued lipolysis in WAT.”
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Metadata
- Authors
- Gilson, H., Schakman, O., Kalista, S., Lause, P., Tsuchida, K., & Thissen, J.-P.
- Affiliations
- UCLouvain (BE)
- 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
- 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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