Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins
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Follistatin (FST) and FST-like-3 (FSTL3) are activin-binding and neutralization proteins that also bind myostatin. Three FST isoforms have been described that differ in tissue distribution and cell-surface binding activity, suggesting that the FST isoforms and FSTL3 may have some nonoverlapping biological actions. We produced recombinant FST isoforms and FSTL3 and compared their biochemical and biological properties. Activin-binding affinities and kinetics were comparable between the isoforms and FSTL3, whereas cell-surface binding differed markedly (FST288 > FST303 > FST315 > FSTL3). Inhibition of endogenous activin bioactivity, whether the FST isoforms were administered endogenously or exogenously, correlated closely with surface binding activity, whereas neutralization of exogenous activin when FST and FSTL3 were also exogenous was consistent with their equivalent activin-binding affinities. This difference in activin inhibition was also evident in an in vitro bioassay because FST288 suppressed, whereas FST315 enhanced, activin-dependent TT cell proliferation. Moreover, when FSTL3, which does not associate with cell membranes, was expressed as a membrane-anchored protein, its endogenous activin inhibitory activity was dramatically increased. In competitive binding assays, myostatin was more potent than bone morphogenetic proteins (BMPs) 6 and 7, and BMPs 2 and 4 were inactive in binding to FST isoforms, whereas none of the BMPs tested competed with activin for binding to FSTL3. Neutralization of exogenous BMP or myostatin bioactivity correlated with the relative abilities of the isoforms to bind cell-surface proteoglycans. These results indicate that the differential biological actions among the FST isoforms and FSTL3 are primarily dependent on their relative cell-surface binding ability and ligand specificity.
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FST acts as an inhibitor of TGF-β superfamily members including myostatin and activins, and can promote skeletal muscle growth.
“FST acts as an inhibitor of members of the TGF-β superfamily, including myostatin and activins [185,186], and can function as a promoter of skeletal muscle growth [187].”
From Hepatokines and metabolism: Deciphering communication from the liver (2021) · cites this paper as [185]
FST is present in three main isoforms, FST288, FST303, and FST315, with FST315 being the predominant isoform in circulation.
“FST is present in three main isoforms, FST288, FST303, and FST315, with FST315 being the predominant isoform found in the circulation [185,194,195].”
From Hepatokines and metabolism: Deciphering communication from the liver (2021) · cites this paper as [185]
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- Authors
- Sidis, Y., Mukherjee, A., Keutmann, H., Delbaere, A., Sadatsuki, M., & Schneyer, A.
- Affiliations
- Massachusetts General Hospital (US)
- Corresponding author
- Schneyer, Alan
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2006-07
- Volume
- 147
- Issue
- 7
- Pages
- 3586-3597
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2034316793
- Cited by
- 211
- References
- 56
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 5 · 2023: 14 · 2022: 10 · 2021: 9 · 2020: 16 · 2019: 10 · 2018: 12 · 2017: 14 · 2016: 10 · 2015: 14 · 2014: 8 · 2013: 7 · 2012: 11
- FWCI
- 4.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Endocrinology (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) (submittedVersion)
- Funders
- Belgian American Educational Foundation
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK55838, R01DK055838, R01DK053828)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01-HD-39777, R01HD039777)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- follistatin, FSTL3, myostatin, bone morphogenetic proteins, cell surface binding, proteoglycans, ligand specificity, T cell proliferation
- MeSH terms
- Animals, Cell Membrane, Chlorocebus aethiops, Humans, Recombinant Proteins, Transforming Growth Factor beta, Bone Morphogenetic Proteins, COS Cells, Activins, Follistatin, Follistatin-Related Proteins, Cell Line, Tumor, Cell Proliferation, Myostatin
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