The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis
Open accessAbstract
Follistatin is known to antagonise the function of several members of the TGF-beta family of secreted signalling factors, including Myostatin, the most powerful inhibitor of muscle growth characterised to date. In this study, we compare the expression of Myostatin and Follistatin during chick development and show that they are expressed in the vicinity or in overlapping domains to suggest possible interaction during muscle development. We performed yeast and mammalian two-hybrid studies and show that Myostatin and Follistatin interact directly. We further show that single modules of the Follistatin protein cannot associate with Myostatin suggesting that the entire protein is required for the interaction. We analysed the interaction kinetics of the two proteins and found that Follistatin binds Myostatin with a high affinity of 5.84 x 10(-10) M. We next tested whether Follistatin suppresses Myostatin activity during muscle development. We confirmed our previous observation that treatment of chick limb buds with Myostatin results in a severe decrease in the expression of two key myogenic regulatory genes Pax-3 and MyoD. However, in the presence of Follistatin, the Myostatin-mediated inhibition of Pax-3 and MyoD expression is blocked. We additionally show that Myostatin inhibits terminal differentiation of muscle cells in high-density cell cultures of limb mesenchyme (micromass) and that Follistatin rescues muscle differentiation in a concentration-dependent manner. In summary, our data suggest that Follistatin antagonises Myostatin by direct protein interaction, which prevents Myostatin from executing its inhibitory effect on muscle development.
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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.”
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Cites
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
A series of normal stages in the development of the chick embryo
Hamburger, V., & Hamilton, H. L. (1992) · Developmental Dynamics · doi:10.1002/aja.1001950404 · Cited by 2,218
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
Controlling TGF-beta signaling.
Massagué, J., & Chen, Y. (2000) · PubMed · Cited by 1,780
Regulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
Controlling TGF-β signalingPreprint
Massagué, J., & Chen, Y. (2000) · Genes & Development · doi:10.1101/gad.14.6.627 · Cited by 1,589
Mutations in myostatin ( GDF8 ) in Double-Muscled Belgian Blue and Piedmontese Cattle
Kambadur, R., Sharma, M., Smith, T. P. L., & Bass, J. J. (1997) · Genome Research · doi:10.1101/gr.7.9.910 · Cited by 1,204
Self-citationMyostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
Self-citationMyostatin Inhibits Myoblast Differentiation by Down-regulating MyoD Expression
Langley, B. C., Thomas, M., Bishop, A., Sharma, M., Gilmour, S., & Kambadur, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204291200 · Cited by 910
Self-citationInduction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908
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Research works printed but not linked: 1
- Hill, 2003, Regulation of myostatin in vivo by GASP-1: a novel protein with protease inhibitor and follistatin domains, Mol. Endocrinol., 20, 20
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Parenté, A. (2019) · theses.fr (ABES) · doi:10.70675/3d9a23f5z3546z46f1z957cz5d167994539d
Putting the brakes on muscle growth: Myostatin as regulator of disuse atrophy
Nieuwenhuijsen, D. H. C., Eggelbusch, M., & Wüst, R. C. I. (2026) · Experimental Physiology · doi:10.1113/ep093732
Metadata
- Authors
- Amthor, H., Nicholas, G., McKinnell, I., Kemp, C. F., Sharma, M., Kambadur, R., & Patel, K.
- Affiliations
- Royal Veterinary College (GB)
- AgResearch (NZ)
- University of Reading (GB)
- Corresponding author
- Patel, Ketan
- Venue
- Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2004-06
- Volume
- 270
- Issue
- 1
- Pages
- 19-30
- ISSN
- 0012-1606 (ISSN-L)
- OpenAlex
- W2068756636
- Cited by
- 401
- References
- 39
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 15 · 2023: 10 · 2022: 19 · 2021: 17 · 2020: 21 · 2019: 16 · 2018: 26 · 2017: 18 · 2016: 32 · 2015: 22 · 2014: 25 · 2013: 20 · 2012: 16
- FWCI
- 5.09
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- CentAUR (University of Reading) (acceptedVersion)
- Carleton University's Institutional Repository (MacOdrum Library, Carleton University) (submittedVersion, other-oa)
- RVC Research Online (Royal Veterinary College) (submittedVersion, cc-by)
- Funders
- Wellcome Trust
- Deutsche Forschungsgemeinschaft
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- follistatin, myostatin, TGF-beta superfamily, protein-protein interaction, myogenesis, chick limb bud, Pax3, MyoD, micromass culture, limb mesenchyme, binding affinity
- MeSH terms
- PAX3 Transcription Factor, Animals, Cell Differentiation, Chick Embryo, DNA-Binding Proteins, Embryonic Structures, Extremities, Cricetinae, Membrane Glycoproteins, Recombinant Fusion Proteins, Transcription Factors, Transforming Growth Factor beta, CHO Cells, MyoD Protein, Mice, Knockout, Surface Plasmon Resonance, Two-Hybrid System Techniques, Muscle Development, Follistatin, Culture Techniques, Mice, Paired Box Transcription Factors, Myostatin
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