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Gene Review

MSTN  -  myostatin

Homo sapiens

Synonyms: GDF-8, GDF8, Growth/differentiation factor 8, MSLHP, Myostatin
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Disease relevance of GDF8


Psychiatry related information on GDF8

  • Results indicate that increases in bone strength with exercise are greater in myostatin-deficient mice than in wildtype mice, suggesting that the combination of increased muscle mass and physical activity has a greater effect on bone strength than either increased muscle mass or intense exercise alone [6].
  • Manipulations of myostatin signalling may be useful for agriculture applications, treatment of muscle diseases, inhibition of muscle atrophy and last but not least as life style drugs in antiaging therapies or manipulations of the muscle to fat ratio [7].

High impact information on GDF8

  • We herein demonstrate that the GDF8 allele of Texel sheep is characterized by a G to A transition in the 3' UTR that creates a target site for mir1 and mir206, microRNAs (miRNAs) that are highly expressed in skeletal muscle [8].
  • We mapped a quantitative trait locus with a major effect on muscle mass to chromosome 2 and subsequently fine-mapped it to a chromosome interval encompassing the myostatin (GDF8) gene [8].
  • This causes translational inhibition of the myostatin gene and hence contributes to the muscular hypertrophy of Texel sheep [8].
  • A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle [9].
  • During early stages of embryogenesis, GDF-8 expression is restricted to the myotome compartment of developing somites [10].

Chemical compound and disease context of GDF8

  • Rats that received dexamethasone showed significant body and muscle weight loss accompanied by an increase in intramuscular myostatin expression, compared with their saline-treated controls [11].
  • We hypothesized that glutamine effect on reversal of GC-induced muscle atrophy is mediated in part by suppression of myostatin [11].

Biological context of GDF8

  • Linkage patterns were observed between knee extension and flexion peak torque with markers D2S118 (GDF8), D6S1051 (CDKN1A), and D11S4138 (MYOD1), and a maximum LOD score of 2.63 (P = 0.0002) was observed with D2S118 [4].
  • Functional studies show that FLRG inhibits myostatin activity in a reporter gene assay [12].
  • Moreover, we observed a decrease in wingless-type MMTV integration site family member 10B and an upregulation of growth differentiation factor 8 expression, both being independent of PPARG activation [13].
  • Impact of resistance loading on myostatin expression and cell cycle regulation in young and older men and women [2].
  • The myostatin gene comprises three exons and two introns, maps to chromosomal region 2q33.2, has three putative transcription initiation sites, and is transcribed as a 3.1-kb mRNA species that encodes a 375-aa precursor protein [5].

Anatomical context of GDF8

  • GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle [1].
  • Myostatin inhibits myoblast proliferation and differentiation in developing muscle [2].
  • RESULTS: Human placentas were shown to express myostatin protein, with a significantly lower expression in term samples compared with samples collected in preterm samples [14].
  • In this investigation, we show that myostatin, a skeletal muscle-specific inhibitor of growth and differentiation is expressed and translated in the cultured RMS cell line, RD [15].
  • Myostatin treatment resulted in a reduction in both myotube number and size in vitro, as well as a loss in body mass in vivo [16].

Associations of GDF8 with chemical compounds


Physical interactions of GDF8


Regulatory relationships of GDF8


Other interactions of GDF8

  • Muscle mass and myofibrillar protein synthesis rates among eight older men did not correlate with either IGF-1 or myostatin mRNA levels [26].
  • These findings suggest that hSGT may play a role in the regulation of myostatin secretion and activation [19].
  • Herein, we report the identification of a myostatin-associated protein hSGT (human small glutamine-rich tetratricopeptide repeat-containing protein) by using a yeast two-hybrid system [19].
  • Activins, myostatin and related TGF-beta family members as novel therapeutic targets for endocrine, metabolic and immune disorders [3].
  • Here we describe a potent myostatin inhibitor, a soluble form of the activin type IIB receptor (ACVR2B), which can cause dramatic increases in muscle mass (up to 60% in 2 weeks) when injected into wild-type mice [27].

Analytical, diagnostic and therapeutic context of GDF8


  1. GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle. Park, J.J., Berggren, J.R., Hulver, M.W., Houmard, J.A., Hoffman, E.P. Physiol. Genomics (2006) [Pubmed]
  2. Impact of resistance loading on myostatin expression and cell cycle regulation in young and older men and women. Kim, J.S., Cross, J.M., Bamman, M.M. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  3. Activins, myostatin and related TGF-beta family members as novel therapeutic targets for endocrine, metabolic and immune disorders. Tsuchida, K. Curr. Drug Targets Immune Endocr. Metabol. Disord. (2004) [Pubmed]
  4. Linkage of myostatin pathway genes with knee strength in humans. Huygens, W., Thomis, M.A., Peeters, M.W., Aerssens, J., Janssen, R., Vlietinck, R.F., Beunen, G. Physiol. Genomics (2004) [Pubmed]
  5. Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Gonzalez-Cadavid, N.F., Taylor, W.E., Yarasheski, K., Sinha-Hikim, I., Ma, K., Ezzat, S., Shen, R., Lalani, R., Asa, S., Mamita, M., Nair, G., Arver, S., Bhasin, S. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  6. Increased muscle mass with myostatin deficiency improves gains in bone strength with exercise. Hamrick, M.W., Samaddar, T., Pennington, C., McCormick, J. J. Bone Miner. Res. (2006) [Pubmed]
  7. The growth factor myostatin, a key regulator in skeletal muscle growth and homeostasis. Matsakas, A., Diel, P. International journal of sports medicine. (2005) [Pubmed]
  8. A mutation creating a potential illegitimate microRNA target site in the myostatin gene affects muscularity in sheep. Clop, A., Marcq, F., Takeda, H., Pirottin, D., Tordoir, X., Bibé, B., Bouix, J., Caiment, F., Elsen, J.M., Eychenne, F., Larzul, C., Laville, E., Meish, F., Milenkovic, D., Tobin, J., Charlier, C., Georges, M. Nat. Genet. (2006) [Pubmed]
  9. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Grobet, L., Martin, L.J., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Massabanda, J., Fries, R., Hanset, R., Georges, M. Nat. Genet. (1997) [Pubmed]
  10. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. McPherron, A.C., Lawler, A.M., Lee, S.J. Nature (1997) [Pubmed]
  11. The effect of glutamine on prevention of glucocorticoid-induced skeletal muscle atrophy is associated with myostatin suppression. Salehian, B., Mahabadi, V., Bilas, J., Taylor, W.E., Ma, K. Metab. Clin. Exp. (2006) [Pubmed]
  12. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. Hill, J.J., Davies, M.V., Pearson, A.A., Wang, J.H., Hewick, R.M., Wolfman, N.M., Qiu, Y. J. Biol. Chem. (2002) [Pubmed]
  13. Rosiglitazone modifies the adipogenic potential of human muscle satellite cells. De Coppi, P., Milan, G., Scarda, A., Boldrin, L., Centobene, C., Piccoli, M., Pozzobon, M., Pilon, C., Pagano, C., Gamba, P., Vettor, R. Diabetologia (2006) [Pubmed]
  14. Myostatin is a human placental product that regulates glucose uptake. Mitchell, M.D., Osepchook, C.C., Leung, K.C., McMahon, C.D., Bass, J.J. J. Clin. Endocrinol. Metab. (2006) [Pubmed]
  15. Myostatin inhibits rhabdomyosarcoma cell proliferation through an Rb-independent pathway. Langley, B., Thomas, M., McFarlane, C., Gilmour, S., Sharma, M., Kambadur, R. Oncogene (2004) [Pubmed]
  16. Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism. McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M., Ling, N., Smith, H., Sharma, M., Kambadur, R. J. Cell. Physiol. (2006) [Pubmed]
  17. Myostatin Induces Cyclin D1 Degradation to Cause Cell Cycle Arrest through a Phosphatidylinositol 3-Kinase/AKT/GSK-3beta Pathway and Is Antagonized by Insulin-like Growth Factor 1. Yang, W., Zhang, Y., Li, Y., Wu, Z., Zhu, D. J. Biol. Chem. (2007) [Pubmed]
  18. Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin. Schneyer, A.L., Sidis, Y., Gulati, A., Sun, J.L., Keutmann, H., Krasney, P.A. Endocrinology (2008) [Pubmed]
  19. hSGT interacts with the N-terminal region of myostatin. Wang, H., Zhang, Q., Zhu, D. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  20. Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. Allen, D.L., Unterman, T.G. Am. J. Physiol., Cell Physiol. (2007) [Pubmed]
  21. Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers. Wójcik, S., Engel, W.K., McFerrin, J., Askanas, V. Acta Neuropathol. (2005) [Pubmed]
  22. Effects of heavy resistance training on myostatin mRNA and protein expression. Willoughby, D.S. Medicine and science in sports and exercise. (2004) [Pubmed]
  23. The Orphan Nuclear Receptor, NOR-1, Is a Target of {beta}-Adrenergic Signaling in Skeletal Muscle. Pearen, M.A., Ryall, J.G., Maxwell, M.A., Ohkura, N., Lynch, G.S., Muscat, G.E. Endocrinology (2006) [Pubmed]
  24. Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism. Zhu, X., Topouzis, S., Liang, L.F., Stotish, R.L. Cytokine (2004) [Pubmed]
  25. The effects of myostatin on adipogenic differentiation of human bone marrow-derived mesenchymal stem cells are mediated through cross-communication between Smad3 and Wnt/beta-catenin signaling pathways. Guo, W., Flanagan, J., Jasuja, R., Kirkland, J., Jiang, L., Bhasin, S. J. Biol. Chem. (2008) [Pubmed]
  26. Insulin-like growth factor-1 and myostatin mRNA expression in muscle: comparison between 62-77 and 21-31 yr old men. Welle, S., Bhatt, K., Shah, B., Thornton, C. Exp. Gerontol. (2002) [Pubmed]
  27. Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Lee, S.J., Reed, L.A., Davies, M.V., Girgenrath, S., Goad, M.E., Tomkinson, K.N., Wright, J.F., Barker, C., Ehrmantraut, G., Holmstrom, J., Trowell, B., Gertz, B., Jiang, M.S., Sebald, S.M., Matzuk, M., Li, E., Liang, L.F., Quattlebaum, E., Stotish, R.L., Wolfman, N.M. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  28. Changes in muscle myostatin expression in obese subjects after weight loss. Milan, G., Dalla Nora, E., Pilon, C., Pagano, C., Granzotto, M., Manco, M., Mingrone, G., Vettor, R. J. Clin. Endocrinol. Metab. (2004) [Pubmed]
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