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Gene Review

MSTN  -  myostatin

Bos taurus

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Disease relevance of GDF8

  • In contrast, loss of MSTN activity in the dyW/dyW mouse model of laminin-deficient congenital muscular dystrophy, a much more severe and lethal disease model, does not improve all aspects of muscle pathology [1].
  • Thus, we propose that the generalized muscular hyperplasia phenotype observed in animals that lack functional myostatin could be as a result of deregulated myoblast proliferation [2].
  • Early loss of MSTN activity achieved either by monoclonal antibody administration or by gene deletion each improved muscle mass, regeneration, and reduced fibrosis in scgd-/- mice [1].
  • Here we examined disease severity associated with myostatin (mstn-/-) deletion in mice nullizygous for delta-sarcoglycan (scgd-/-), a model of limb-girdle muscular dystrophy [1].
  • Interestingly, studies have demonstrated some rescue effects of myostatin in muscular pathologies such as myopathies, providing a novel pharmacological strategy for treatment [3].

High impact information on GDF8

  • Because targeted disruption of myostatin in mice results in a muscular phenotype very similar to that seen in double-muscled cattle, we have evaluated this gene as a candidate gene for double-muscling condition by cloning the bovine myostatin cDNA and examining the expression pattern and sequence of the gene in normal and double-muscled cattle [4].
  • The autosomal recessive mh locus causing double-muscling condition in these cattle maps to bovine chromosome 2 within the same interval as myostatin, a member of the TGF-beta superfamily of genes [4].
  • This deletion results in a frame-shift mutation that removes the portion of the Myostatin protein that is most highly conserved among TGF-beta family members and that is the portion targeted for disruption in the mouse study [4].
  • Furthermore, we also observed that in myoblasts treated with myostatin protein, Rb was predominately present in the hypophosphorylated form [2].
  • Myostatin, a member of the transforming growth factor-beta (TGF-beta) superfamily, has been shown to be a negative regulator of myogenesis [2].

Biological context of GDF8

  • Myostatin, or growth and differentiation factor 8 (GDF8), has been identified as the factor causing a phenotype known as double muscling, in which a series of mutations render the gene inactive, and therefore, unable to regulate muscle fibre deposition [5].
  • A number of recessive alleles in the bovine myostatin gene (GDF8, mapped to bovine chromosome 2 and apparently orthologous to the human 2q22 region) have been shown to be responsible for DM [6].
  • Myostatin, a secreted growth factor, is a member of the TGF-beta superfamily and an inhibitor of myogenesis [7].
  • Based on these results, we propose that myostatin auto-regulates its gene expression through a Smad7 dependent mechanism in myogenic cells [7].
  • In the first exon of bovine myostatin, a single transcription initiation site is found at 133 bps from the translation start codon ATG [8].

Anatomical context of GDF8


Associations of GDF8 with chemical compounds

  • Piedmontese cattle are a heavy-muscled breed that express a mutated form of myostatin in which cysteine (313) is substituted with tyrosine [11].
  • Single cysteine to tyrosine transition inactivates the growth inhibitory function of Piedmontese myostatin [11].
  • Myostatin, a member of the transforming growth factor-beta superfamily, is a secreted growth factor that is proteolytically processed to give COOH-terminal mature myostatin and NH2-terminal latency-associated peptide in myoblasts [11].
  • These results indicate that, in Piedmontese myostatin, substitution of cysteine with tyrosine results in the distortion of the "cystine knot" structure and a loss of biological activity of the myostatin [11].
  • Use of inactive myostatin was profitable as long as the price for Select was at least 80% of the Choice price and the price for Standard at least 60% [12].

Regulatory relationships of GDF8


Other interactions of GDF8


Analytical, diagnostic and therapeutic context of GDF8


  1. Age-dependent effect of myostatin blockade on disease severity in a murine model of limb-girdle muscular dystrophy. Parsons, S.A., Millay, D.P., Sargent, M.A., McNally, E.M., Molkentin, J.D. Am. J. Pathol. (2006) [Pubmed]
  2. Myostatin, 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. J. Biol. Chem. (2000) [Pubmed]
  3. Myostatin regulation of muscle development: molecular basis, natural mutations, physiopathological aspects. Dominique, J.E., Gérard, C. Exp. Cell Res. (2006) [Pubmed]
  4. Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle. Kambadur, R., Sharma, M., Smith, T.P., Bass, J.J. Genome Res. (1997) [Pubmed]
  5. Myostatin and its implications on animal breeding: a review. Bellinge, R.H., Liberles, D.A., Iaschi, S.P., O'brien, P.A., Tay, G.K. Anim. Genet. (2005) [Pubmed]
  6. "Double-muscle" trait in cattle: a possible model for Wiedemann-Beckwith syndrome. Best, L.G., Gilbert-Barness, E., Gerrard, D.E., Gendron-Fitzpatrick, A., Opitz, J.M. Fetal and pediatric pathology. (2006) [Pubmed]
  7. Myostatin auto-regulates its expression by feedback loop through Smad7 dependent mechanism. Forbes, D., Jackman, M., Bishop, A., Thomas, M., Kambadur, R., Sharma, M. J. Cell. Physiol. (2006) [Pubmed]
  8. Genomic organization and neonatal expression of the bovine myostatin gene. Jeanplong, F., Sharma, M., Somers, W.G., Bass, J.J., Kambadur, R. Mol. Cell. Biochem. (2001) [Pubmed]
  9. Development of skeletal muscle and expression of candidate genes in bovine fetuses from embryos produced in vivo or in vitro. Crosier, A.E., Farin, C.E., Rodriguez, K.F., Blondin, P., Alexander, J.E., Farin, P.W. Biol. Reprod. (2002) [Pubmed]
  10. Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells. Taylor, W.E., Bhasin, S., Artaza, J., Byhower, F., Azam, M., Willard, D.H., Kull, F.C., Gonzalez-Cadavid, N. Am. J. Physiol. Endocrinol. Metab. (2001) [Pubmed]
  11. Single cysteine to tyrosine transition inactivates the growth inhibitory function of Piedmontese myostatin. Berry, C., Thomas, M., Langley, B., Sharma, M., Kambadur, R. Am. J. Physiol., Cell Physiol. (2002) [Pubmed]
  12. Optimum mating systems for the myostatin locus in cattle. Keele, J.W., Fahrenkrug, S.C. J. Anim. Sci. (2001) [Pubmed]
  13. Myostatin inhibits differentiation of bovine preadipocyte. Hirai, S., Matsumoto, H., Hino, N., Kawachi, H., Matsui, T., Yano, H. Domest. Anim. Endocrinol. (2007) [Pubmed]
  14. Gene expression of myostatin during development and regeneration of skeletal muscle in Japanese Black Cattle. Shibata, M., Matsumoto, K., Aikawa, K., Muramoto, T., Fujimura, S., Kadowaki, M. J. Anim. Sci. (2006) [Pubmed]
  15. Growth hormone differentially regulates muscle myostatin1 and -2 and increases circulating cortisol in rainbow trout (Oncorhynchus mykiss). Biga, P.R., Cain, K.D., Hardy, R.W., Schelling, G.T., Overturf, K., Roberts, S.B., Goetz, F.W., Ott, T.L. Gen. Comp. Endocrinol. (2004) [Pubmed]
  16. PCR based detection of bovine myostatin Q204X mutation. Antoniou, E., Grosz, M. Anim. Genet. (1999) [Pubmed]
  17. Genetic variation in the bovine myostatin gene in UK beef cattle: allele frequencies and haplotype analysis in the South Devon. Smith, J.A., Lewis, A.M., Wiener, P., Williams, J.L. Anim. Genet. (2000) [Pubmed]
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