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A stop lever on muscle protein synthesis with no other known roles in the body, abolishing Myostatin in the body results in excessive muscle growth and a reduction of fat mass; the 'holy grail' of bodybuilding due to its potency, supplements targeting Myostatin are lacklustre.

Our evidence-based analysis on myostatin features 66 unique references to scientific papers.

Research analysis lead by Kamal Patel
All content reviewed by Examine.com Team.
Last Updated:

Human Effect Matrix

The Human Effect Matrix looks at human studies (it excludes animal and in vitro studies) to tell you what supplements affect myostatin
Grade Level of Evidence
Robust research conducted with repeated double-blind clinical trials
Multiple studies where at least two are double-blind and placebo controlled
Single double-blind study or multiple cohort studies
Uncontrolled or observational studies only
Level of Evidence
? The amount of high quality evidence. The mo re evidence, the more we can trust the results.
Outcome Magnitude of effect
? The direction and size of the supplement's impact on each outcome. Some supplements can have an increasing effect, others have a decreasing effect, and others have no effect.
Consistency of research results
? Scientific research does not always agree. HIGH or VERY HIGH means that most of the scientific research agrees.
grade-c Creatine Notable - See study
The reduction in circulating Myostatin, while notable (17%), is of uncertain practical relevance.

All comparative evidence is now gathered in our ​A-to-Z Supplement Reference.

The evidence for each separate supplement is still freely available ​here.

Scientific Research on Myostatin

Click on any below to expand the corresponding section. Click on to collapse it.

Click here to fully expand all sections or here to fully collapse them.


  1. Hiroki E, et al. A comparative study of myostatin, follistatin and decorin expression in muscle of different origin. Anat Sci Int. (2011)
  2. Lebrasseur NK. Building muscle, browning fat and preventing obesity by inhibiting myostatin. Diabetologia. (2012)
  3. Abe S, et al. Expression of myostatin and follistatin in Mdx mice, an animal model for muscular dystrophy. Zoolog Sci. (2009)
  4. Sharma M, et al. Myostatin, a transforming growth factor-beta superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct. J Cell Physiol. (1999)
  5. Zhang C, et al. Myostatin-Null Mice Exhibit Delayed Skin Wound Healing through The Blockade of Transforming Growth Factor-β Signaling by Decorin. Am J Physiol Cell Physiol. (2012)
  6. Zhang T, et al. Oral administration of myostatin-specific whole recombinant yeast Saccharomyces cerevisiae vaccine increases body weight and muscle composition in mice. Vaccine. (2011)
  7. Zhu J, et al. Follistatin improves skeletal muscle healing after injury and disease through an interaction with muscle regeneration, angiogenesis, and fibrosis. Am J Pathol. (2011)
  8. Nakatani M, et al. Follistatin-derived peptide expression in muscle decreases adipose tissue mass and prevents hepatic steatosis. Am J Physiol Endocrinol Metab. (2011)
  9. Kang JK, et al. Antisense-induced myostatin exon skipping leads to muscle hypertrophy in mice following octa-guanidine morpholino oligomer treatment. Mol Ther. (2011)
  10. Fakhfakh R, Michaud A, Tremblay JP. Blocking the myostatin signal with a dominant negative receptor improves the success of human myoblast transplantation in dystrophic mice. Mol Ther. (2011)
  11. Chelh I, et al. Molecular profiles of Quadriceps muscle in myostatin-null mice reveal PI3K and apoptotic pathways as myostatin targets. BMC Genomics. (2009)
  12. Baligand C, et al. Functional assessment of skeletal muscle in intact mice lacking myostatin by concurrent NMR imaging and spectroscopy. Gene Ther. (2010)
  13. Welle S, Bhatt K, Pinkert CA. Myofibrillar protein synthesis in myostatin-deficient mice. Am J Physiol Endocrinol Metab. (2006)
  14. Double muscling in cattle due to mutations in the myostatin gene.
  15. Clop A, et al. A mutation creating a potential illegitimate microRNA target site in the myostatin gene affects muscularity in sheep. Nat Genet. (2006)
  16. Grobet L, et al. Molecular definition of an allelic series of mutations disrupting the myostatin function and causing double-muscling in cattle. Mamm Genome. (1998)
  17. Grobet L, et al. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat Genet. (1997)
  18. Mosher DS, et al. A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs. PLoS Genet. (2007)
  19. Chisada S, et al. Myostatin-deficient medaka exhibit a double-muscling phenotype with hyperplasia and hypertrophy, which occur sequentially during post-hatch development. Dev Biol. (2011)
  20. Follistatin Gene Delivery Enhances Muscle Growth and Strength in Nonhuman Primates.
  21. Schuelke M, et al. Myostatin mutation associated with gross muscle hypertrophy in a child. N Engl J Med. (2004)
  22. Guo T, et al. Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity. PLoS One. (2009)
  23. Zhang C, et al. Inhibition of myostatin protects against diet-induced obesity by enhancing fatty acid oxidation and promoting a brown adipose phenotype in mice. Diabetologia. (2012)
  24. Chen Y, et al. Myostatin regulates glucose metabolism via the AMP-activated protein kinase pathway in skeletal muscle cells. Int J Biochem Cell Biol. (2010)
  25. Zhang C, et al. Myostatin-deficient mice exhibit reduced insulin resistance through activating the AMP-activated protein kinase signalling pathway. Diabetologia. (2011)
  26. Wilkes JJ, Lloyd DJ, Gekakis N. Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance. Diabetes. (2009)
  27. Huang Z, Chen X, Chen D. Myostatin: a novel insight into its role in metabolism, signal pathways, and expression regulation. Cell Signal. (2011)
  28. Hittel DS, et al. Myostatin decreases with aerobic exercise and associates with insulin resistance. Med Sci Sports Exerc. (2010)
  29. Tu P, et al. Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice. Diabetes. (2009)
  30. Hill JJ, et al. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J Biol Chem. (2002)
  31. Zhao B, Wall RJ, Yang J. Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance. Biochem Biophys Res Commun. (2005)
  32. Li Z, et al. Administration of a mutated myostatin propeptide to neonatal mice significantly enhances skeletal muscle growth. Mol Reprod Dev. (2010)
  33. Matsakas A, et al. Molecular, cellular and physiological investigation of myostatin propeptide-mediated muscle growth in adult mice. Neuromuscul Disord. (2009)
  34. Yang J, Zhao B. Postnatal expression of myostatin propeptide cDNA maintained high muscle growth and normal adipose tissue mass in transgenic mice fed a high-fat diet. Mol Reprod Dev. (2006)
  35. Hamrick MW, et al. Recombinant myostatin (GDF-8) propeptide enhances the repair and regeneration of both muscle and bone in a model of deep penetrant musculoskeletal injury. J Trauma. (2010)
  36. Hu S, et al. Enhanced muscle growth by plasmid-mediated delivery of myostatin propeptide. J Biomed Biotechnol. (2010)
  37. Lee SJ, et al. Regulation of muscle mass by follistatin and activins. Mol Endocrinol. (2010)
  38. Gilson H, et al. Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am J Physiol Endocrinol Metab. (2009)
  39. Lee SJ. Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways. PLoS One. (2007)
  40. Nakatani M, et al. Transgenic expression of a myostatin inhibitor derived from follistatin increases skeletal muscle mass and ameliorates dystrophic pathology in mdx mice. FASEB J. (2008)
  41. Tsuchida K. Myostatin inhibition by a follistatin-derived peptide ameliorates the pathophysiology of muscular dystrophy model mice. Acta Myol. (2008)
  42. Miura T, et al. Decorin binds myostatin and modulates its activity to muscle cells. Biochem Biophys Res Commun. (2006)
  43. Zhu J, et al. Relationships between transforming growth factor-beta1, myostatin, and decorin: implications for skeletal muscle fibrosis. J Biol Chem. (2007)
  44. Li Y, et al. Decorin gene transfer promotes muscle cell differentiation and muscle regeneration. Mol Ther. (2007)
  45. Kishioka Y, et al. Decorin enhances the proliferation and differentiation of myogenic cells through suppressing myostatin activity. J Cell Physiol. (2008)
  46. Nishimura T, et al. Spatiotemporal expression of decorin and myostatin during rat skeletal muscle development. Biochem Biophys Res Commun. (2007)
  47. Morissette MR, et al. Myostatin regulates cardiomyocyte growth through modulation of Akt signaling. Circ Res. (2006)
  48. Morissette MR, et al. Effects of myostatin deletion in aging mice. Aging Cell. (2009)
  49. Kim JS, Cross JM, Bamman MM. Impact of resistance loading on myostatin expression and cell cycle regulation in young and older men and women. Am J Physiol Endocrinol Metab. (2005)
  50. Walker KS, et al. Resistance training alters plasma myostatin but not IGF-1 in healthy men. Med Sci Sports Exerc. (2004)
  51. Hulmi JJ, et al. Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men. J Appl Physiol. (2009)
  52. Willoughby DS. Effects of heavy resistance training on myostatin mRNA and protein expression. Med Sci Sports Exerc. (2004)
  53. Kim JS, et al. Load-mediated downregulation of myostatin mRNA is not sufficient to promote myofiber hypertrophy in humans: a cluster analysis. J Appl Physiol. (2007)
  54. Heinemeier KM. Using ribosomal RNA as a reference in mRNA quantification. J Appl Physiol. (2007)
  55. Kawada S, Tachi C, Ishii N. Content and localization of myostatin in mouse skeletal muscles during aging, mechanical unloading and reloading. J Muscle Res Cell Motil. (2001)
  56. Jespersen JG, et al. Myostatin expression during human muscle hypertrophy and subsequent atrophy: increased myostatin with detraining. Scand J Med Sci Sports. (2011)
  57. Sakuma K, et al. The adaptive responses in several mediators linked with hypertrophy and atrophy of skeletal muscle after lower limb unloading in humans. Acta Physiol (Oxf). (2009)
  58. Gustafsson T, et al. Effects of 3 days unloading on molecular regulators of muscle size in humans. J Appl Physiol. (2010)
  59. George Carlson C, et al. Soluble activin receptor type IIB increases forward pulling tension in the mdx mouse. Muscle Nerve. (2011)
  60. Bamman MM, et al. Cluster analysis tests the importance of myogenic gene expression during myofiber hypertrophy in humans. J Appl Physiol. (2007)
  61. Garcia LA, et al. 1,25(OH)2vitamin D3 stimulates myogenic differentiation by inhibiting cell proliferation and modulating the expression of promyogenic growth factors and myostatin in C2C12 skeletal muscle cells. Endocrinology. (2011)
  62. Metabolic characteristics and body composition in house finches: effects of seasonal acclimatization.
  63. Barre H, et al. Potentiated muscular thermogenesis in cold-acclimated muscovy duckling. Am J Physiol. (1985)
  64. Ijiri D, Kanai Y, Hirabayashi M. Possible roles of myostatin and PGC-1alpha in the increase of skeletal muscle and transformation of fiber type in cold-exposed chicks: expression of myostatin and PGC-1alpha in chicks exposed to cold. Domest Anim Endocrinol. (2009)
  65. Cooper SJ. Seasonal metabolic acclimatization in mountain chickadees and juniper titmice. Physiol Biochem Zool. (2002)
  66. Dalbo VJ, et al. Acute loading and aging effects on myostatin pathway biomarkers in human skeletal muscle after three sequential bouts of resistance exercise. J Gerontol A Biol Sci Med Sci. (2011)