Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Open accessAbstract
uscle wasting and weakness are among the most common inherited and acquired disorders and include the muscular dystrophies, cachexia, and age-related wasting.Since there is no generally accepted treatment to improve muscle bulk and strength, these conditions pose a substantial burden to patients as well as to public health.Consequently, there has been considerable interest in a recently described inhibitor of muscle growth, myostatin, or growth/ differentiation factor 8 (GDF-8), which belongs to the transforming growth factor b superfamily of secreted proteins that control the growth and differentiation of tissues throughout the body.The myostatin gene is expressed almost exclusively in cells of skeletal-muscle lineage throughout embryonic development as well as in adult animals and functions as a negative regulator of muscle growth.1,2 Targeted disruption of the myostatin gene in mice doubles skeletal-muscle mass. 1 Conversely, systemic overexpression of the myostatin gene leads to a wasting syndrome characterized by extensive muscle loss.3 In adult animals, myostatin appears to inhibit the activation of satellite cells, which are stem cells resident in skeletal muscle.4,5 The potential relevance of myostatin to the treatment of disease in humans has been suggested by studies involving mdx mice, which carry a mutation in the dystrophin gene and therefore serve as a genetic model of Duchenne's and Becker's muscular dystrophy.6 For example , mdx mice that lacked myostatin were found not only to be stronger and more muscular than their mdx counterparts with normal myostatin, but also to have reduced fibrosis and fatty remodeling, suggesting improved regeneration of muscle.7 Furthermore, injection of neutralizing monoclonal antibodies directed against myostatin into either wild-type or mdx mice increases muscle mass and specific force, suggesting that myostatin plays an important role in regulating muscle growth in adult animals.8,9 The function of myostatin appears to be conserved across species, since mutations in the myostatin gene have been shown to be responsible for the "double-muscling" phenotype in cattle.[10][11][12][13] The phenotypes of mice and cattle lacking myostatin and the high degree of sequence conservation of the predicted myostatin protein in many mammalian species have raised the possibility that myostatin may help regulate muscle growth in humans.We report the identification of a myostatin mutation in a child with muscle hypertrophy, thereby providing strong evidence that myostatin does play an important role in regulating muscle mass in humans.A healthy woman who was a former professional athlete gave birth to a son after a normal pregnancy.The identity of the child's father was not revealed.The child's birth weight was in the 75th percentile.Stimulus-induced myoclonus developed several m case report
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Both activin A and myostatin negatively affect muscle mass and growth.
“Both peptides negatively affect muscle mass and growth and myostatin deficiency results in increases of muscle mass in animals and humans.89”
From Changes in lean body mass with <scp>glucagon‐like peptide</scp> ‐1‐based therapies and mitigation strategies (2024) · cites this paper as [89]
The paper’s Abstract describes myostatin as a negative regulator of muscle growth and reports increased muscle mass when it is absent in mice and a child. The passages do not address whether activin A negatively affects muscle mass or growth (searched: “activin A,” “activin”). (LLM, conf=0.88)
Experimental — accuracy not yet measuredA toddler with high muscle mass was homozygous for a knockout mutation in the first intron of the human myostatin-encoding GDF8 gene.
“The link between myostatin and muscle mass was confirmed in humans by showing that a toddler with a high muscle mass was homozygous for a knockout mutation in the first intron of the human myostatin-encoding GDF8 gene (116).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [116]
Loss of Mstn causes muscle hypertrophy, or double muscling, in many species, including mice and humans.
“The loss of this gene causes muscle hypertrophy, or double muscling, in many species, including mice [38] and humans [39].”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [39]
In animal models, loss of myostatin signalling through loss of myostatin itself or by targeting the myostatin receptor with antibodies such as bimagrumab causes muscle hypertrophy.
“In animal models, the loss of myostatin signalling, either through the loss of myostatin itself [38, 39] or by targeting the myostatin receptor with antibodies such as bimagrumab causes muscle hypertrophy [23].”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [39]
A heavily muscled boy was found to carry a mutation in a splice site in the MSTN gene, showing that MSTN plays a similar role in humans.
“Moreover, a heavily muscled boy was found to carry a mutation in a splice site in the MSTN gene, showing that MSTN plays a similar role in humans as well (12).”
From Targeting myostatin/activin A protects against skeletal muscle and bone loss during spaceflight (2020) · cites this paper as [12]
Myostatin deficiency results in increases of muscle mass in animals and humans.
“Both peptides negatively affect muscle mass and growth and myostatin deficiency results in increases of muscle mass in animals and humans.89”
From Changes in lean body mass with <scp>glucagon‐like peptide</scp> ‐1‐based therapies and mitigation strategies (2024) · cites this paper as [89]
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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 · see citing works
Self-citationSATELLITE CELL OF SKELETAL MUSCLE FIBERS
Mauro, A. (1961) · The Journal of Cell Biology · doi:10.1083/jcb.9.2.493 · Cited by 3,683 · see citing works
Shapiro, M. B., & Senapathy, P. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.17.7155 · Cited by 2,313 · see citing works
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 · see citing works
Self-citationRegulation 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 · see citing works
Self-citationA deletion in the bovine myostatin gene causes the double–muscled phenotype in cattle
Grobet, L., Royo Martin, L. J., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Massabanda, J., et al. (1997) · Nature Genetics · doi:10.1038/ng0997-71 · Cited by 1,556 · see citing works
Krawczak, M., Reiss, J., & Cooper, D. N. (1992) · Human Genetics · doi:10.1007/bf00210743 · Cited by 1,344 · see citing works
Mutations in <i>myostatin</i> ( <i>GDF8</i> ) 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 · see citing works
The Molecular Basis of Muscular Dystrophy in the <i>mdx</i> Mouse: a Point Mutation
Sicinski, P., Geng, Y., Ryder-Cook, A. S., Barnard, E. A., Darlison, M. G., & Barnard, P. J. (1989) · Science · doi:10.1126/science.2662404 · Cited by 1,086 · see citing works
Induction 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 · see citing works
Self-citationFunctional improvement of dystrophic muscle by myostatin blockade
Bogdanovich, S., Krag, T. O. B., Barton, E. R., Morris, L. D., Whittemore, L.-A., Ahima, R. S., & Khurana, T. S. (2002) · Nature · doi:10.1038/nature01154 · Cited by 831 · see citing works
Hentze, M. W., & Kulozik, A. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80542-5 · Cited by 809 · see citing works
Myostatin negatively regulates satellite cell activation and self-renewal
McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207056 · Cited by 784 · see citing works
Suppression of body fat accumulation in myostatin-deficient mice
McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505 · see citing works
Self-citationInhibition of myostatin in adult mice increases skeletal muscle mass and strength
Whittemore, L.-A., Song, K., Li, X., Aghajanian, J. D., Davies, M. V., Girgenrath, S., Hill, J. J., Jalenak, M., Kelley, P. E., Knight, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02953-4 · Cited by 503 · see citing works
Grobet, L., Poncelet, D. A., Royo, L. J., Brouwers, B., Pirottin, D., Michaux, C., Ménissier, F., Zanotti, M., Dunner, S., & Georges, M. (1998) · Mammalian Genome · doi:10.1007/s003359900727 · Cited by 471 · see citing works
Hill, J. J., Davies, M. V., Pearson, A. A., Wang, J. H., Hewick, R. M., Wolfman, N. M., & Qiu, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206379200 · Cited by 444 · see citing works
Loss of myostatin attenuates severity of muscular dystrophy in mdx mice
Wagner, K. R., McPherron, A. C., Winik, N., & Lee, S. (2002) · Annals of Neurology · doi:10.1002/ana.10385 · Cited by 378 · see citing works
Self-citationMyostatin Knockout in Mice Increases Myogenesis and Decreases Adipogenesis
Lin, J., Arnold, H. B., Della-Fera, M. A., Azain, M. J., Hartzell, D. L., & Baile, C. A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6500 · Cited by 313 · see citing works
A deletion in the myostatin gene causes the compact ( Cmpt ) hypermuscular mutation in mice
Szabó, G., Dallmann, G., Müller, G., Patthy, L., Soller, M., & Varga, L. (1998) · Mammalian Genome · doi:10.1007/s003359900843 · Cited by 161 · see citing works
Amthor, H., Huang, R., McKinnell, I. W., Christ, B., Kambadur, R., Sharma, M., & Patel, K. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0812 · Cited by 138 · see citing works
Chelly, J., Gilgenkrantz, H., Hugnot, J., et al. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115417 · Cited by 54 · see citing works
Allen (1999) · doi:10.1002/(sici)1097-4652(199907)180:1
Flagged first, then by citations
Research works printed but not linked: 2
- Hentze MW, Kulozik AE. A perfect mes- sage: RNA surveillance and nonsense-medi- ated decay. Cell 1999;96:307-10.
- Sharma M, Kambadur R, Matthews KG, et al. Myostatin, a transforming growth fac- tor-b superfamily member, is expressed in heart muscle and is upregulated in cardi- omyocytes after infarct. J Cell Physiol 1999; 180:1-9.
Cited by
Sorted by citations
Genomic atlas of the human plasma proteome
Sun, B. B., Maranville, J. C., Peters, J. E., Stacey, D., Staley, J. R., Blackshaw, J., Burgess, S., Jiang, T., Paige, E., Surendran, P., et al. (2018) · Nature · doi:10.1038/s41586-018-0175-2 · Cited by 2,268 · see citing works
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Clop, A., Marcq, F., Takeda, H., Pirottin, D., Tordoir, X., Bibé, B., Bouix, J., Caiment, F., Elsen, J.-M., Eychenne, F., et al. (2006) · Nature Genetics · doi:10.1038/ng1810 · Cited by 1,260 · see citing works
Self-citationUnconstrained genome targeting with near-PAMless engineered CRISPR-Cas9 variants
Walton, R. T., Christie, K. A., Whittaker, M. N., & Kleinstiver, B. P. (2020) · Science · doi:10.1126/science.aba8853 · Cited by 1,233 · see citing works
Sarcopenia: its assessment, etiology, pathogenesis, consequences and future perspectives
Rolland, Y., Czerwinski, S., van Kan, G. A., Morley, J. E., Cesari, M., Onder, G., Woo, J., Baumgartner, R., Pillard, F., Boirie, Y., et al. (2008) · The Journal of nutrition, health and aging · doi:10.1007/bf02982704 · Cited by 1,071 · see citing works
TGF-β signaling in health and disease
Massagué, J., & Sheppard, D. (2023) · Cell · doi:10.1016/j.cell.2023.07.036 · Cited by 890 · see citing works
Mosher, D. S., Quignon, P., Bustamante, C. D., Sutter, N. B., Mellersh, C. S., Parker, H. G., & Ostrander, E. A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030079 · Cited by 826 · see citing works
The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756 · see citing works
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517 · see citing works
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. P., Tomkinson, K. N., Wright, J. F., Barker, C., Ehrmantraut, G., Holmstrom, J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505996102 · Cited by 501 · see citing works
Self-citationA phase I/IItrial of MYO‐029 in adult subjects with muscular dystrophy
Wagner, K. R., Fleckenstein, J. L., Amato, A. A., Barohn, R. J., Bushby, K., Escolar, D. M., Flanigan, K. M., Pestronk, A., Tawil, R., Wolfe, G. I., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21338 · Cited by 481 · see citing works
Self-citationNew fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437 · see citing works
Role of Myokines in Regulating Skeletal Muscle Mass and Function
Lee, J. H., & Jun, H.-S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00042 · Cited by 432 · see citing works
Skeletal muscle as an endocrine organ: PGC-1α, myokines and exercise
Schnyder, S., & Handschin, C. (2015) · Bone · doi:10.1016/j.bone.2015.02.008 · Cited by 419 · see citing works
Myostatin and the skeletal muscle atrophy and hypertrophy signaling pathways
Rodriguez, J., Vernus, B., Chelh, I., Cassar-Malek, I., Gabillard, J. C., Hadj Sassi, A., Seiliez, I., Picard, B., & Bonnieu, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1689-x · Cited by 397 · see citing works
Neeland, I. J., Linge, J., & Birkenfeld, A. L. (2024) · Diabetes, Obesity and Metabolism · doi:10.1111/dom.15728 · Cited by 391 · see citing works
Skeletal Muscle as an Endocrine Organ: The Role of Myokines in Exercise Adaptations
Hoffmann, C., & Weigert, C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029793 · Cited by 393 · see citing works
Substantial skeletal muscle loss occurs during only 5 days of disuse
Wall, B. T., Dirks, M. L., Snijders, T., Senden, J. M. G., Dolmans, J., & van Loon, L. J. C. (2014) · Acta Physiologica · doi:10.1111/apha.12190 · Cited by 346 · see citing works
Myostatin/activin pathway antagonism: molecular basis and therapeutic potential
Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314 · see citing works
Quadrupling Muscle Mass in Mice by Targeting TGF-ß Signaling Pathways
Lee, S.-J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000789 · Cited by 316 · see citing works
Self-citationLach-Trifilieff, E., Minetti, G. C., Sheppard, K., Ibebunjo, C., Feige, J. N., Hartmann, S., Brachat, S., Rivet, H., Koelbing, C., Morvan, F., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-13 · Cited by 306 · see citing works
Myokines and Adipokines: Involvement in the Crosstalk between Skeletal Muscle and Adipose Tissue
Li, F., Li, Y., Duan, Y., Hu, C.-A. A., Tang, Y., & Yin, Y. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.10.003 · Cited by 288 · see citing works
Wasting in chronic kidney disease
Mak, R. H., Ikizler, A. T., Kovesdy, C. P., Raj, D. S., Stenvinkel, P., & Kalantar-Zadeh, K. (2011) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1007/s13539-011-0019-5 · Cited by 281 · see citing works
Regulation of Muscle Mass by Follistatin and Activins
Lee, S.-J., Lee, Y.-S., Zimmers, T. A., Soleimani, A., Matzuk, M. M., Tsuchida, K., Cohn, R. D., & Barton, E. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0127 · Cited by 273 · see citing works
Self-citationThe role of exercise-induced myokines in regulating metabolism
Huh, J. Y. (2018) · Archives of Pharmacal Research · doi:10.1007/s12272-017-0994-y · Cited by 242 · see citing works
Pharmacologic Options for the Treatment of Sarcopenia
Morley, J. E. (2016) · Calcified Tissue International · doi:10.1007/s00223-015-0022-5 · Cited by 225 · see citing works
Sex-Related Differences in Gene Expression in Human Skeletal Muscle
Welle, S., Tawil, R., & Thornton, C. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001385 · Cited by 224 · see citing works
Winbanks, C. E., Weeks, K. L., Thomson, R. E., Sepulveda, P. V., Beyer, C., Qian, H., Chen, J. L., Allen, J. M., Lancaster, G. I., Febbraio, M. A., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109091 · Cited by 218 · see citing works
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214 · see citing works
Dong, J., Dong, Y., Dong, Y., Chen, F., Mitch, W. E., & Zhang, L. (2016) · International Journal of Obesity · doi:10.1038/ijo.2015.200 · Cited by 212 · see citing works
Expression and function of myostatin in obesity, diabetes, and exercise adaptation
ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3182178bb4 · Cited by 207 · see citing works
Zhang, C., McFarlane, C., Lokireddy, S., Masuda, S., Ge, X., Gluckman, P. D., Sharma, M., & Kambadur, R. (2012) · Diabetologia · doi:10.1007/s00125-011-2304-4 · Cited by 192 · see citing works
Myostatin and Sarcopenia: Opportunities and Challenges - A Mini-Review
White, T. A., & LeBrasseur, N. K. (2014) · Gerontology · doi:10.1159/000356740 · Cited by 191 · see citing works
Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance
Zhao, B., Wall, R. J., & Yang, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.044 · Cited by 186 · see citing works
Camporez, J.-P. G., Petersen, M. C., Abudukadier, A., Moreira, G. V., Jurczak, M. J., Friedman, G., Haqq, C. M., Petersen, K. F., & Shulman, G. I. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525795113 · Cited by 184 · see citing works
Allen, D. L., Cleary, A. S., Speaker, K. J., Lindsay, S. F., Uyenishi, J., Reed, J. M., Madden, M. C., & Mehan, R. S. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00798.2007 · Cited by 183 · see citing works
TGFβ and BMP signaling in skeletal muscle: potential significance for muscle-related disease
Sartori, R., Gregorevic, P., & Sandri, M. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.002 · Cited by 177 · see citing works
LeBrasseur, N. K., Schelhorn, T. M., Bernardo, B. L., Cosgrove, P. G., Loria, P. M., & Brown, T. A. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp068 · Cited by 180 · see citing works
Kwak, J. Y., & Kwon, K.-S. (2019) · Annals of Geriatric Medicine and Research · doi:10.4235/agmr.19.0028 · Cited by 171 · see citing works
Linge, J., Birkenfeld, A. L., & Neeland, I. J. (2024) · Circulation · doi:10.1161/circulationaha.124.067676 · Cited by 180 · see citing works
Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men
Hulmi, J. J., Tannerstedt, J., Selänne, H., Kainulainen, H., Kovanen, V., & Mero, A. A. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00087.2009 · Cited by 163 · see citing works
The<i>myostatin</i>gene: an overview of mechanisms of action and its relevance to livestock animals
Aiello, D., Patel, K., & Lasagna, E. (2018) · Animal Genetics · doi:10.1111/age.12696 · Cited by 162 · see citing works
Zhang, C., McFarlane, C., Lokireddy, S., Bonala, S., Ge, X., Masuda, S., Gluckman, P. D., Sharma, M., & Kambadur, R. (2011) · Diabetologia · doi:10.1007/s00125-011-2079-7 · Cited by 158 · see citing works
Modifying muscle mass – the endocrine perspective
Solomon, A. M., & Bouloux, P. M. G. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06837 · Cited by 156 · see citing works
Sako, D., Grinberg, A. V., Liu, J., Davies, M. V., Castonguay, R., Maniatis, S., Andreucci, A. J., Pobre, E. G., Tomkinson, K. N., Monnell, T. E., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.114959 · Cited by 152 · see citing works
Morvan, F., Rondeau, J.-M., Zou, C., Minetti, G., Scheufler, C., Scharenberg, M., Jacobi, C., Brebbia, P., Ritter, V., Toussaint, G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707925114 · Cited by 142 · see citing works
Latres, E., Pangilinan, J., Miloscio, L., Bauerlein, R., Na, E., Potocky, T. B., Huang, Y., Eckersdorff, M., Rafique, A., Mastaitis, J., et al. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0060-8 · Cited by 143 · see citing works
Sarcopenic obesity: how do we treat it?
Bouchonville, M. F., & Villareal, D. T. (2013) · Current Opinion in Endocrinology, Diabetes & Obesity · doi:10.1097/01.med.0000433071.11466.7f · Cited by 141 · see citing works
The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity
Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.162 · Cited by 140 · see citing works
Androgen regulation of satellite cell function
Chen, Y., Zajac, J. D., & MacLean, H. E. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.05976 · Cited by 137 · see citing works
Targeting myostatin/activin A protects against skeletal muscle and bone loss during spaceflight
Lee, S.-J., Lehar, A., Meir, J. U., Koch, C., Morgan, A., Warren, L. E., Rydzik, R., Youngstrom, D. W., Chandok, H., George, J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014716117 · Cited by 115 · see citing works
“Moreover, a heavily muscled boy was found to carry a mutation in a splice site in theMSTN gene, showing that MSTN plays a similar role in humans as well (12).”
Self-citationTherapies for Musculoskeletal Disease: Can we Treat Two Birds with One Stone?
Girgis, C. M., Mokbel, N., & DiGirolamo, D. J. (2014) · Current Osteoporosis Reports · doi:10.1007/s11914-014-0204-5 · Cited by 110 · see citing works
LY2495655, an antimyostatin antibody, in pancreatic cancer: a randomized, phase 2 trial
Golan, T., Geva, R., Richards, D., Madhusudan, S., Lin, B. K., Wang, H. T., Walgren, R. A., & Stemmer, S. M. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12331 · Cited by 109 · see citing works
Roberts, M. D., Haun, C. T., Mobley, C. B., Mumford, P. W., Romero, M. A., Roberson, P. A., Vann, C. G., & McCarthy, J. J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00834 · Cited by 107 · see citing works
Guo, B., Zhang, Z.-K., Liang, C., Li, J., Liu, J., Lu, A., Zhang, B.-T., & Zhang, G. (2017) · Calcified Tissue International · doi:10.1007/s00223-016-0209-4 · Cited by 96 · see citing works
Doping in sport: effects, harm and misconceptions
Birzniece, V. (2015) · Internal Medicine Journal · doi:10.1111/imj.12629 · Cited by 99 · see citing works
Effects of oral creatine and resistance training on serum myostatin and GASP-1
Saremi, A., Gharakhanloo, R., Sharghi, S., Gharaati, M. R., Larijani, B., & Omidfar, K. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.12.019 · Cited by 93 · see citing works
Peng, L., Lee, W., Liu, L., Lin, M., & Chen, L. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12302 · Cited by 93 · see citing works
Myostatin: a skeletal muscle chalone
Lee, S.-J. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012422-112116 · Cited by 84 · see citing works
Self-citationHjorth, M., Pourteymour, S., Görgens, S. W., Langleite, T. M., Lee, S., Holen, T., Gulseth, H. L., Birkeland, K. I., Jensen, J., Drevon, C. A., et al. (2016) · Acta Physiologica · doi:10.1111/apha.12631 · Cited by 83 · see citing works
Self-citationThe Role of the Skeletal Muscle Secretome in Mediating Endurance and Resistance Training Adaptations
Leuchtmann, A. B., Adak, V., Dilbaz, S., & Handschin, C. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.709807 · Cited by 84 · see citing works
Skeletal Muscle Degenerative Diseases and Strategies for Therapeutic Muscle Repair
Tabebordbar, M., Wang, E. T., & Wagers, A. J. (2013) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132450 · Cited by 79 · see citing works
Myostatin – The Holy Grail for Muscle, Bone, and Fat?
Buehring, B., & Binkley, N. (2013) · Current Osteoporosis Reports · doi:10.1007/s11914-013-0160-5 · Cited by 79 · see citing works
Effect of Various Exercise Regimens on Selected Exercise-Induced Cytokines in Healthy People
Domin, R., Dadej, D., Pytka, M., Zybek-Kocik, A., Ruchała, M., & Guzik, P. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18031261 · Cited by 79 · see citing works
Lee, S.-J., Lehar, A., Liu, Y., Ly, C. H., Pham, Q.-M., Michaud, M., Rydzik, R., Youngstrom, D. W., Shen, M. M., Kaartinen, V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019263117 · Cited by 59 · see citing works
Self-citationMyokines as possible therapeutic targets in cancer cachexia
Manole, E., Ceafalan, L. C., Popescu, B. O., Dumitru, C., & Bastian, A. E. (2018) · Journal of Immunology Research · doi:10.1155/2018/8260742 · Cited by 60 · see citing works
Verbrugge, S. A. J., Schönfelder, M., Becker, L., Yaghoob Nezhad, F., Hrabě de Angelis, M., & Wackerhage, H. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00553 · Cited by 56 · see citing works
Mastaitis, J. W., Gomez, D., Raya, J. G., Li, D., Min, S., Stec, M., Kleiner, S., McWilliams, T., Altarejos, J. Y., Murphy, A. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59485-9 · Cited by 53 · see citing works
“Myostatin de fi ciency has been studied in many species including mice, dogs, sheep, cattle and humans 46 – 50 .”
The Hippo signal transduction network for exercise physiologists
Gabriel, B. M., Hamilton, D. L., Tremblay, A. M., & Wackerhage, H. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01076.2015 · Cited by 48 · see citing works
Building muscle, browning fat and preventing obesity by inhibiting myostatin
LeBrasseur, N. K. (2012) · Diabetologia · doi:10.1007/s00125-011-2361-8 · Cited by 46 · see citing works
Effect of Bimagrumab on Body Composition: A Systematic Review and Meta-Analysis
Kanbay, M., Siriopol, D., Copur, S., Hasbal, N. B., Güldan, M., Kalantar-Zadeh, K., Garfias-Veitl, T., & von Haehling, S. (2024) · Aging Clinical and Experimental Research · doi:10.1007/s40520-024-02825-4 · Cited by 45 · see citing works
Sakuma, K., Watanabe, K., Hotta, N., Koike, T., Ishida, K., Katayama, K., & Akima, H. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01995.x · Cited by 42 · see citing works
Pervin, S., Reddy, S. T., & Singh, R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.653179 · Cited by 42 · see citing works
High-quality weight loss in obesity: importance of skeletal muscle
Harper, M.-E., Dent, R. R. M., & McPherson, R. (2025) · Diabetes · doi:10.2337/dbi25-0003 · Cited by 27 · see citing works
Havers, T., Held, S., Schönfelder, M., Geisler, S., & Wackerhage, H. (2025) · Sports Medicine · doi:10.1007/s40279-025-02263-w · Cited by 19 · see citing works
“In animal models, the loss of myostatin signalling, either through the loss of myostatin itself [38, 39] or by targeting the myostatin receptor with antibodies such as bimagrumab causes muscle hypertrophy [23].”
Critical analytical evaluation of promising markers for sarcopenia
Cavalier, E., Beaudart, C., Buckinx, F., Bruyère, O., & Reginster, J.-Y. (2016) · European Geriatric Medicine · doi:10.1016/j.eurger.2015.11.002 · Cited by 12 · see citing works
Lee, S.-J. (2012) · Muscle · doi:10.1016/b978-0-12-381510-1.00079-x · Cited by 8 · see citing works
Self-citation(2015) · International Journal of Kinesiology and Sports Science · doi:10.7575/aiac.ijkss.v.3n.4p.40 · Cited by 5 · see citing works
- Authors
- Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J.
- Affiliations
- Charité – Universitätsmedizin Berlin (DE)
- Johns Hopkins University (US)
- Wyeth (US)
- Martin Luther University Halle-Wittenberg (DE)
- Venue
- New England Journal of Medicine
- Publisher
- Massachusetts Medical Society
- Published
- 2004-06-24
- Volume
- 350
- Issue
- 26
- Pages
- 2682-2688
- ISSN
- 0028-4793 (ISSN-L)
- 1533-4406
- OpenAlex
- W2166877291
- Cited by
- 1,399
- References
- 23
- Citations by year
- 2026: 31 · 2025: 37 · 2024: 39 · 2023: 40 · 2022: 64 · 2021: 65 · 2020: 62 · 2019: 64 · 2018: 62 · 2017: 55 · 2016: 84 · 2015: 80 · 2014: 66 · 2013: 80 · 2012: 81
- FWCI
- 21.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- New England Journal of Medicine (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- National Cancer Institute (R01CA088866, R01 CA 88866)
- National Institute of General Medical Sciences (01GM0302)
- National Institute of Neurological Disorders and Stroke (K08NS002212, K08NS02212)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01 HD35887, R01HD035887)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Physical Performance
- Keywords
- myostatin, muscle hypertrophy, skeletal muscle growth, double muscling, muscle atrophy, Duchenne muscular dystrophy, mdx mice, satellite cells, TGF-beta superfamily, pediatric patients, muscle mass regulation, dystrophin, Becker muscular dystrophy, muscle regeneration, fibrosis
- MeSH terms
- DNA Mutational Analysis, Female, Humans, Hypertrophy, Infant, Newborn, Male, Muscular Diseases, Mutation, Pedigree, Phenotype, RNA, Messenger, Ultrasonography, Transforming Growth Factor beta, Muscle, Skeletal, Reverse Transcriptase Polymerase Chain Reaction, Myostatin
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