The DOI matches its Crossref record; 74 of the 75 references it cites were found in a registry or an index.
Expression and Function of Myostatin in Obesity, Diabetes, and Exercise Adaptation
Open accessAbstract
Myostatin is a member of the transforming growth factor-β/bone morphogenetic protein (TGF-β/BMP) superfamily of secreted factors that functions as a potent inhibitor of skeletal muscle growth. Moreover, considerable evidence has accumulated that myostatin also regulates metabolism and that its inhibition can significantly attenuate the progression of obesity and diabetes. Although at least part of these effects on metabolism can be attributable to myostatin's influence over skeletal muscle growth and therefore on the total volume of metabolically active lean body mass, there is mounting evidence that myostatin affects the growth and metabolic state of other tissues, including the adipose and the liver. In addition, recent work has explored the role of myostatin in substrate mobilization, uptake, and/or utilization of muscle independent of its effects on body composition. Finally, the effects of both endurance and resistance exercise on myostatin expression, as well as the potential role of myostatin in the beneficial metabolic adaptations occurring in response to exercise, have also begun to be delineated in greater detail. The purpose of this review was to summarize the work to date on the expression and function of myostatin in obesity, diabetes, and exercise adaptation.
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“On the contrary, inhibition of myostatin upregulates oxidative metabolism in SkM [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
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“Myostatin was the first identified muscle-secreted factor and is known to promote SkM atrophy [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
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“It is the only myokine known to be downregulated by acute and chronic endurance- and resistance-type exercise in both rodents and humans [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
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“Myostatin expression increases in skeletal muscle due to obesity and IR. Thus, it could favor the loss of skeletal muscle in SO [14, 61, 62].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [61]
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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
Self-citationDouble 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
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
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
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
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. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
Myostatin 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
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
Self-citationMosher, 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
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792
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Muscles, exercise and obesity: skeletal muscle as a secretory organ
Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909
Pedersen, B. K. (2013) · Comprehensive physiology · doi:10.1002/cphy.c120033 · Cited by 516
The long noncoding RNA Malat1: Its physiological and pathophysiological functions
Zhang, X., Hamblin, M. H., & Yin, K. (2017) · RNA Biology · doi:10.1080/15476286.2017.1358347 · Cited by 489
Transcriptomic profiling of skeletal muscle adaptations to exercise and inactivity
Pillon, N. J., Gabriel, B. M., Dollet, L., Smith, J. A. B., Sardón Puig, L., Botella, J., Bishop, D. J., Krook, A., & Zierath, J. R. (2020) · Nature Communications · doi:10.1038/s41467-019-13869-w · Cited by 457
PGC-1α as a Pivotal Factor in Lipid and Metabolic Regulation
Cheng, C., Ku, H., & Lin, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113447 · Cited by 450
Metadata
- Authors
- ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C.
- Affiliations
- University of Colorado Boulder (US)
- University of Calgary (CA)
- National Institutes of Health (US)
- Venue
- Medicine & Science in Sports & Exercise
- Published
- 2011-10
- Volume
- 43
- Issue
- 10
- Pages
- 1828-1835
- ISSN
- 0195-9131 (ISSN-L)
- PMC
- PMC3192366
- OpenAlex
- W2008438711
- Cited by
- 207
- References
- 75
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 19 · 2023: 17 · 2022: 24 · 2021: 16 · 2020: 13 · 2019: 14 · 2018: 12 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 17 · 2013: 9 · 2012: 9
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Medicine & Science in Sports & Exercise (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (ZIADK056020, ZIADK075048)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- myostatin, obesity, diabetes mellitus, exercise adaptation, skeletal muscle growth, adipose tissue, liver, substrate mobilization, lean body mass, endurance exercise, resistance training, metabolic adaptation
- MeSH terms
- Adaptation, Physiological, Adipose Tissue, Animals, Diabetes Mellitus, Type 2, Female, Humans, Liver, Male, Obesity, Exercise, Muscle, Skeletal, Mice, Rats, Myostatin
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