The role of skeletal muscle mTOR in the regulation of mechanical load‐induced growth
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Non‐Technical Summary Chronic mechanical loading (CML) of skeletal muscle induces growth and this effect can be blocked by the drug rapamycin. Rapamycin is considered to be a highly specific inhibitor of the mammalian target of rapamycin (mTOR), and thus, many have concluded that mTOR plays a key role in CML‐induced growth. However, direct evidence that mTOR confers the CML‐induced activation of growth promoting events such as hypertrophy, hyperplasia and ribosome biogenesis is lacking. This study addressed that gap in knowledge by using a specialized line of transgenic mice. Surprisingly, the results indicate that only a few of the growth promoting events induced by CML are fully dependent on mTOR signalling (e.g. hypertrophy). These results advance our understanding of the molecular mechanisms that regulate skeletal muscle mass and should help future studies aimed at identifying targets for therapies that can prevent the loss of muscle mass during conditions such as bedrest, immobilization, and ageing.
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Resistance exercise-induced muscle hypertrophy is completely dependent on mTOR.
“These data showed conclusively that resistance exercise-induced muscle hypertrophy is completely dependent on mTOR.”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [29]
In wild-type animals rapamycin completely blocked muscle hypertrophy, whereas in mice expressing a rapamycin-resistant mutant of mTOR, muscle hypertrophy occurred normally both in the presence and absence of rapamycin.
“As would be expected, in the wild-type animals rapamycin completely blocked muscle hypertrophy. However, in the mice expressing a rapamycin-resistant mutant of mTOR muscle, hypertrophy occurred normally both in the presence and absence of rapamycin [29].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [29]
Readily digestible, leucine-rich protein consumed after resistance training maximizes mTOR recruitment to the lysosome.
“Resistance exercise should be supported by readily digestible, leucine-rich protein as soon as possible after training to maximize leucine uptake [64], mTOR recruitment to the lysosome [29], and protein synthesis [25].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [29]
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- Authors
- Goodman, C. A., Frey, J. W., Mabrey, D. M., Jacobs, B. L., Lincoln, H. C., You, J., & Hornberger, T. A.
- Affiliations
- University of Wisconsin–Madison (US)
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2011-11
- Volume
- 589
- Issue
- 22
- Pages
- 5485-5501
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- PMC
- PMC3240886
- OpenAlex
- W2117741579
- Cited by
- 297
- References
- 57
- Citations by year
- 2026: 10 · 2025: 20 · 2024: 8 · 2023: 23 · 2022: 21 · 2021: 25 · 2020: 25 · 2019: 22 · 2018: 25 · 2017: 16 · 2016: 22 · 2015: 28 · 2014: 19 · 2013: 24 · 2012: 9
- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- University of Illinois at Urbana-Champaign
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-057347, R56AR057347, R03AR053280, AR053280, R01AR057347)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- mTOR signaling, skeletal muscle, muscle hypertrophy, muscle hyperplasia, rapamycin, FOXO1, Akt phosphorylation, muscle growth regulation
- MeSH terms
- Animals, Hypertrophy, Male, Mice, Transgenic, Mutation, Ribosomes, Weight-Bearing, Muscle, Skeletal, Sirolimus, Mice, Ablation Techniques, TOR Serine-Threonine Kinases
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