Activation of mTORC1 signaling and protein synthesis in human muscle following blood flow restriction exercise is inhibited by rapamycin

Gundermann, David M.; Walker, Dillon K.; Reidy, Paul T.; Borack, Michael S.; Dickinson, Jared M.; Volpi, Elena; Rasmussen, Blake B.

doi:10.1152/ajpendo.00600.2013

Cited by 143Muscle metabolism and nutritionMuscle Physiology and DisordersCardiovascular and exercise physiology

Activation of mTORC1 signaling and protein synthesis in human muscle following blood flow restriction exercise is inhibited by rapamycin

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Gundermann, David M., Walker, Dillon K., Reidy, Paul T., Borack, Michael S., Dickinson, Jared M., Volpi, Elena, Rasmussen, Blake B.·2014·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00600.2013PMC PMC4116405

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Abstract

Restriction of blood flow to a contracting muscle during low-intensity resistance exercise (BFR exercise) stimulates mTORC1 signaling and protein synthesis in human muscle within 3 h postexercise. However, there is a lack of mechanistic data to provide a direct link between mTORC1 activation and protein synthesis in human skeletal muscle following BFR exercise. Therefore, the primary purpose of this study was to determine whether mTORC1 signaling is necessary for stimulating muscle protein synthesis after BFR exercise. A secondary aim was to describe the 24-h time course response in muscle protein synthesis and breakdown following BFR exercise. Sixteen healthy young men were randomized to one of two groups. Both the control (CON) and rapamycin (RAP) groups completed BFR exercise; however, RAP was administered 16 mg of the mTOR inhibitor rapamycin 1 h prior to BFR exercise. BFR exercise consisted of four sets of leg extension exercise at 20% of 1 RM. Muscle biopsies were collected from the vastus lateralis before exercise and at 3, 6, and 24 h after BFR exercise. Mixed-muscle protein fractional synthetic rate increased by 42% at 3 h postexercise and 69% at 24 h postexercise in CON, whereas this increase was inhibited in the RAP group. Phosphorylation of mTOR (Ser(2448)) and S6K1 (Thr(389)) was also increased in CON but inhibited in RAP. Mixed-muscle protein breakdown was not significantly different across time or groups. We conclude that activation of mTORC1 signaling and protein synthesis in human muscle following BFR exercise is inhibited in the presence of rapamycin.

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Phosphorylation of mTOR and its downstream substrates (p70s6k, 4EBP1) are critically involved in facilitating post-exercise increases in muscle protein synthesis.
“Human studies have since shown that phosphorylation of mTOR and its downstream substrates (i.e., p70s6k, 4EBP1) are critically involved in facilitating post-exercise increases in muscle protein synthesis (Drummond et al., 2009; Gundermann et al., 2014).”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Gundermann et al., 2014

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Blood Flow Restriction Only Increases Myofibrillar Protein Synthesis with Exercise
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Early Postoperative Role of Blood Flow Restriction Therapy to Avoid Muscle Atrophy
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Rapamycin prevents the post‐exercise increase in protein synthesis and alters cell signaling in human skeletal muscle
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Reactive hyperemia is not responsible for stimulating muscle protein synthesis following blood flow restriction exercise
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Effect of Resistance Exercise with Blood Flow Restriction on Muscle Protein Synthesis and mTOR Signaling in Older Men
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Muscle protein synthesis, degradation and the effect of mTORC1, after resistance exercise (1163.7)
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Authors: Gundermann, D. M., Walker, D. K., Reidy, P. T., Borack, M. S., Dickinson, J. M., Volpi, E., & Rasmussen, B. B.
Affiliations: Department of Nutrition and Metabolism,
The University of Texas Medical Branch at Galveston (US)
Corresponding author: Rasmussen, Blake B.
ORCID: Gundermann, David M.
Reidy, Paul T.
Dickinson, Jared M.
Volpi, Elena
Rasmussen, Blake B.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2014-05-15
Volume: 306
Issue: 10
Pages: E1198-E1204
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00600.2013
PMC: PMC4116405
OpenAlex: W2140240000
Cited by: 143
References: 40
Citations by year: 2026: 11 · 2025: 13 · 2024: 8 · 2023: 17 · 2022: 13 · 2021: 10 · 2020: 14 · 2019: 12 · 2018: 12 · 2017: 8 · 2016: 11 · 2015: 12 · 2014: 2
FWCI: 5.48
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Institute of Clinical and Translational Sciences
National Institutes of Health
National Institute on Aging (P30AG024832)
National Institute of Arthritis and Musculoskeletal and Skin Diseases
National Institute of Child Health and Human Development
National Center for Advancing Translational Sciences
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Complementary and alternative medicine › Cardiovascular and exercise physiology
Keywords: blood flow restriction exercise, mTORC1 signaling, muscle protein synthesis, rapamycin, muscle protein degradation, skeletal muscle, S6K1 phosphorylation, mTOR phosphorylation, vastus lateralis, resistance training, leg extension
MeSH terms: Mechanistic Target of Rapamycin Complex 1, Adolescent, Adult, Constriction, Humans, Male, Muscle Contraction, Regional Blood Flow, Protein Biosynthesis, Signal Transduction, Exercise, Muscle, Skeletal, Sirolimus, Multiprotein Complexes, Young Adult, TOR Serine-Threonine Kinases

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Activation of mTORC1 signaling and protein synthesis in human muscle following blood flow restriction exercise is inhibited by rapamycin

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