The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Low-Load High Volume Resistance Exercise Stimulates Muscle Protein Synthesis More Than High-Load Low Volume Resistance Exercise in Young Men
Open accessAbstract
BACKGROUND: We aimed to determine the effect of resistance exercise intensity (%1 repetition maximum-1RM) and volume on muscle protein synthesis, anabolic signaling, and myogenic gene expression. METHODOLOGY/PRINCIPAL FINDINGS: Fifteen men (21+/-1 years; BMI=24.1+/-0.8 kg/m2) performed 4 sets of unilateral leg extension exercise at different exercise loads and/or volumes: 90% of repetition maximum (1RM) until volitional failure (90FAIL), 30% 1RM work-matched to 90%FAIL (30WM), or 30% 1RM performed until volitional failure (30FAIL). Infusion of [ring-13C6] phenylalanine with biopsies was used to measure rates of mixed (MIX), myofibrillar (MYO), and sarcoplasmic (SARC) protein synthesis at rest, and 4 h and 24 h after exercise. Exercise at 30WM induced a significant increase above rest in MIX (121%) and MYO (87%) protein synthesis at 4 h post-exercise and but at 24 h in the MIX only. The increase in the rate of protein synthesis in MIX and MYO at 4 h post-exercise with 90FAIL and 30FAIL was greater than 30WM, with no difference between these conditions; however, MYO remained elevated (199%) above rest at 24 h only in 30FAIL. There was a significant increase in AktSer473 at 24h in all conditions (P=0.023) and mTORSer2448 phosphorylation at 4 h post-exercise (P=0.025). Phosporylation of Erk1/2Tyr202/204, p70S6KThr389, and 4E-BP1Thr37/46 increased significantly (P<0.05) only in the 30FAIL condition at 4 h post-exercise, whereas, 4E-BP1Thr37/46 phosphorylation was greater 24 h after exercise than at rest in both 90FAIL (237%) and 30FAIL (312%) conditions. Pax7 mRNA expression increased at 24 h post-exercise (P=0.02) regardless of condition. The mRNA expression of MyoD and myogenin were consistently elevated in the 30FAIL condition. CONCLUSIONS/SIGNIFICANCE: These results suggest that low-load high volume resistance exercise is more effective in inducing acute muscle anabolism than high-load low volume or work matched resistance exercise modes.
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“This strongly indicates that the translational capacity bottleneck possesses a high activation threshold: a minimal mechanical volume is strictly required to sustain the Pol I transcription spark long enough to outpace the basal decay rate of existing ribosomes [35,87,88].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [88]
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“Consistent with this line of evidence, research where participants expended a high level of effort suggests that the MPS response to low-load training is at least as robust as when training with heavier loads [39].”
From Loading recommendations for muscle strength, hypertrophy, and local endurance: a re-examination of the repetition continuum. (2021) · cites this paper as [39]
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“Some studies show an impaired acute MPS response when training with lower loads [37,38] while others report similar increases in mixed and myofibrillar protein synthesis rates [39].”
From Loading recommendations for muscle strength, hypertrophy, and local endurance: a re-examination of the repetition continuum. (2021) · cites this paper as [39]
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“Figueiredo et al. showed that post-exercise cold-water immersion attenuated markers associated with ribosome biogenesis compared with active recovery [88].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [88]
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Citations
Cites
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Pax7 Is Required for the Specification of Myogenic Satellite Cells
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Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle
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“The reason for sustained increase in MIX protein synthesis in the 90FAIL and 30WM conditions may be manifested in the SARC fraction which represents ,30% of MIX protein and has been established to turn over at a rate that is twice that of myofibrillar proteins [24,36,37].”
BackgroundSelf-citationMixed muscle protein synthesis and breakdown after resistance exercise in humans
Phillips, S. M., Tipton, K. D., Aarsland, A., Wolf, S. E., & Wolfe, R. R. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.273.1.e99 · Cited by 1,132
Self-citationMoore, D. R., Robinson, M. J., Fry, J. L., Tang, J. E., Glover, E. I., Wilkinson, S. B., Prior, T., Tarnopolsky, M. A., & Phillips, S. M. (2009) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.26401 · Cited by 973
Self-citationKumar, V., Selby, A., Rankin, D., Patel, R., Atherton, P., Hildebrandt, W., Williams, J., Smith, K., Seynnes, O., Hiscock, N., et al. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.164483 · Cited by 740
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Resistance exercise load does not determine training-mediated hypertrophic gains in young men
Mitchell, C. J., Churchward-Venne, T. A., West, D. W. D., Burd, N. A., Breen, L., Baker, S. K., & Phillips, S. M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00307.2012 · Cited by 627
Self-citationEffective fiber hypertrophy in satellite cell-depleted skeletal muscle
McCarthy, J. J., Mula, J., Miyazaki, M., Erfani, R., Garrison, K., Farooqui, A. B., Srikuea, R., Lawson, B. A., Grimes, B., Keller, C., et al. (2011) · Development · doi:10.1242/dev.068858 · Cited by 616
Breen, L., & Phillips, S. M. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-68 · Cited by 576
Self-citationNarici, M. V., VITO, G. D., Franchi, M. V., Paoli, A., Moro, T., Marcolin, G., Grassi, B., Baldassarre, G., Zuccarelli, L., Biolo, G., et al. (2020) · European Journal of Sport Science · doi:10.1080/17461391.2020.1761076 · Cited by 494
Schoenfeld, B. J., Peterson, M. D., Ogborn, D., Contreras, B., & Sonmez, G. T. (2015) · Journal of Strength and Conditioning Research · doi:10.1519/jsc.0000000000000958 · Cited by 418
Metadata
- Authors
- Burd, N. A., West, D. W. D., Staples, A. W., Atherton, P. J., Baker, J. M., Moore, D. R., Holwerda, A. M., Parise, G., Rennie, M. J., Baker, S. K., & Phillips, S. M.
- Affiliations
- McMaster University (CA)
- University of Nottingham (GB)
- Corresponding author
- Phillips, Stuart M.
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-08-09
- Volume
- 5
- Issue
- 8
- Pages
- e12033
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2918506
- OpenAlex
- W2160436389
- Cited by
- 531
- References
- 54
- Citations by year
- 2026: 18 · 2025: 29 · 2024: 37 · 2023: 21 · 2022: 40 · 2021: 31 · 2020: 37 · 2019: 45 · 2018: 30 · 2017: 37 · 2016: 44 · 2015: 38 · 2014: 34 · 2013: 26 · 2012: 37
- FWCI
- 12.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Keywords
- resistance training, exercise intensity, exercise volume, muscle protein synthesis, myofibrillar protein synthesis, Akt signaling, mTOR signaling, ERK1/2, p70S6K, 4E-BP1, Pax7, myogenic gene expression, leg extension, young men
- MeSH terms
- Gene Expression Regulation, Humans, Male, Muscle Proteins, Phenylalanine, RNA, Messenger, Signal Transduction, Exercise, Weight-Bearing, Myogenic Regulatory Factors, Muscle Fibers, Skeletal, Intracellular Space, PAX7 Transcription Factor, Resistance Training, Young Adult
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