CoChat
Sign Up
Cited by 531Muscle metabolism and nutritionMuscle Physiology and DisordersCardiovascular and exercise physiology

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 access
Burd, Nicholas A., West, Daniel W. D., Staples, Aaron W., Atherton, Philip J., Baker, Jeff M., Moore, Daniel R., Holwerda, Andrew M., Parise, Gianni, Rennie, Michael J., Baker, Steven K., Phillips, Stuart M.·2010·PLoS ONE
DOI 10.1371/journal.pone.0012033PMC PMC2918506
Open this paper in CoChat — free accountOpen PDF

Abstract

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.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1371/journal.pone.0012033

Cites

54 of 54 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Fasted-state mixed (A), myofibrillar (B), and sarcoplasmic (C) protein synthesis (FSR) at rest and following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point, P<0.05. ‡Significantly different from 24h post within group. Values are means ± SEM.
Figure 1 Fasted-state mixed (A), myofibrillar (B), and sarcoplasmic (C) protein synthesis (FSR) at rest and following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point, P<0.05. ‡Significantly different from 24h post within group. Values are means ± SEM.CC BY · PubMed Central
Figure 2 Akt (A), Erk1/2 (B), mTOR (C) following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point. #Significant main effect for time, P<0.05. Data are expressed as fold change from rest. Values are means ± SEM.
Figure 2 Akt (A), Erk1/2 (B), mTOR (C) following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point. #Significant main effect for time, P<0.05. Data are expressed as fold change from rest. Values are means ± SEM.CC BY · PubMed Central
Figure 3 p70S6K (A), 4E-BP1 (B), and eEF2 (C) following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point, P<0.05. #Significant main effect for time, P<0.05. Data are expressed as fold change from rest. Values are means ± SEM.
Figure 3 p70S6K (A), 4E-BP1 (B), and eEF2 (C) following resistance exercise. Capital letter indicates a mean that is significantly different from rest, P<0.05. *Significantly different from 30WM within that time point, P<0.05. †Significantly different from 90FAIL within that time point, P<0.05. #Significant main effect for time, P<0.05. Data are expressed as fold change from rest. Values are means ± SEM.CC BY · PubMed Central
Figure 4 Relationship between myofibrillar protein synthesis and the extent of phosphorylation of 4E-BP1 (Thr 37/46) at 24 hours following resistance exercise. There was a significant correlation (P = 0.049) between the degree of phosphorylation (fold-change from basal) and myofibrillar protein synthesis (FSR, %/hr).
Figure 4 Relationship between myofibrillar protein synthesis and the extent of phosphorylation of 4E-BP1 (Thr 37/46) at 24 hours following resistance exercise. There was a significant correlation (P = 0.049) between the degree of phosphorylation (fold-change from basal) and myofibrillar protein synthesis (FSR, %/hr).CC BY · PubMed Central
Figure 5 Pax7 (A), MyoD (B), myogenin (C) mRNA expression in skeletal muscle 24 hours following resistance exercise. Data are expressed as fold change from rest. Data are normalized to GAPDH and reported as mean ± SEM. *Significantly different from rest, P<0.05. †Significantly different from 30WM.
Figure 5 Pax7 (A), MyoD (B), myogenin (C) mRNA expression in skeletal muscle 24 hours following resistance exercise. Data are expressed as fold change from rest. Data are normalized to GAPDH and reported as mean ± SEM. *Significantly different from rest, P<0.05. †Significantly different from 30WM.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 54 references

Cited by

Sorted by citations

Related

See all

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)
DOI
10.1371/journal.pone.0012033
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
Licence
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review