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Cited by 72Muscle metabolism and nutritionMuscle Physiology and DisordersAdvanced Proteomics Techniques and Applications

Dynamic proteome profiling of individual proteins in human skeletal muscle after a high-fat diet and resistance exercise

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Camera, Donny M., Burniston, Jatin G., Pogson, Mark A., Smiles, William J., Hawley, John A.·2017·The FASEB Journal
DOI 10.1096/fj.201700531r
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Abstract

It is generally accepted that muscle adaptation to resistance exercise (REX) training is underpinned by contraction-induced, increased rates of protein synthesis and dietary protein availability. By using dynamic proteome profiling (DPP), we investigated the contribution of both synthesis and breakdown to changes in abundance on a protein-by-protein basis in human skeletal muscle. Age-matched, overweight males consumed 9 d of a high-fat, low-carbohydrate diet during which time they either undertook 3 sessions of REX or performed no exercise. Precursor enrichment and the rate of incorporation of deuterium oxide into newly synthesized muscle proteins were determined by mass spectrometry. Ninety proteins were included in the DPP, with 28 proteins exhibiting significant responses to REX. The most common pattern of response was an increase in turnover, followed by an increase in abundance with no detectable increase in protein synthesis. Here, we provide novel evidence that demonstrates that the contribution of synthesis and breakdown to changes in protein abundance induced by REX differ on a protein-by-protein basis. We also highlight the importance of the degradation of individual muscle proteins after exercise in human skeletal muscle.-Camera, D. M., Burniston, J. G., Pogson, M. A., Smiles, W. J., Hawley, J. A. Dynamic proteome profiling of individual proteins in human skeletal muscle after a high-fat diet and resistance exercise.

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  • D2O labeling coupled with high-resolution mass spectrometry directly resolves the absolute infrastructural expansion of the ribosomal pool with temporal precision.

    “When coupled with high-resolution mass spectrometry to track ribosomal protein turnover, D2O labeling directly resolves the absolute infrastructural expansion of the ribosomal pool with temporal precision [70,71].”

    From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [71]

    The Methods (pp. 9–10) describe using D2O labeling and mass spectrometry to estimate synthesis rates for individual proteins, with muscle sampled on days 0, 3, 6, and 9 (Figure 1, p. 22). But the paper describes relative changes in protein abundance (Introduction, p. 4); it does not show that this method directly resolves absolute expansion of the ribosomal protein pool. Its mention of 18S ribosomal RNA is as a normalization reference (Methods, p. 13). (LLM, conf=0.88)

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  • D2O labeling allows quantification of the fractional synthetic rate and decay kinetics of ribosomes in human muscle biopsies over longitudinal training periods.

    “The integration of dynamic metabolic labeling using deuterium oxide (D2O) allows researchers to quantify the fractional synthetic rate (FSR) and decay kinetics of ribosomes in human muscle biopsies over longitudinal training periods [70,71].”

    From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [71]

    The Methods (p. 10) describe calculating individual muscle-protein synthesis and breakdown rates, and the Figure 1 description (p. 22) documents D2O labeling of human muscle biopsies. The paper does not establish these measurements specifically for ribosomes; its intervention lasted nine days, not a longitudinal training period. (LLM, conf=0.87)

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Authors
Camera, D. M., Burniston, J. G., Pogson, M. A., Smiles, W. J., & Hawley, J. A.
Affiliations
  • Australian Catholic University (AU)
  • Research Institute for Sport and Exercise Sciences and Liverpool United Kingdom
  • Liverpool John Moores University (GB)
Corresponding author
Hawley, John A.
ORCID
Venue
The FASEB Journal
Publisher
Wiley
Published
2017-08-30
Volume
31
Issue
12
Pages
5478-5494
ISSN
  • 0892-6638 (ISSN-L)
  • 1530-6860
DOI
10.1096/fj.201700531r
OpenAlex
W2753833746
Cited by
72
References
56
Citations by year
2026: 5 · 2025: 14 · 2024: 3 · 2023: 8 · 2022: 5 · 2021: 10 · 2020: 10 · 2019: 5 · 2018: 11 · 2017: 1
FWCI
3.94
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations
  • The FASEB Journal (publishedVersion)
  • PubMed (publishedVersion)
  • Liverpool John Moores University (acceptedVersion)
  • Research Bank (Australian Catholic University) (submittedVersion)
Funders
Australian Catholic University (2013000443)
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
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
human skeletal muscle, resistance training, high-fat diet, low-carbohydrate diet, protein synthesis, protein degradation, protein turnover, muscle adaptation
MeSH terms
Chromatography, Liquid, Energy Metabolism, Humans, Male, Gas Chromatography-Mass Spectrometry, Muscle Proteins, Mass Spectrometry, Exercise, Muscle, Skeletal, Resistance Training, Diet, High-Fat, Real-Time Polymerase Chain Reaction

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