Effects of skeletal muscle energy availability on protein turnover responses to exercise

Smiles, William J.; Hawley, John A.; Camera, Donny M.

doi:10.1242/jeb.125104

Cited by 48Muscle metabolism and nutritionMuscle Physiology and DisordersCardiovascular and exercise physiology

Effects of skeletal muscle energy availability on protein turnover responses to exercise

Smiles, William J., Hawley, John A., Camera, Donny M.·2016·Journal of Experimental Biology

DOI 10.1242/jeb.125104

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Abstract

Skeletal muscle adaptation to exercise training is a consequence of repeated contraction-induced increases in gene expression that lead to the accumulation of functional proteins whose role is to blunt the homeostatic perturbations generated by escalations in energetic demand and substrate turnover. The development of a specific 'exercise phenotype' is the result of new, augmented steady-state mRNA and protein levels that stem from the training stimulus (i.e. endurance or resistance based). Maintaining appropriate skeletal muscle integrity to meet the demands of training (i.e. increases in myofibrillar and/or mitochondrial protein) is regulated by cyclic phases of synthesis and breakdown, the rate and turnover largely determined by the protein's half-life. Cross-talk among several intracellular systems regulating protein synthesis, breakdown and folding is required to ensure protein equilibrium is maintained. These pathways include both proteasomal and lysosomal degradation systems (ubiquitin-mediated and autophagy, respectively) and the protein translational and folding machinery. The activities of these cellular pathways are bioenergetically expensive and are modified by intracellular energy availability (i.e. macronutrient intake) and the 'training impulse' (i.e. summation of the volume, intensity and frequency). As such, exercise-nutrient interactions can modulate signal transduction cascades that converge on these protein regulatory systems, especially in the early post-exercise recovery period. This review focuses on the regulation of muscle protein synthetic response-adaptation processes to divergent exercise stimuli and how intracellular energy availability interacts with contractile activity to impact on muscle remodelling.

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It would be convenient to start resistance exercises with replenished glycogen stores.
“For this reason, it would be convenient to start resistance exercises with replenished glycogen stores [16,17].”
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Exercise enhances skeletal muscle regeneration by promoting senescence in fibro-adipogenic progenitors
Saito, Y., Chikenji, T. S., Matsumura, T., Nakano, M., & Fujimiya, M. (2020) · Nature Communications · doi:10.1038/s41467-020-14734-x · Cited by 196 · see citing works
Carbohydrate Availability and Physical Performance: Physiological Overview and Practical Recommendations
Mata, F., Valenzuela, P. L., Gimenez, J., Tur, C., Ferreria, D., Domínguez, R., Sanchez-Oliver, A. J., & Martínez Sanz, J. M. (2019) · Nutrients · doi:10.3390/nu11051084 · Cited by 112 · see citing works
Nutritional Considerations for the Vegan Athlete
West, S., Monteyne, A. J., van der Heijden, I., Stephens, F. B., & Wall, B. T. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.04.012 · Cited by 42 · see citing works
“performing resistance exercise with low muscle glycogen, and therefore low cellular energy status, can blunt the signaling pathways responsible for hypertrophic adaptation [119,120].”
Background
Effects of a resistance-training programme on endoplasmic reticulum unfolded protein response and mitochondrial functions in PBMCs from elderly subjects
Estébanez, B., Moreira, O. C., Almar, M., de Paz, J. A., Gonzalez‐Gallego, J., & Cuevas, M. J. (2019) · European Journal of Sport Science · doi:10.1080/17461391.2018.1561950 · Cited by 26 · see citing works

Derailed protein turnover in the aging mammalian brain
Rao, N. R., Upadhyay, A., & Savas, J. N. (2024) · Molecular Systems Biology · doi:10.1038/s44320-023-00009-2 · Cited by 30 · see citing works
Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity
Basisty, N., Holtz, A. N., & Schilling, B. (2019) · PROTEOMICS · doi:10.1002/pmic.201800403 · Cited by 27 · see citing works
Myofibrillar protein turnover. Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation
BATES, P. C., & Millward, D. J. (1983) · Biochemical Journal · doi:10.1042/bj2140587 · Cited by 112 · see citing works
Protein Turnover in Aging and Longevity
Basisty, N., Meyer, J. G., & Schilling, B. (2018) · PROTEOMICS · doi:10.1002/pmic.201700108 · Cited by 112 · see citing works
Degradation and evaluation of myofibril proteins induced by endogenous protease in aquatic products during storage: a review
Li, N., Xie, J., & Chu, Y. (2023) · Food Science and Biotechnology · doi:10.1007/s10068-023-01291-4 · Cited by 49 · see citing works

Authors: Smiles, W. J., Hawley, J. A., & Camera, D. M.
Affiliations: Australian Catholic University (AU)
Liverpool John Moores University (GB)
ORCID: Smiles, William J.
Hawley, John A.
Camera, Donny M.
Venue: Journal of Experimental Biology
Publisher: The Company of Biologists
Published: 2016-01-01
Volume: 219
Issue: 2
Pages: 214-225
ISSN: 0022-0949 (ISSN-L)
1477-9145
DOI: 10.1242/jeb.125104
OpenAlex: W2398539570
Cited by: 48
References: 154
Citations by year: 2026: 3 · 2025: 1 · 2024: 2 · 2023: 8 · 2022: 8 · 2021: 2 · 2020: 4 · 2019: 5 · 2018: 7 · 2017: 7 · 2016: 1
FWCI: 0.72
Type: journal article
Language: en
Open access: closed
Licence: www.biologists.com/user-licence-1-1 (vor, 182 d)
Locations: Journal of Experimental Biology (publishedVersion)
PubMed (publishedVersion)
Research Bank (Australian Catholic University) (submittedVersion)
HighWire Press Open Archive (submittedVersion)
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: skeletal muscle, protein turnover, exercise training, energy availability, muscle protein synthesis, muscle protein degradation, autophagy, ubiquitin-proteasome degradation, myofibrillar proteins, mitochondrial proteins, post-exercise recovery, training impulse, macronutrient intake, signal transduction
MeSH terms: Animals, Energy Metabolism, Humans, Models, Biological, Muscle Proteins, Exercise, Muscle, Skeletal

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Effects of skeletal muscle energy availability on protein turnover responses to exercise

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