Cited by 171Muscle metabolism and nutritionMuscle Physiology and DisordersSports Performance and Training

Fasted‐state skeletal muscle protein synthesis after resistance exercise is altered with training

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Kim, Paul L., Staron, Robert S., Phillips, Stuart M.·2005·The Journal of Physiology

Abstract

The purpose of the present investigation was to determine how fasted‐state protein synthesis was affected, acutely, by resistance training. Eight men (24.8 ± 1.7 years, body mass index = 23.2 ± 1.0 kg m−2; means ±s.e.m.) undertook an 8 week programme of unilateral resistance exercise training (3 sessions week−1, progression from two to four sets; intensity was 80% of the subjects' single repetition maximum (1RM): knee extension and leg press). Following training, subjects underwent two primed constant infusions of l‐[ring‐13 C 6]phenylalanine to determine mixed and myofibrillar muscle protein synthesis (MPS) at rest and 12 h after an acute bout of resistance exercise at the same exercise intensity – each leg 80% of 1RM. Biopsies (vastus lateralis) were taken to measure incorporation of labelled phenylalanine into mixed and myofibrillar skeletal muscle proteins and yield fractional MPS. Training resulted in significant dynamic strength gains that were greater (P < 0.001) in the trained leg. Hypertrophy of type IIa and IIx fibres (P < 0.05) was observed following training. After training, resting mixed MPS rate was elevated (+48%; P < 0.05). Acutely, resistance exercise stimulated mixed MPS only in the untrained leg (P < 0.05). Myofibrillar MPS was unchanged at rest following training (P= 0.61). Myofibrillar MPS increased after resistance exercise (P < 0.05), but was not different between the trained and untrained legs (P= 0.36). We observed divergent changes in resting mixed versus myofibrillar protein synthesis with training. In addition, resistance training modified the acute response of MPS to resistance exercise by dampening the increased synthesis of non‐myofibrillar proteins while maintaining the synthesis of myofibrillar proteins.

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Authors
Kim, P. L., Staron, R. S., & Phillips, S. M.
Affiliations
  • McMaster University (CA)
  • Ohio University (US)
Venue
The Journal of Physiology
Publisher
Wiley
Published
2005-09-28
Volume
568
Issue
1
Pages
283-290
ISSN
  • 0022-3751 (ISSN-L)
  • 1469-7793
OpenAlex
W1961685256
Cited by
171
References
32
Citations by year
2026: 1 · 2025: 6 · 2024: 4 · 2023: 7 · 2022: 7 · 2021: 8 · 2020: 6 · 2019: 8 · 2018: 8 · 2017: 14 · 2016: 11 · 2015: 16 · 2014: 12 · 2013: 10 · 2012: 10
FWCI
2.57
Type
journal article
Language
en
Open access
Locations
  • The Journal of Physiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Canadian Institutes of Health Research
  • Natural Sciences and Engineering Research Council of Canada
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 › Orthopedics and Sports Medicine › Sports Performance and Training
Keywords
resistance training, skeletal muscle protein synthesis, fasting state, myofibrillar protein synthesis, muscle hypertrophy, fast-twitch muscle, vastus lateralis, phenylalanine tracer, muscle strength gain
MeSH terms
Fasting, Humans, Leg, Male, Muscle Contraction, Muscle Proteins, Phenylalanine, Time Factors, Weight Lifting, Exercise, Muscle, Skeletal, Muscle Fibers, Fast-Twitch, Cell Enlargement

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