Role of Leucine in Protein Metabolism During Exercise and Recovery
Abstract
Exercise produces changes in protein and amino acid metabolism. These changes include degradation of the branched-chain amino acids, production of alanine and glutamine, and changes in protein turnover. One of the amino acid most affected by exercise is the branched-chain amino acid leucine. Recently, there has been an increased understanding of the role of leucine in metabolic regulations and remarkable new findings about the role of leucine in intracellular signaling. Leucine appears to exert a synergistic role with insulin as a regulatory factor in the insulin/phosphatidylinositol-3 kinase (PI3-K) signal cascade. Insulin serves to activate the signal pathway, while leucine is essential to enhance or amplify the signal for protein synthesis at the level of peptide initiation. Studies feeding amino acids or leucine soon after exercise suggest that post-exercise consumption of amino acids stimulates recovery of muscle protein synthesis via translation regulations. This review focuses on the unique roles of leucine in amino acid metabolism in skeletal muscle during and after exercise. Key words: branched-chain amino acids, insulin, protein synthesis, skeletal muscle
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Exercise improves net muscle protein balance and in the absence of protein feeding, this balance becomes more negative.
“It is well known that exercise improves net muscle protein balance and in the absence of protein feeding, this balance becomes more negative.”
From International Society of Sports Nutrition Position Stand: protein and exercise (2017) · cites this paper as [161]
When combined with protein feeding, net muscle protein balance after exercise becomes positive.
“When combined with protein feeding, net muscle protein balance after exercise becomes positive [161].”
From International Society of Sports Nutrition Position Stand: protein and exercise (2017) · cites this paper as [161]
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International Society of Sports Nutrition Position Stand: protein and exercise
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“with protein feeding, net muscle protein balance after exercise becomes positive [161].”
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Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise
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- Authors
- Layman, D. K.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Layman, Donald K.
- ORCID
- Layman, Donald K.
- Venue
- Canadian Journal of Applied Physiology
- Publisher
- Canadian Science Publishing
- Published
- 2002-12-01
- Volume
- 27
- Issue
- 6
- Pages
- 646-662
- ISSN
- 1066-7814 (ISSN-L)
- OpenAlex
- W1971400811
- Cited by
- 104
- References
- 2
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 3 · 2017: 4 · 2016: 3 · 2015: 8 · 2014: 7 · 2013: 6 · 2012: 7
- FWCI
- 0.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Canadian Journal of Applied Physiology (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- leucine, protein metabolism, physical activity, post-exercise recovery, branched-chain amino acids, protein synthesis, skeletal muscle, insulin signaling, phosphatidylinositol 3-kinase, translational regulation, amino acid supplementation, muscle protein turnover
- MeSH terms
- Humans, Leucine, Muscle Proteins, Signal Transduction, Exercise, Muscle, Skeletal
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