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Leucine or carbohydrate supplementation reduces AMPK and eEF2 phosphorylation and extends postprandial muscle protein synthesis in rats

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Wilson, Gabriel J., Layman, Donald K., Moulton, Christopher J., Norton, Layne E., Anthony, Tracy G., Proud, Christopher G., Rupassara, S. Indu, Garlick, Peter J.·2011·American Journal of Physiology-Endocrinology and Metabolism
DOI 10.1152/ajpendo.00242.2011PMC PMC4395871
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Abstract

Muscle protein synthesis (MPS) increases after consumption of a protein-containing meal but returns to baseline values within 3 h despite continued elevations of plasma amino acids and mammalian target of rapamycin (mTORC1) signaling. This study evaluated the potential for supplemental leucine (Leu), carbohydrates (CHO), or both to prolong elevated MPS after a meal. Male Sprague-Dawley rats (∼270 g) trained to consume three meals daily were food deprived for 12 h, and then blood and gastrocnemius muscle were collected 0, 90, or 180 min after a standard 4-g test meal (20% whey protein). At 135 min postmeal, rats were orally administered 2.63 g of CHO, 270 mg of Leu, both, or water (sham control). Following test meal consumption, MPS peaked at 90 min and then returned to basal (time 0) rates at 180 min, although ribosomal protein S6 kinase and eIF4E-binding protein-1 phosphorylation remained elevated. In contrast, rats administered Leu and/or CHO supplements at 135 min postmeal maintained peak MPS through 180 min. MPS was inversely associated with the phosphorylation states of translation elongation factor 2, the "cellular energy sensor" adenosine monophosphate-activated protein kinase-α (AMPKα) and its substrate acetyl-CoA carboxylase, and increases in the ratio of AMP/ATP. We conclude that the incongruity between MPS and mTORC1 at 180 min reflects a block in translation elongation due to reduced cellular energy. Administering Leu or CHO supplements ∼2 h after a meal maintains cellular energy status and extends the postprandial duration of MPS.

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  • In an animal model, leucine consumption resulted in a lower duration of protein synthesis compared to a whole meal.

    “Wilson et al. [139] demonstrated in an animal model that leucine consumption resulted in a lower duration of protein synthesis compared to a whole meal.”

    From International Society of Sports Nutrition Position Stand: protein and exercise (2017) · cites this paper as [139]

    The Abstract reports the opposite direction: after a meal, muscle protein synthesis returned to baseline by 180 minutes in control rats, while rats given leucine after the meal maintained peak synthesis through 180 minutes. The Experimental treatments section makes clear that leucine was given after a test meal, not compared as a stand-alone intake against a whole meal. No page numbers are available in our copy. (LLM, conf=0.88)

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Cited by

Sorted by citations

Authors
Wilson, G. J., Layman, D. K., Moulton, C. J., Norton, L. E., Anthony, T. G., Proud, C. G., Rupassara, S. I., & Garlick, P. J.
Affiliations
  • University of Illinois Urbana-Champaign (US)
  • Indiana University School of Medicine (US)
  • University of Southampton (GB)
Corresponding author
Layman, Donald K.
ORCID
Venue
American Journal of Physiology-Endocrinology and Metabolism
Publisher
American Physiological Society
Published
2011-12
Volume
301
Issue
6
Pages
E1236-E1242
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
DOI
10.1152/ajpendo.00242.2011
PMC
PMC4395871
OpenAlex
W2164568414
Cited by
71
References
5
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 6 · 2014: 11 · 2013: 13 · 2012: 4
FWCI
4.45
Type
journal article
Language
en
Open access
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Rutgers University Community Repository (Rutgers University) (submittedVersion)
  • ePrints Soton (University of Southampton) (submittedVersion)
  • IUScholarWorks (Indiana University) (submittedVersion)
Funders
  • Egg Nutrition Center
  • Wellcome Trust (086688)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords
muscle protein synthesis, leucine supplementation, carbohydrate supplementation, AMPK, eEF2 phosphorylation, mTORC1 signaling, translation elongation, S6K, eIF4E-binding protein 1, acetyl-CoA carboxylase, AMP/ATP ratio, cellular energy status, gastrocnemius
MeSH terms
Adenylate Kinase, Amino Acids, Animals, Dietary Carbohydrates, Leucine, Male, Muscle Proteins, Phosphorylation, Protein Kinases, Time Factors, Protein Biosynthesis, Rats, Sprague-Dawley, Postprandial Period, Dietary Supplements, Peptide Elongation Factor 2, Rats

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