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Cited by 220Muscle metabolism and nutritionNutrition and Health in AgingMuscle Physiology and Disorders

Leucine co-ingestion improves post-prandial muscle protein accretion in elderly men

Wall, Benjamin T., Hamer, Henrike M., de Lange, Anneke, Kiskini, Alexandra, Groen, Bart B.L., Senden, Joan M.G., Gijsen, Annemie P., Verdijk, Lex B. +1 more·2013·Clinical Nutrition
DOI 10.1016/j.clnu.2012.09.002
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Abstract

Background & aims It has been speculated that the amount of leucine in a meal largely determines the post-prandial muscle protein synthetic response to food intake. The present study investigates the impact of leucine co-ingestion on subsequent post-prandial muscle protein accretion following the ingestion of a single bolus of dietary protein in elderly males.Methods Twenty-four elderly men (74.3±1.0 y) were randomly assigned to ingest 20 g intrinsically L-[1-(13)C]phenylalanine-labeled casein protein with (PRO+LEU) or without (PRO) 2.5 g crystalline leucine. Ingestion of specifically produced intrinsically labeled protein allowed us to create a plasma phenylalanine enrichment pattern similar to the absorption pattern of phenylalanine from the ingested protein and assess the subsequent post-prandial incorporation of L-[1-(13)C] phenylalanine into muscle protein.Results Plasma amino acid concentrations increased rapidly following protein ingestion in both groups, with higher leucine concentrations observed in the PRO+LEU compared with the PRO group (P<0.01). Plasma L-[1-(13)C]phenylalanine enrichments increased rapidly and to a similar extent in both groups following protein ingestion. Muscle protein-bound L-[1-(13)C]phenylalanine enrichments were significantly greater after PRO+LEU when compared with PRO at 2 h (72%; 0.0078±0.0010 vs. 0.0046±0.00100 MPE, respectively; P<0.05) and 6 h (25%; 0.0232±0.0015 vs. 0.0185±0.0010 MPE, respectively; P<0.05) following protein ingestion. The latter translated into a greater muscle protein synthetic rate following PRO+LEU compared with PRO over the entire 6 h post-prandial period (22%; 0.049±0.003 vs. 0.040±0.003% h(-1), respectively; P<0.05).Conclusion Leucine co-ingestion with a bolus of pure dietary protein further stimulates post-prandial muscle protein synthesis rates in elderly men.

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  • Co-ingestion of leucine with a bolus of pure dietary protein further stimulated postprandial muscle protein synthesis rates in older men.

    “Wall 2012 25 Co-ingestion of leucine with a bolus of pure dietary protein further stimulated postprandial muscle protein synthesis rates in older men.”

    From Evidence-Based Recommendations for Optimal Dietary Protein Intake in Older People: A Position Paper From the PROT-AGE Study Group (2013) · cites this paper as Wall 2012 25

  • The robust postexercise MPS responses to milk, egg, and meat-derived proteins have been attributed to their high essential amino acid content, particularly leucine, a lack of notable amino acid deficiencies, rapid digestibility, and high total digestibility/absorbability.

    “This has been attributed to their high essential amino acid (EAA) content [69], particularly leucine [70], a lack of any notable amino acid deficiencies [71], rapid digestibility [72], and a high total digestibility/absorbability and therefore availability in the circulation (ie, ‘bioavailability’) [72].”

    From Nutritional Considerations for the Vegan Athlete (2023) · cites this paper as [70]

  • Leucine fortification has been shown, though not always, to augment the MPS response to suboptimal doses of animal protein.

    “In line, leucine fortification has been shown [70,97,98], though not always [99], to augment the MPS response to suboptimal doses of animal protein.”

    From Nutritional Considerations for the Vegan Athlete (2023) · cites this paper as [70]

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Authors
Wall, B. T., Hamer, H. M., de Lange, A., Kiskini, A., Groen, B. B. L., Senden, J. M. G., Gijsen, A. P., Verdijk, L. B., & van Loon, L. J. C.
Affiliations
Maastricht University Medical Centre (NL)
ORCID
Venue
Clinical Nutrition
Publisher
Elsevier BV
Published
2013-06
Volume
32
Issue
3
Pages
412-419
ISSN
0261-5614 (ISSN-L)
DOI
10.1016/j.clnu.2012.09.002
OpenAlex
W2079758889
Cited by
220
References
72
Citations by year
2026: 5 · 2025: 11 · 2024: 12 · 2023: 10 · 2022: 16 · 2021: 20 · 2020: 21 · 2019: 18 · 2018: 20 · 2017: 17 · 2016: 21 · 2015: 19 · 2014: 22 · 2013: 7 · 2012: 1
FWCI
7.43
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Clinical Nutrition (publishedVersion)
  • PubMed (publishedVersion)
  • Research Bank (Australian Catholic University) (submittedVersion)
  • Research Publications (Maastricht University) (submittedVersion)
  • VUBIR (Vrije Universiteit Brussel) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
  • Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords
leucine supplementation, muscle protein synthesis, older men, dietary protein, muscle protein accretion, amino acid kinetics, sarcopenia
MeSH terms
Aged, Blood Glucose, Carbon Isotopes, Caseins, Diet, Dietary Proteins, Humans, Insulin, Leucine, Male, Muscle Proteins, Phenylalanine, Muscle, Skeletal, Postprandial Period

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