Impaired anabolic response of muscle protein synthesis is associated with S6K1 dysregulation in elderly humans
Abstract
Age‐related loss of muscle protein may involve a decreased response to anabolic factors of muscle protein synthesis through dysregulation of translation factors. To verify this hypothesis, we simultaneously investigated muscle protein synthesis and expression of some factors implicated in insulin signal transduction during hyperinsulinemia and hyperaminoacidemia in 6 young (25±1 year; mean± SEM ) and 8 elderly subjects (72±2 year). Incorporation of L‐[1‐ 13 C] leucine in muscle proteins (fractional synthesis rate, FSR) was measured in vastus lateralis, before and during a euglycemic hyperinsulinemic hyperaminoacidemic clamp, together with Western blot analysis of protein kinase B (PKB), mTOR, 4E‐BP1, and S6K1 phosphorylation. In basal state, muscle protein FSR was reduced in elderly in comparison with young subjects (0.061±0.004% per hour) vs 0.082±0.010% per hour, elderly vs. young, P <0.05). During clamp, muscle protein FSR was stimulated in young (0.119±0.006% per hour; P <0.05), but this response was significantly lower in elderly subjects (0.084±0.005% per hour, P <0.05 vs young subjects). Phosphorylation of PKB, mTOR, and 4E‐BP1 were similarly increased by insulin and amino acid in both groups, except for S6K1 phosphorylation, which was not stimulated in elderly subjects. In conclusion, 1) response of muscle protein synthesis to insulin and amino acid is impaired in elderly humans; 2) a defect in S6K1 pathway activation may be responsible for this alteration. This modification is a mechanistic basis of sarcopenia development during aging.
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In the fed state, most researchers agree there is an impairment of the muscle protein anabolic response to meal intake in older adults, although some studies found no difference, especially with high amino acid or protein amounts.
“In the fed state, however, most researchers now agree that there is an impairment of the muscle protein anabolic response to meal intake in older adults, 46,49,50 although some studies found no difference between older and younger adults, especially when high amounts of amino acids or proteins were administered.”
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 [46]
With aging, the body's anabolic response to dietary protein or amino acids is limited.
“With aging, the normal balance between muscle protein synthesis and degradation is shifted toward net catabolism, the body's anabolic response to dietary protein or amino acids is limited, 46,120,122,123 and the normal antiproteolytic response to insulin is impaired.46,124,125”
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 [46]
With aging, the normal balance between muscle protein synthesis and degradation is shifted toward net catabolism.
“With aging, the normal balance between muscle protein synthesis and degradation is shifted toward net catabolism, the body's anabolic response to dietary protein or amino acids is limited, 46,120,122,123 and the normal antiproteolytic response to insulin is impaired.46,124,125”
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 [46]
With aging, the normal antiproteolytic response to insulin is impaired.
“With aging, the normal balance between muscle protein synthesis and degradation is shifted toward net catabolism, the body's anabolic response to dietary protein or amino acids is limited, 46,120,122,123 and the normal antiproteolytic response to insulin is impaired.46,124,125”
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 [46]
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- Authors
- Guillet, C., Prod'homme, M., Balage, M., Gachon, P., Giraudet, C., Morin, L., Grizard, J., & Boirie, Y.
- Affiliations
- Centre Hospitalier Universitaire de Clermont-Ferrand (FR)
- Unité de Nutrition et du Métabolisme Protéique, INRA‐Theix CRNH Clermont‐Ferrand France
- Centre de Recherche en Nutrition Humaine d'Auvergne (FR)
- Unité du Métabolisme Protéino‐Energétique UMR Université d'Auvergne/INRA CRNH Centre Hospitalier Universitaire Clermont‐Ferrand France
- ORCID
- Guillet, Christelle
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2004-08-19
- Volume
- 18
- Issue
- 13
- Pages
- 1586-1587
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2072998904
- Cited by
- 412
- References
- 4
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 13 · 2023: 14 · 2022: 16 · 2021: 9 · 2020: 20 · 2019: 21 · 2018: 25 · 2017: 23 · 2016: 29 · 2015: 24 · 2014: 18 · 2013: 27 · 2012: 29
- FWCI
- 4.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- 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
- muscle protein synthesis, sarcopenia, aging, S6K1, mTOR signaling, insulin signaling, leucine incorporation, Akt, 4E-BP1, translation factors, older adults
- MeSH terms
- Adult, Aged, Aging, Amino Acids, Enzyme Activation, Humans, Insulin, Muscle Proteins, Muscles, Phosphorylation, Ribosomal Protein S6 Kinases, 70-kDa, Anabolic Agents
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