Cited by 184Muscle metabolism and nutritionMuscle Physiology and DisordersNutrition and Health in Aging

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Effect of branched-chain amino acids on muscle atrophy in cancer cachexia

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Eley, Helen L., Russell, Steven T., Tisdale, Michael J.·2007·Biochemical Journal

DOI 10.1042/bj20070651PMC PMC2267397

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Abstract

In the present study, the BCAAs (branched-chain amino acids) leucine and valine caused a significant suppression in the loss of body weight in mice bearing a cachexia-inducing tumour (MAC16), producing a significant increase in skeletal muscle wet weight, through an increase in protein synthesis and a decrease in degradation. Leucine attenuated the increased phosphorylation of PKR (double-stranded-RNA-dependent protein kinase) and eIF2alpha (eukaryotic initiation factor 2alpha) in skeletal muscle of mice bearing the MAC16 tumour, due to an increased expression of PP1 (protein phosphatase 1). Weight loss in mice bearing the MAC16 tumour was associated with an increased amount of eIF4E bound to its binding protein 4E-BP1 (eIF4E-binding protein 1), and a progressive decrease in the active eIF4G-eIF4E complex due to hypophosphorylation of 4E-BP1. This may be due to a reduction in the phosphorylation of mTOR (mammalian target of rapamycin), which may also be responsible for the decreased phosphorylation of p70(S6k) (70 kDa ribosomal S6 kinase). There was also a 5-fold increase in the phosphorylation of eEF2 (eukaryotic elongation factor 2), which would also decrease protein synthesis through a decrease in translation elongation. Treatment with leucine increased phosphorylation of mTOR and p70(S6k), caused hyperphosphorylation of 4E-BP1, reduced the amount of 4E-BP1 associated with eIF4E and caused an increase in the eIF4G-eIF4E complex, together with a reduction in phosphorylation of eEF2. These changes would be expected to increase protein synthesis, whereas a reduction in the activation of PKR would be expected to attenuate the increased protein degradation.

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Authors: Eley, H. L., Russell, S. T., & Tisdale, M. J.
Affiliations: Aston University (GB)
ORCID: Russell, Steven T.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2007-09-12
Volume: 407
Issue: 1
Pages: 113-120
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20070651
PMC: PMC2267397
OpenAlex: W2112898640
Cited by: 184
References: 40
Citations by year: 2026: 6 · 2025: 5 · 2024: 8 · 2023: 13 · 2022: 6 · 2021: 9 · 2020: 13 · 2019: 10 · 2018: 10 · 2017: 12 · 2016: 7 · 2015: 11 · 2014: 11 · 2013: 11 · 2012: 10
FWCI: 4.69
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
Keywords: branched-chain amino acids, leucine, valine, cancer cachexia, muscle atrophy, skeletal muscle protein synthesis, protein degradation, eIF2α, protein phosphatase 1, 4E-BP1, eIF4E, mTOR, p70S6K, elongation factor 2, weight loss
MeSH terms: Amino Acids, Branched-Chain, Animals, Cachexia, Carrier Proteins, Cells, Cultured, Leucine, Mice, Inbred Strains, Muscular Atrophy, Neoplasms, Phosphoproteins, Phosphorylation, Protein Kinases, Proteoglycans, Time Factors, Valine, Cell Cycle Proteins, Myoblasts, Eukaryotic Initiation Factor-4E, Eukaryotic Initiation Factor-4G, Eukaryotic Initiation Factors, Adaptor Proteins, Signal Transducing, Mice

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Effect of branched-chain amino acids on muscle atrophy in cancer cachexia

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