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Effect of branched-chain amino acids on muscle atrophy in cancer cachexia
Open accessAbstract
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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“In cachexia-inducing tumor Naval Medical Research Institute mice with a significant suppression in the loss of body weight, leucine or valine could increase protein synthesis and attenuate the increased protein degradation [26].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [26]
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Metadata
- 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
- 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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