SIRT1 Protein, by Blocking the Activities of Transcription Factors FoxO1 and FoxO3, Inhibits Muscle Atrophy and Promotes Muscle Growth
Open accessAbstract
In several cell types, the protein deacetylase SIRT1 regulates the activities of FoxO transcription factors whose activation is critical in muscle atrophy. However, the possible effects of SIRT1 on the activity of FoxOs in skeletal muscle and on the regulation of muscle size have not been investigated. Here, we show that after food deprivation, SIRT1 levels fall dramatically in type II skeletal muscles (tibialis anterior), which show marked atrophy, unlike in the liver (where SIRT1 rises) or heart or the soleus, a type I muscle (where SIRT1 is unchanged). Maintenance of high SIRT1 levels by electroporation in mouse muscle inhibits markedly the muscle wasting induced by fasting as well as by denervation, and these protective effects require its deacetylase activity. SIRT1 overexpression reduces muscle wasting by blocking the activation of FoxO1 and 3. It thus prevents the induction of key atrogenes, including the muscle-specific ubiquitin ligases, atrogin1 and MuRF1, and multiple autophagy (Atg) genes and the increase in overall proteolysis. In normal muscle, SIRT1 overexpression by electroporation causes rapid fiber hypertrophy without, surprisingly, activation of the PI3K-AKT signaling pathway. Thus, SIRT1 activation favors postnatal muscle growth, and its fall appears to be critical for atrophy during fasting. Consequently, SIRT1 activation represents an attractive possible pharmacological approach to prevent muscle wasting and cachexia.
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Overexpression of SIRT1 reduces muscle dysfunction by inhibiting key atrophy genes in skeletal muscles.
“Overexpression of SIRT1 reduces muscle dysfunction by inhibiting key atrophy genes in skeletal muscles.17”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [17]
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- Authors
- Lee, D., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- ORCID
- Goldberg, Alfred L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 288
- Issue
- 42
- Pages
- 30515-30526
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3798522
- OpenAlex
- W1979153753
- Cited by
- 211
- References
- 50
- Citations by year
- 2026: 10 · 2025: 19 · 2024: 9 · 2023: 22 · 2022: 18 · 2021: 23 · 2020: 13 · 2019: 17 · 2018: 16 · 2017: 15 · 2016: 14 · 2015: 22 · 2014: 13
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- ALS Association
- Muscular Dystrophy Association
- National Institutes of Health
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR055255)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Keywords
- SIRT1, FOXO1, FOXO3, muscle atrophy, muscle growth, skeletal muscle, fasting, denervation, atrogenes, atrogin-1, MuRF1, autophagy, proteolysis, protein deacetylase, muscle fiber hypertrophy, cachexia, PI3K/Akt signaling
- MeSH terms
- Tripartite Motif Proteins, Forkhead Box Protein O1, Forkhead Box Protein O3, Animals, Cachexia, Fasting, Male, Muscle Proteins, Muscular Atrophy, Signal Transduction, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Ubiquitin-Protein Ligases, SKP Cullin F-Box Protein Ligases, Proto-Oncogene Proteins c-akt, Mice, Forkhead Transcription Factors, Sirtuin 1
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