IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
Abstract
Muscle atrophy results primarily from accelerated protein degradation and is associated with increased expression of two muscle-specific ubiquitin ligases (E3s): atrogin-1 and muscle ring finger 1 (MuRF1). Glucocorticoids are essential for many types of muscle atrophy, and their effects are opposite to those of insulin-like growth factor I (IGF-I) and insulin, which promote growth. In myotubes, dexamethasone (Dex) inhibited growth and enhanced breakdown of long-lived cell proteins, especially myofibrillar proteins (as measured by 3-methylhistidine release), while also increasing atrogin-1 and MuRF1 mRNA. Conversely, IGF-I suppressed protein degradation and prevented the Dex-induced increase in proteolysis. IGF-I rapidly reduced atrogin-1 expression within 1 h by blocking mRNA synthesis without affecting mRNA degradation, whereas IGF-I decreased MuRF1 mRNA slowly. IGF-I and insulin also blocked Dex induction of these E3s and several other atrophy-related genes (“atrogenes”). Changes in overall proteolysis with Dex and IGF-I correlated tightly with changes in atrogin-1 mRNA content, but not with changes in MuRF1 mRNA. IGF-I activates the phosphatidylinositol 3-kinase (PI3K)-Akt pathway, and inhibition of this pathway [but not the calcineurin-nuclear factor of activated T cell (NFAT) or the MEK-ERK pathway] increased proteolysis and atrogin-1 mRNA expression. Thus an important component of growth stimulation by IGF-I, through the PI3K-Akt pathway, is its ability to rapidly suppress transcription of the atrophy-related E3 atrogin-1 and other atrogenes and degradation of myofibrillar proteins.
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Expression of the ubiquitin ligases atrogin-1 and MuRF-1 in muscle increases dramatically in catabolic states.
“Notably, expression of the ubiquitin ligases atrogin-1 and MuRF-1 in muscle increases dramatically in catabolic states.”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [111]
Atrogin-1 and MuRF-1 could serve as biomarkers for rates of proteolysis and muscle loss.
“Atrogin-1 and MuRF-1 could serve as a biomarker for rates of proteolysis and muscle loss.111”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [111]
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- Authors
- Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2004-10
- Volume
- 287
- Issue
- 4
- Pages
- E591-E601
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2134479830
- Cited by
- 606
- References
- 57
- Citations by year
- 2026: 11 · 2025: 13 · 2024: 13 · 2023: 15 · 2022: 27 · 2021: 21 · 2020: 23 · 2019: 19 · 2018: 26 · 2017: 26 · 2016: 28 · 2015: 22 · 2014: 27 · 2013: 31 · 2012: 49
- FWCI
- 13.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Muscular Dystrophy Association
- National Space Biomedical Research Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- insulin-like growth factor I, muscle atrophy, protein degradation, atrogin-1, MuRF1, ubiquitin ligase, glucocorticoids, dexamethasone, myofibrillar protein degradation, PI3K/Akt signaling, insulin, atrogenes, gene transcription, myotubes
- MeSH terms
- Tripartite Motif Proteins, Phosphoinositide-3 Kinase Inhibitors, Cells, Cultured, Dexamethasone, Enzyme Inhibitors, Humans, Hypoglycemic Agents, Insulin, Insulin Resistance, Insulin-Like Growth Factor I, Methylhistidines, Muscle Proteins, Muscular Atrophy, Myofibrils, RNA, Messenger, Stimulation, Chemical, Blotting, Northern, Gene Expression Regulation, Enzymologic, Muscle, Skeletal, Muscle Fibers, Skeletal, Reverse Transcriptase Polymerase Chain Reaction, Ubiquitin, Myoblasts, Ubiquitin-Protein Ligases, SKP Cullin F-Box Protein Ligases
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