Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
Open accessAbstract
SIRT3 is a member of the sirtuin family of NAD(+)-dependent deacetylases, which is localized to the mitochondria and is enriched in kidney, brown adipose tissue, heart, and other metabolically active tissues. We report here that SIRT3 responds dynamically to both exercise and nutritional signals in skeletal muscle to coordinate downstream molecular responses. We show that exercise training increases SIRT3 expression as well as associated CREB phosphorylation and PGC-1alpha up-regulation. Furthermore, we show that SIRT3 is more highly expressed in slow oxidative type I soleus muscle compared to fast type II extensor digitorum longus or gastrocnemius muscles. Additionally, we find that SIRT3 protein levels in skeletal muscle are sensitive to diet, for SIRT3 expression increases by fasting and caloric restriction, yet it is decreased by high-fat diet. Interestingly, the caloric restriction regimen also leads to phospho-activation of AMPK in muscle. Conversely in SIRT3 knockout mice, we find that the phosphorylation of both AMPK and CREB and the expression of PGC-1alpha are down regulated, suggesting that these key cellular factors may be important components of SIRT3-mediated biological signals in vivo.
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SIRT3 regulates energy metabolism and fatty acid β-oxidation by regulating AMPK phosphorylation and PGC1α expression, as shown by decreased phosphorylated AMPK:total AMPK ratio and downregulation of PGC1α in skeletal muscle of SIRT3 KO mice.
“SIRT3 appears to regulate energy metabolism and, particularly, fatty acid β-oxidation, by regulating AMPK phosphorylation and PGC 1α expression as demonstrated by the decrease in phosphorylated AMPK:total AMPK ratio and the downregulation of PGC 1α in the skeletal muscle of SIRT3 KO mice (Palacios et al., 2009).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Palacios et al., 2009
A high-fat diet downregulates the protein levels of SIRT3.
“Finally, a high-fat diet has also been reported to downregulate the protein levels of SIRT3 (Palacios et al., 2009)”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Palacios et al., 2009
SIRT3 is a key regulator of mitochondrial energy metabolism.
“which represents a key regulator of mitochondrial energy metabolism (Palacios et al., 2009; Hirschey et al., 2010, 2011; Anderson and Hirschey, 2012).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Palacios et al., 2009
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Dietary restriction.; mitochondrial function and aging: From yeast to humans
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“Furthermore, SIRT3 KO mice show repression of PGC1α down regulation and low levels of AMPK phosphorylation after CR indicating a key 9 role of this mitochondrial sirtuin in metabolic adaptation to calorie intake (Palacios et al., 2009).”
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Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3
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Self-citationLipotoxicity, aging, and muscle contractility: does fiber type matter?
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Dietary ursolic acid improves health span and life span in male <i>Drosophila melanogaster</i>
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Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion
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- Authors
- Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q.
- Affiliations
- Baylor College of Medicine (US)
- Howard Hughes Medical Institute (US)
- Paul F. Glenn Laboratories for the Biological Mechanisms of Aging, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA
- Brigham and Women's Hospital (US)
- USDA/ARS Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030, USA
- Corresponding author
- Tong, Qiang
- Venue
- Aging
- Publisher
- Impact Journals, LLC
- Published
- 2009-08-15
- Volume
- 1
- Issue
- 9
- Pages
- 771-783
- ISSN
- 1945-4589 (ISSN-L)
- PMC
- PMC2815736
- OpenAlex
- W1762535185
- Cited by
- 487
- References
- 63
- Citations by year
- 2026: 11 · 2025: 21 · 2024: 13 · 2023: 20 · 2022: 29 · 2021: 31 · 2020: 25 · 2019: 34 · 2018: 44 · 2017: 24 · 2016: 31 · 2015: 35 · 2014: 44 · 2013: 42 · 2012: 41
- FWCI
- 19.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Aging (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Agriculture (6250‐51000)
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK068626, R01DK075978)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (T32HD007445)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- SIRT3, sirtuins, AMPK, PGC-1α, skeletal muscle, exercise training, caloric restriction, fasting, high-fat diet, CREB phosphorylation, mitochondrial deacetylase, muscle fiber type, SIRT3 knockout mice, mitochondrial biogenesis
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Animal Structures, Citrate (si)-Synthase, Diet, Fasting, Female, Male, Mice, Inbred BALB C, Mice, Inbred C57BL, Phosphorylation, Physical Conditioning, Animal, Sex Characteristics, Transcription Factors, Trans-Activators, Cyclic AMP Response Element-Binding Protein, Mice, Knockout, Muscle, Skeletal, Caloric Restriction, Mice, AMP-Activated Protein Kinases, Sirtuin 3
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