SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function
Open accessAbstract
Resveratrol induces mitochondrial biogenesis and protects against metabolic decline, but whether SIRT1 mediates these benefits is the subject of debate. To circumvent the developmental defects of germline SIRT1 knockouts, we have developed an inducible system that permits whole-body deletion of SIRT1 in adult mice. Mice treated with a moderate dose of resveratrol showed increased mitochondrial biogenesis and function, AMPK activation, and increased NAD(+) levels in skeletal muscle, whereas SIRT1 knockouts displayed none of these benefits. A mouse overexpressing SIRT1 mimicked these effects. A high dose of resveratrol activated AMPK in a SIRT1-independent manner, demonstrating that resveratrol dosage is a critical factor. Importantly, at both doses of resveratrol no improvements in mitochondrial function were observed in animals lacking SIRT1. Together these data indicate that SIRT1 plays an essential role in the ability of moderate doses of resveratrol to stimulate AMPK and improve mitochondrial function both in vitro and in vivo.
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Resveratrol can inhibit the activity of phosphodiesterases (PDE), particularly PDE4, thus increasing intracellular cAMP.
“As for other mechanisms of action of resveratrol, experimental evidence has shown that this polyphenol can inhibit the activity of phosphodiesterases (PDE) and in particular of the PDE4 isoform, thus increasing the intracellular levels of cyclic adenosine monophosphate (cAMP) [17].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [17]
In a SIRT-1 knock-out mouse model, resveratrol is unable to induce AMPK phosphorylation at a low dose, but AMPK phosphorylation is observed at a 10 times higher dose.
“Indeed, in a SIRT-1 knock-out mouse model, resveratrol is unable to induce AMPK phosphorylation at a low dose. In contrast, AMPK phosphorylation was observed at 10 times higher dose.”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [17]
Resveratrol can phosphorylate AMPK in a dose-dependent manner and independently of SIRT-1.
“These results, therefore, indicate that resveratrol can phosphorylate AMPK in a dose-dependent manner and independently of SIRT-1 [17].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [17]
Sirtuin-regulated mitochondrial activity acts directly on stem cells and also indirectly alters ROS and nutrient sensing, further changing stem cell phenotypes.
“Likewise, mitochondrial function, largely regulated by sirtuins, not only affects stem cell functions directly but also causes secondary effects on ROS and nutrient-sensing activities, which further modulate stem cell phenotypes29,30,108,113,184.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [184]
AMPK and SIRT1 participate in a positive feedback loop that engages both sensors of low-energy states into a univocal response.
“Notably, AMPK and SIRT1 participate in a positive feedback loop that engages both sensors of low-energy states into a univocal response.227”
From Meta-hallmarks of aging and cancer (2023) · cites this paper as [227]
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sirt1-null mice develop an autoimmune-like condition
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“SIRT1-iKO mice were fed tamoxifen (360 mg/kg) diet for five weeks to elicit whole-body SIRT1 exon 4 excision as described previously (Price et al., 2012).”
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Zemel, M. B. (2020) · Journal of Medicinal Food · doi:10.1089/jmf.2020.0105 · Cited by 12 · see citing works
- Authors
- Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., Hubbard, B. P., Varela, A. T., Davis, J. G., Varamini, B., Hafner, A., Moaddel, R., Rolo, A. P., Coppari, R., Palmeira, C. M., de Cabo, R., Baur, J. A., & Sinclair, D. A.
- Affiliations
- Harvard University (US)
- Centro de Neurociências e Biologia Celular (PT)
- University of Pennsylvania (US)
- The University of Texas Southwestern Medical Center (US)
- National Institutes of Health (US)
- Marche Polytechnic University (IT)
- Corresponding author
- Sinclair, David A.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 15
- Issue
- 5
- Pages
- 675-690
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC3545644
- OpenAlex
- W2078575160
- Cited by
- 1,602
- References
- 103
- Citations by year
- 2026: 99 · 2025: 103 · 2024: 115 · 2023: 86 · 2022: 120 · 2021: 139 · 2020: 130 · 2019: 121 · 2018: 87 · 2017: 124 · 2016: 98 · 2015: 121 · 2014: 120 · 2013: 92 · 2012: 43
- FWCI
- 59.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- National Institute on Aging (R37AG028730, P01AG027916, R01AG028730, R01AG019719)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK080836, R01DK080836)
- National Center for Research Resources
- 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
- SIRT1, AMPK activation, resveratrol, mitochondrial biogenesis, mitochondrial function, NAD levels, skeletal muscle, SIRT1 overexpression, dose-dependent effects, metabolic decline
- MeSH terms
- Resveratrol, AMP-Activated Protein Kinase Kinases, Animals, Cells, Cultured, Enzyme Activation, Mice, Inbred C57BL, Mitochondria, NAD, Protein Kinases, Stilbenes, Signal Transduction, Mice, Knockout, Muscle, Skeletal, Hepatocytes, Mice, Sirtuin 1
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