Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells
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We examined in HepG2 cells whether glucose-induced changes in AMP-activated protein kinase (AMPK) activity could be mediated by SIRT1, an NAD(+)-dependent histone/protein deacetylase that has been linked to the increase in longevity caused by caloric restriction. Incubation with 25 vs. 5mM glucose for 6h concurrently diminished the phosphorylation of AMPK (Thr 172) and ACC (Ser 79), increased lactate release, and decreased the abundance and activity of SIRT1. In contrast, incubation with pyruvate (0.1 and 1mM) for 2h increased AMPK phosphorylation and SIRT1 abundance and activity. The putative SIRT1 activators resveratrol and quercetin also increased AMPK phosphorylation. None of the tested compounds (low or high glucose, pyruvate, and resveratrol) significantly altered the AMP/ATP ratio. Collectively, these findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state.
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In vitro, quercetin increases fatty acid β-oxidation in C2C12 myotubes, hepatocytes, and HeLa cells.
“Quercetin has been reported to modulate fatty acid metabolism in vitro with an increase in fatty acid β-oxidation being reported in C2C12 myotubes, hepatocytes and Hela cells (Suchankova et al., 2009; Eid et al., 2010).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Suchankova et al., 2009
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- Authors
- Suchankova, G., Nelson, L. E., Gerhart-Hines, Z., Kelly, M., Gauthier, M.-S., Saha, A. K., Ido, Y., Puigserver, P., & Ruderman, N. B.
- Affiliations
- Boston Medical Center (US)
- Harvard University (US)
- Corresponding author
- Ruderman, Neil B.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 378
- Issue
- 4
- Pages
- 836-841
- ISSN
- 0006-291X (ISSN-L)
- PMC
- PMC2764524
- OpenAlex
- W2031372661
- Cited by
- 162
- References
- 28
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 6 · 2019: 6 · 2018: 8 · 2017: 8 · 2016: 10 · 2015: 15 · 2014: 14 · 2013: 14 · 2012: 18
- FWCI
- 5.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- National Institutes of Health (5r01dk019514-35)
- National Heart, Lung, and Blood Institute (P01HL068758, P01 HL08758)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK19514, T32DK007201, R01DK067509, DK-67509, F30DK082136, T32DK07201-31, R01-DK-019514)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- AMPK, SIRT1, glucose metabolism, pyruvate, resveratrol, quercetin, AMPK phosphorylation, acetyl-CoA carboxylase, lactate release, redox state, caloric restriction, HepG2 cells, NAD+-dependent deacetylase
- MeSH terms
- Resveratrol, Adenosine Monophosphate, Adenosine Triphosphate, Animals, Cell Line, Glucose, Humans, Muscles, Niacinamide, Oxidation-Reduction, Phosphorylation, Quercetin, Serine, Stilbenes, Threonine, Pyruvic Acid, Sirtuins, Rats, AMP-Activated Protein Kinases, Sirtuin 1
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