SIRT1: recent lessons from mouse models (original) (raw)

• Michan, S. & Sinclair, D. Sirtuins in mammals: insights into their biological function. Biochem. J. 404, 1–13 (2007).
  Article CAS Google Scholar
• Kaeberlein, M., McVey, M. & Guarente, L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570–2580 (1999).
  Article CAS Google Scholar
• Tissenbaum, H. A. & Guarente, L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227–230 (2001).
  Article CAS Google Scholar
• Rogina, B. & Helfand, S. L. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl Acad. Sci. USA 101, 15998–16003 (2004).
  Article CAS Google Scholar
• Howitz, K. T. et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191–196 (2003).
  Article CAS Google Scholar
• Wood, J. G. et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430, 686–689 (2004).
  Article CAS Google Scholar
• Lin, S. J., Defossez, P. A. & Guarente, L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289, 2126–2128 (2000).
  Article CAS Google Scholar
• Kaeberlein, M., Kirkland, K. T., Fields, S. & Kennedy, B. K. Sir2-independent life span extension by calorie restriction in yeast. PLoS Biol. 2, e296 (2004).
  Article Google Scholar
• Fabrizio, P. et al. Sir2 blocks extreme life-span extension. Cell 123, 655–667 (2005).
  Article CAS Google Scholar
• Bass, T. M., Weinkove, D., Houthoofd, K., Gems, D. & Partridge, L. Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans. Mech. Ageing Dev. 128, 546–552 (2007).
  Article CAS Google Scholar
• Baur, J. A. et al. Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444, 337–342 (2006).
  CAS PubMed PubMed Central Google Scholar
• Lagouge, M. et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1α. Cell 127, 1109–1122 (2006).
  Article CAS Google Scholar
• Pearson, K. J. et al. Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span. Cell Metab. 8, 157–168 (2008).
  Article CAS Google Scholar
• Kaeberlein, M. et al. Substrate-specific activation of sirtuins by resveratrol. J. Biol. Chem. 280, 17038–17045 (2005).
  Article CAS Google Scholar
• Beher, D. et al. Resveratrol is not a direct activator of SIRT1 enzyme activity. Chem. Biol. Drug Des. 74, 619–624 (2009).
  Article CAS Google Scholar
• Pacholec, M. et al. SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J. Biol. Chem. 285, 8340–8351 (2010).
  Article CAS Google Scholar
• Canto, C. et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458, 1056–1060 (2009).
  Article CAS Google Scholar
• Hawley, S. A. et al. Use of cells expressing γ subunit variants to identify diverse mechanisms of AMPK activation. Cell Metab. 11, 554–565 (2010).
  Article CAS Google Scholar
• Garber, K. A mid-life crisis for aging theory. Nature Biotech. 26, 371–374 (2008).
  Article CAS Google Scholar
• Luo, J. et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137–148 (2001).
  Article CAS Google Scholar
• Vaziri, H. et al. hSIR2SIRT1 functions as an NAD-dependent p53 deacetylase. Cell 107, 149–159 (2001).
  Article CAS Google Scholar
• Cheng, H. L. et al. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc. Natl Acad. Sci. USA 100, 10794–10799 (2003).
  Article CAS Google Scholar
• Kamel, C., Abrol, M., Jardine, K., He, X. & McBurney, M. W. SirT1 fails to affect p53-mediated biological functions. Aging Cell 5, 81–88 (2006).
  Article CAS Google Scholar
• Deng, C. X. SIRT1, is it a tumor promoter or tumor suppressor? Int. J. Biol. Sci. 5, 147–152 (2009).
  Article CAS Google Scholar
• Firestein, R. et al. The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS ONE 3, e2020 (2008).
  Article Google Scholar
• Herranz, D. et al. Sirt1 improves healthy ageing and protects from metabolic syndrome -associated cancer. Nature Commun. 12 Apr 2010 (doi:10.1038/ncomms1001).
• Oberdoerffer, P. et al. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135, 907–918 (2008).
  Article CAS Google Scholar
• Wang, R. H. et al. Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell 14, 312–323 (2008).
  Article CAS Google Scholar
• Brooks, C. L. & Gu, W. How does SIRT1 affect metabolism, senescence and cancer? Nature Rev. Cancer 9, 123–128 (2009).
  Article CAS Google Scholar
• Haigis, M. C. & Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253–295 (2010).
  Article CAS Google Scholar
• Moynihan, K. A. et al. Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice. Cell Metab. 2, 105–117 (2005).
  Article CAS Google Scholar
• Bordone, L. et al. SIRT1 transgenic mice show phenotypes resembling calorie restriction. Aging Cell 6, 759–767 (2007).
  Article CAS Google Scholar
• Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M. & Tschop, M. H. Sirt1 protects against high-fat diet-induced metabolic damage. Proc. Natl Acad. Sci. USA 105, 9793–9798 (2008).
  Article CAS Google Scholar
• Banks, A. S. et al. SirT1 gain of function increases energy efficiency and prevents diabetes in mice. Cell Metab. 8, 333–341 (2008).
  Article CAS Google Scholar
• Escande, C. et al. Deleted in breast cancer-1 regulates SIRT1 activity and contributes to high-fat diet-induced liver steatosis in mice. J. Clin. Invest. 120, 545–558 (2010).
  Article CAS Google Scholar
• Xu, F. et al. Lack of SIRT1 (Mammalian Sirtuin 1) activity leads to liver steatosis in the SIRT1+/− mice: a role of lipid mobilization and inflammation. Endocrinology 151, 2504–2514 (2010).
  Article CAS Google Scholar
• Schug, T. T. et al. Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress. Mol. Cell. Biol. 30, 4712–4721 (2010).
  Article CAS Google Scholar
• Cohen, D. E., Supinski, A. M., Bonkowski, M. S., Donmez, G. & Guarente, L. P. Neuronal SIRT1 regulates endocrine and behavioral responses to calorie restriction. Genes Dev. 23, 2812–2817 (2009).
  Article CAS Google Scholar
• Ramadori, G. et al. SIRT1 deacetylase in POMC neurons is required for homeostatic defenses against diet-induced obesity. Cell Metab. 12, 78–87 (2010).
  Article CAS Google Scholar
• Purushotham, A. et al. Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 9, 327–338 (2009).
  Article CAS Google Scholar
• Chen, D. et al. Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 22, 1753–1757 (2008).
  Article CAS Google Scholar
• Bordone, L. et al. Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic β cells. PLoS Biol. 4, e31 (2006).
  Article Google Scholar
• Li, X. et al. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 28, 91–106 (2007).
  Article Google Scholar
• McBurney, M. W. et al. The mammalian SIR2α protein has a role in embryogenesis and gametogenesis. Mol. Cell. Biol. 23, 38–54 (2003).
  Article CAS Google Scholar
• Yeung, F. et al. Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23, 2369–2380 (2004).
  Article CAS Google Scholar
• Kemper, J. K. et al. FXR acetylation is normally dynamically regulated by p300 and SIRT1 but constitutively elevated in metabolic disease states. Cell Metab. 10, 392–404 (2009).
  Article CAS Google Scholar
• Rodgers, J. T. et al. Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature 434, 113–118 (2005).
  Article CAS Google Scholar
• Walker, A. K. et al. Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP. Genes Dev. 24, 1403–1417 (2010).
  Article CAS Google Scholar
• Ponugoti, B. et al. SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism. J. Biol. Chem. 285, 33959–33970 (2010).
  Article CAS Google Scholar
• Picard, F. et al. Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature 429, 771–776 (2004).
  Article CAS Google Scholar
• Kim, H. S. et al. Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metab. 12, 224–236 (2010).
  Article CAS Google Scholar
• Kanfi, Y. et al. SIRT6 protects against pathological damage caused by diet-induced obesity. Aging Cell 9, 162–173 (2010).
  Article CAS Google Scholar
• Hou, X. et al. SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase. J. Biol. Chem. 283, 20015–20026 (2008).
  Article CAS Google Scholar
• Lan, F., Cacicedo, J. M., Ruderman, N. & Ido, Y. SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J. Biol. Chem. 283, 27628–27635 (2008).
  Article CAS Google Scholar
• Guarente, L. Sirtuins as potential targets for metabolic syndrome. Nature 444, 868–874 (2006).
  Article CAS Google Scholar
• Alcendor, R. R. et al. Sirt1 regulates aging and resistance to oxidative stress in the heart. Circ. Res. 100, 1512–1521 (2007).
  Article CAS Google Scholar
• Zhang, Q. J. et al. Endothelium-specific overexpression of class III deacetylase SIRT1 decreases atherosclerosis in apolipoprotein E-deficient mice. Cardiovasc. Res. 80, 191–199 (2008).
  Article CAS Google Scholar
• Stein, S. et al. SIRT1 reduces endothelial activation without affecting vascular function in ApoE−/− mice. Aging (Albany NY) 2, 353–360 (2010).
  Article CAS Google Scholar
• Stein, S. et al. SIRT1 decreases Lox-1-mediated foam cell formation in atherogenesis. Eur. Heart J. 31, 2301–2309 (2010).
  Article CAS Google Scholar
• Park, E. J. et al. Dietary and genetic obesity promote liver inflammation and tumorigenesis by enhancing IL-6 and TNF expression. Cell 140, 197–208 (2010).
  Article CAS Google Scholar
• Kabra, N. et al. SirT1 is an inhibitor of proliferation and tumor formation in colon cancer. J. Biol. Chem. 284, 18210–18217 (2009).
  Article CAS Google Scholar
• Boily, G., He, X. H., Pearce, B., Jardine, K. & McBurney, M. W. SirT1-null mice develop tumors at normal rates but are poorly protected by resveratrol. Oncogene 28, 2882–2893 (2009).
  Article CAS Google Scholar
• Kim, D. et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J. 26, 3169–3179 (2007).
  Article CAS Google Scholar
• Donmez, G., Wang, D., Cohen, D. E. & Guarente, L. Sirt1 supresses β-amyloid production by activating the α-secretase gene ADAM10. Cell 142, 320–332 (2010).
  Article CAS Google Scholar
• Boily, G. et al. SirT1 regulates energy metabolism and response to caloric restriction in mice. PLoS ONE 3, e1759 (2008).
  Article Google Scholar
• Chen, D., Steele, A. D., Lindquist, S. & Guarente, L. Increase in activity during calorie restriction requires Sirt1. Science 310, 1641 (2005).
  Article CAS Google Scholar
• Qin, W. et al. Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J. Biol. Chem. 281, 21745–21754 (2006).
  Article CAS Google Scholar
• Satoh, A. et al. SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus. J. Neurosci. 30, 10220–10232 (2010).
  Article CAS Google Scholar
• Kume, S. et al. Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney. J. Clin. Invest. 120, 1043–1055 (2010).
  Article CAS Google Scholar
• Zheng, J. & Ramirez, V. D. Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals. Br. J. Pharmacol. 130, 1115–1123 (2000).
  Article CAS Google Scholar
• Gledhill, J. R., Montgomery, M. G., Leslie, A. G. & Walker, J. E. Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols. Proc. Natl Acad. Sci. USA 104, 13632–13637 (2007).
  Article CAS Google Scholar