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Sirtuin Functions in Health and Disease
Open accessAbstract
Sirtuins or Sir2 (silent information regulator 2)-related enzymes have originally been defined as a family of nicotinamide adenine dinucleotide-dependent enzymes that deacetylate lysine residue on various proteins. Certain sirtuins have in addition an ADP-ribosyltransferase activity. The sirtuins are remarkably conserved throughout evolution from archaebacteria to eukaryotes. The mammalian sirtuins SIRT1-SIRT7 are implicated in a variety of cellular functions ranging from gene silencing, over the control of the cell cycle and apoptosis, to energy homeostasis. On a whole-body level, the wide range of cellular activities of the sirtuins suggests that they could constitute therapeutic targets to combat metabolic, neurodegenerative, and proliferative diseases. Here, we review some of the recent data related to the sirtuins and discuss their mode of action, their biological role in cellular and organismal models, and their possible association to age-related human diseases.
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“A higher intake of soya isoflavones (114 mg/d) for 3 months also did not reduce serum CRP or sE-selectin concentrations in postmenopausal women (814) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [814]
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“However, SRT1720 has been shown in BAT to modify lipid droplet size and gene expression 157,158.”
From Cellular bioenergetics as a target for obesity therapy (2010) · cites this paper as [157]
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“Sirtuins, a family of NAD+-dependent deacetylases, have recently emerged as integral components of these metabolic networks, which are particularly important for energy homeostasis (Guarente, 2006; Michan and Sinclair, 2007; Yamamoto et al., 2007).”
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Tseng, Y.-H., Cypess, A. M., & Kahn, C. R. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3138 · Cited by 591
“However, SRT1720 has been shown in BAT to modify lipid droplet size and gene expressio”
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Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
“For extensive discussion of the actions of other sirtuin members, we refer the reader to reviews elsewhere (Dali-Youcef et al., 2007; Michan and Sinclair, 2007; Yamamoto et al., 2007; Schwer and Verdin, 2008; Finkel et al., 2009; Guarente, 2011).”
Self-citationSirtuins — novel therapeutic targets to treat age-associated diseases
Lavu, S., Boss, O., Elliott, P. J., & Lambert, P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2665 · Cited by 427
“Metabolic disease Overexpression or activation of SIRT1 has been shown to modulate mitochondrial biogenesis, metabolic rate, insulin sensitivity, glucose and lipid metabolis”
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SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310
Rothgiesser, K. M., Erener, S., Waibel, S., Lüscher, B., & Hottiger, M. O. (2010) · Journal of Cell Science · doi:10.1242/jcs.073783 · Cited by 345
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BackgroundBrown fat as a therapy for obesity and diabetes
Cypess, A. M., & Kahn, C. R. (2010) · Current Opinion in Endocrinology, Diabetes & Obesity · doi:10.1097/med.0b013e328337a81f · Cited by 376
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“The list of Sirt1 substrates is continuously growing and includes several transcription factors: the tumor suppressor protein p53, members of the FoxO family (forkhead box factors regulated by insulin/Akt), HES1 (hairy and enhancer of split 1), HEY2 (hairy/enhancer-of-split related with YRPW motif 2), PPARg (peroxisom…”
BackgroundGenerating specificity and diversity in the transcriptional response to hypoxia
Lendahl, U., Lee, K. L., Yang, H. H., & Poellinger, L. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2665 · Cited by 333
“SIRT1 has already been shown to protect against metabolic, genotoxic and thermal stress by deacetylating key transcriptional regulators, such as PPARγ coactivator 1α (PGC1α), p53 and heat shock factor 1 (HSF1), that respond to these stress stimul”
BackgroundUse of Epigenetic Drugs in Disease: An Overview
Heerboth, S. A., LAPINSKA, K., Snyder, N., Leary, M., Rollinson, S., & Sarkar, S. (2014) · Genetics & Epigenetics · doi:10.4137/geg.s12270 · Cited by 333
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Nuclear Receptor Coregulators and Human Disease
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The Beneficial Roles of SIRT1 in Neuroinflammation-Related Diseases
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“Sirtuins contain a conserved catalytic domain, NAD binding domains, and flanking variable NH2- and COOHterminal regions [19, 20] (Figure 1).”
BackgroundThe Sirtuin family: therapeutic targets to treat diseases of aging
Milne, J. C., & Denu, J. M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.019 · Cited by 274
Vascular smooth muscle cell sirtuin 1 protects against DNA damage and inhibits atherosclerosis
Gorenne, I., Kumar, S., Gray, K., Figg, N., Yu, H., Mercer, J., & Bennett, M. (2013) · Circulation · doi:10.1161/circulationaha.112.124404 · Cited by 238
“ing some forms of neurodegeneration, cancer, and metabolic decline including glucose intolerance and insulin resistance.(7) SIRT1 deacetylase targets include histone proteins and several transcription factors, including p53,(8,9) E2F-1,(10) and forkhead genes,(11) to suppress DNA damage-induced apoptosis.”
BackgroundEpigenetic regulation in the pathophysiology of Alzheimer's disease
Chouliaras, L., Rutten, B. P. F., Kenis, G., Peerbooms, O., Visser, P. J., Verhey, F., van Os, J., Steinbusch, H. W. M., & van den Hove, D. L. A. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.01.002 · Cited by 262
The influence of diet on anti-cancer immune responsiveness
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“In particular, resveratrol is able to activate sirtuins (SIRT), a class of proteins that possesses deacetylase or monoribosyltransferase activity [191].”
BackgroundNegative regulation of inflammation by SIRT1
Xie, J., Zhang, X., & Zhang, L. (2013) · Pharmacological Research · doi:10.1016/j.phrs.2012.10.010 · Cited by 234
“[17] Yamamoto H, Schoonjans K, Auwerx J.”
Trials with ‘epigenetic’ drugs: An update
Nebbioso, A., Carafa, V., Benedetti, R., & Altucci, L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.004 · Cited by 242
“In contrast, SirT4 and 6, catalyze ADP- ribosylation reaction, during which ADP-ribosyl moiety is transferred to the protein substrate (Yamamoto et al., 2007).”
BackgroundFunction of the SIRT1 protein deacetylase in cancer
Stünkel, W., Peh, B. K., Tan, Y. C., Nayagam, V. M., Wang, X., Salto‐Tellez, M., Ni, B., Entzeroth, M., & Wood, J. M. (2007) · Biotechnology Journal · doi:10.1002/biot.200700087 · Cited by 236
Stealing the Keys to the Kitchen: Viral Manipulation of the Host Cell Metabolic Network
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“Sirtuins are evolutionarily conserved NAD-dependent enzymes whose family members enzymatically regulate a number of protein post-translational modifications, including ADP-ribosylation, acetylation, and acylation (reviewed in [79]).”
BackgroundZhang, C., Feng, Y., Qu, S., Wei, X., Zhu, H., Luo, Q., Liu, M., Chen, G., & Xiao, X. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr022 · Cited by 214
“SIRT1 is implicated in various cellular functions, ranging from gene silencing, the control of the cell cycle, and apoptosis to energy homeostasis.(20) Most importantly, SIRT1 could deacetylate p53 and attenuate its ability to transactivate its downstream target genes, such as p21 for cell-cycle arrest and Bax for apo…”
BackgroundProtective effects and mechanisms of sirtuins in the nervous system
Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211
Sirtuin/Sir2 Phylogeny, Evolutionary Considerations and Structural Conservation
Greiss, S., & Gartner, A. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0169-x · Cited by 217
“It has roles in developmental and aging regulation (Yamamoto et al., 2007), and recent evidence also points towards a role in ensuring efficient DNA double-strand break repair (Oberdoerffer et al.”
BackgroundMortuza, R., Chen, S., Feng, B., Sen, S., & Chakrabarti, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054514 · Cited by 208
“Although isolated SIRT alterations have been demonstrated in various studies [19,20,41–43], such comprehensive analysis of SIRTs have not been done.”
BackgroundTranscriptional targets of sirtuins in the coordination of mammalian physiology
Feige, J. N., & Auwerx, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.012 · Cited by 209
“In mammals, only Sirt1–Sirt3, Sirt5 and Sirt6 have a conserved deacetylase domain [1,2], and HDAC activity seems restricted to Sirt1–Sirt3 and Sirt6.”
BackgroundSelf-citationEmerging therapeutic roles for NAD+ metabolism in mitochondrial and age‐related disorders
Srivastava, S. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0104-7 · Cited by 200
“Mammals contain seven sirtuins (SIRT1–7) that are located in different subcellular compartments i.e. nucleus (SIRT1, SIRT6 and SIRT7), cytosol (SIRT2), and mitochondria (SIRT3, SIRT4 and SIRT5) [49, 114], and are implicated in a wide variety of biological functions including control of cellular metabolism and energy h…”
BackgroundThe Role of Sirtuins in the Control of Metabolic Homeostasis
Yu, J., & Auwerx, J. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04952.x · Cited by 145
Self-citationWellman, A. S., Metukuri, M. R., Kazgan, N., Xu, X., Xu, Q., Ren, N. S. X., Czopik, A., Shanahan, M. T., Kang, A., Chen, W., et al. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.05.022 · Cited by 191
Neuroprotective Herbs and Foods from Different Traditional Medicines and Diets
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The Role of Dietary Histone Deacetylases (HDACs) Inhibitors in Health and Disease
Bassett, S. A., & Barnett, M. P. G. (2014) · Nutrients · doi:10.3390/nu6104273 · Cited by 184
“Classes I, II and IV are all zinc-dependent hydrolases and referred to as classical HDACs [20], while Class III consists of the NAD+ dependent sirtuins (SIRT1–7), which are yeast Sir2 homologs [3,21].”
BackgroundSIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model
Wang, Y., Liang, Y. Q., & Vanhoutte, P. M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.047 · Cited by 178
“Sirtuins are a family of NAD-dependent protein deacetylases that exert multiple cellular functions by interacting with, and deacetylating a wide range of signaling molecules, transcription factors, histones and enzymes [34–36].”
BackgroundBeirowski, B., Gustin, J. A., Armour, S. M., Yamamoto, H., Viader, A., North, B. J., Michán, S., Baloh, R. H., Golden, J. P., Schmidt, R. E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104969108 · Cited by 175
“Sirt2 is a member of the conserved sirtuin family of NAD-dependent deacetylases that modulate cellular processes in accord with the metabolic state (12, 13).”
BackgroundSelf-citationMarfè, G., Tafani, M., Indelicato, M., Sinibaldi‐Salimei, P., Reali, V., Pucci, B., Fini, M., & Russo, M. A. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22044 · Cited by 174
“Sirtuins are a family of proteins conserved in all domain of life and involved in many cellular processes from caloric restriction to ageing [Yamamoto et al., 2007].”
InfluentialHigh Levels of SIRT1 Expression as a Protective Mechanism Against Disease-Related Conditions
Elibol, B., & Kilic, U. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00614 · Cited by 171
“Besides its role being a target for histone and non-histone proteins, SIRT1 functions as a transcription factor for many different physiological processes (2).”
BackgroundDevelopment of vorinostat: Current applications and future perspectives for cancer therapy
Richon, V. M., Garcia-Vargas, J. E., & Hardwick, J. S. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.01.002 · Cited by 168
“and -8), Class II (HDAC4, -5, -6, -7, -9, and -10), and Class IV (HDAC 11) are related to the RPD 3/HDA1 deacetylase family while Class III (SIRT1-7) are related to the sirtuin deacetylase family [13,14].”
BackgroundRamis, M. R., Esteban, S., Miralles, A., Tan, D., & Reiter, R. J. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.03.008 · Cited by 165
“Likewise, potential applications of the sirtuins in neuronal cell urvival and response to stress and cell-cycle control hint at the ventual importance of this gene family in the pathogenesis of neuodegenerative diseases and cancer (Yamamoto et al., 2007).”
BackgroundNovel Role of the SIRT1 in Endocrine and Metabolic Diseases
Lu, C., Zhao, H., Liu, Y., Yang, Z., Yao, H., Liu, T., Gou, T., Wang, L., Zhang, J., Tian, Y., et al. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.78654 · Cited by 160
Yahata, N., Yuasa, S., & Araki, T. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4304-08.2009 · Cited by 154
“However, it was not clear how NMNAT overexpression affects Sirt1 activity, because, whereas Sirt1 activity is strictly dependent on intracellular NAD levels (Yamamoto et al., 2007), overexpression of NMNAT activity does not cause major changes in NAD levels (Mack et al.”
BackgroundYu, J., & Auwerx, J. H. (2009) · Pharmacological Research · doi:10.1016/j.phrs.2009.12.006 · Cited by 156
“Among them, SIRT1 is by far the best characterized [8-10].”
BackgroundSelf-citationEffects of Resveratrol and other Polyphenols on Sirt1: Relevance to Brain Function During Aging
Sarubbo, F., Esteban, S., Miralles, A., & Moranta, D. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170703113212 · Cited by 146
“SIRT1 are histone and non-histone deacetylase enzymes responsible for regulating physiological and metabolic responses to stress signals, playing a critical role in cell survival [112-114].”
BackgroundBuelow, B. D., Song, Y., & Scharenberg, A. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802673200 · Cited by 142
Lin, J.-N., Lin, V. C.-H., Rau, K., Shieh, P., Kuo, D., Shieh, J., Chen, W. J., Tsai, S., & Way, T. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9035782 · Cited by 142
Wang, C., Gao, F., Wu, J., Dai, J., Wei, C., & Li, Y. (2010) · Plant and Cell Physiology · doi:10.1093/pcp/pcq087 · Cited by 150
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“Sirt1 is an NAD-dependent deacetylase that regulates lipid and glucose homeostasis and is the proinflammatory cytokine involved in inflammation-associated diseases [29]; in fact, the activation of Sirt1 has been shown to inhibit TNF-α-induced inflammation in fibroblasts [30].”
Oxidative stress-related aging: A role for prostate cancer?
Minelli, A., Bellezza, I., Conte, C., & Čulig, Z. (2008) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.11.001 · Cited by 139
Effect of chronic alcohol consumption on Hepatic SIRT1 and PGC-1α in rats
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Han, Q., Xie, Q. R., Li, F., Cheng, Y., Wu, T., Zhang, Y., Lu, X., Wong, A. S. T., Sha, J., & Xia, W. (2021) · Theranostics · doi:10.7150/thno.53886 · Cited by 135
“Sirtuins belong to a highly conserved family of NAD+-dependent histone deacetylase, involved in a wide variety of cellular functions such as aging, metabolism, stress response, and energy homeostasis [5, 6].”
BackgroundAir Pollution Stress and the Aging Phenotype: The Telomere Connection
Martens, D. S., & Nawrot, T. S. (2016) · Current Environmental Health Reports · doi:10.1007/s40572-016-0098-8 · Cited by 132
Chromatin versus pathogens: the function of epigenetics in plant immunity
Ding, B., & Wang, G. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00675 · Cited by 123
Pieters, N., Janssen, B. G., Dewitte, H., Cox, B., Cuypers, A., Lefebvre, W., Smeets, K., Vanpoucke, C., Plusquin, M., & Nawrot, T. S. (2015) · Environmental Health Perspectives · doi:10.1289/ehp.1509728 · Cited by 125
“SIRT1 belongs to a group of highly conserved NAD+-dependent protein deacetylases and functions as a metabolic sensor since the deacetylase activity is controlled by the cellular NAD+/NADH ratio (Yamamoto et al. 2007).”
BackgroundThe Roles of Sirtuin Family Proteins in Cancer Progression
Zhao, E., Hou, J., Ke, X., Abbas, M. N., Kausar, S., Zhang, L., & Cui, H. (2019) · Cancers · doi:10.3390/cancers11121949 · Cited by 125
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“Silent information regulator 1 (SIRT1) is a nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase (class III HDAC), which has been reported to be a crucial regulator in the pathophysiology of aging, metabolic disease and neurodegenerative disorders [1-6].”
BackgroundAskanas, V., & Engel, W. K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0449-0 · Cited by 124
“SIRT1 belongs to the mammalian sirtuin family of NADdependent histone deacetylases (HDACs) [45, 65, 100, 115].”
BackgroundJayasena, T., Poljak, A., Smythe, G. A., Braidy, N., Münch, G. W., & Sachdev, P. S. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.06.003 · Cited by 122
Salminen, A., Ojala, J. O., Huuskonen, J., Kauppinen, A., Suuronen, T., & Kaarniranta, K. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7461-3 · Cited by 120
The conserved role of sirtuins in chromatin regulation
Vaquero, A. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082675av · Cited by 119
“In fact, SirT1 is the phylogenetic and functional ortholog of both yeast ScSir2p and Hst1p and shows the broadest range of functions as well as the widest array of substrates among sirtuins (Yamamoto et al., 2007).”
BackgroundThe Role of Sirtuin1 in Regulating Endothelial Function, Arterial Remodeling and Vascular Aging
Man, A. W. C., Li, H., & Xia, N. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01173 · Cited by 123
“Most of the sirtuin family members are considered to be potential regulators of metabolism and aging (Yamamoto et al., 2007).”
BackgroundBioactivity of Grape Chemicals for Human Health
Iriti, M., & Faoro, F. (2009) · Natural Product Communications · doi:10.1177/1934578x0900400502 · Cited by 119
Law, I. K. M., Liu, L., Xu, A., Lam, K. S. L., Vanhoutte, P. M., Che, C., Leung, P. T. Y., & Wang, Y. (2009) · PROTEOMICS · doi:10.1002/pmic.200800738 · Cited by 114
“It has been reported that SIRT1 can regulate several nuclear factors that govern cellular growth and survival, including histone, p53, nuclear factor-kB (NF-kB), forkhead box type O transcription factors (FOXO) and Ku70 etc [1, 3, 20].”
The roles of sirtuins family in cell metabolism during tumor development
Zhu, S., Dong, Z., Ke, X., Hou, J., Zhao, E., Zhang, K., Wang, F., Yang, L., Xiang, Z., & Cui, H. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.003 · Cited by 113
NAD+ as a Signaling Molecule Modulating MetabolismPreprint
Canto, C., & Auwerx, J. H. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2012.76.010439 · Cited by 111
“For an extended view on the function of the different sirtuins, we refer the reader to some of the reviews that cover that topic (Yamamoto et al. 2007; Houtkooper et al. 2010; Verdin et al. 2010).”
BackgroundSelf-citationChen, I., Chiang, W., Huang, H.-H., Chen, P., Shen, Y., & Chiang, H. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-254 · Cited by 111
“It was previously shown that SIRT1 helps regulate a variety of physiological processes by interacting with nuclear proteins [28,52-56].”
BackgroundThe complex relationship between obesity and neurodegenerative diseases: an updated review
Neto, A., Fernandes, A. M. A., & Barateiro, A. P. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1294420 · Cited by 120
“Several other beneficial functions include cell survival, DNA repair, chromatin remodeling, and neuronal survival and differentiation (Yamamoto et al., 2007; Duan, 2013; Giblin et al., 2014).”
The role of SIRT1 in ocular aging
Mimura, T., Kaji, Y., Noma, H., Funatsu, H., & Okamoto, S. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.07.017 · Cited by 114
Borengasser, S. J., Lau, F., Kang, P., Blackburn, M. L., Ronis, M. J. J., Badger, T. M., & Shankar, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024068 · Cited by 111
“The sirtuin family consists of seven isoforms (SIRT1-7) that regulate distinct metabolic pathways in various cellular locations [45].”
BackgroundKemper, J. K. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.11.011 · Cited by 108
SIRT2 Regulates LPS-Induced Renal Tubular CXCL2 and CCL2 Expression
Jung, Y. J., Lee, A. S., Nguyen, T. T., Kim, D., Kang, K. P., Lee, S., Park, S. K., & Kim, W. B. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014030226 · Cited by 105
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103
SIRT1 mRNA expression may be associated with energy expenditure and insulin sensitivity
Rutanen, J., Yaluri, N., Modi, S., Pihlajamäki, J., Vänttinen, M., Itkonen, P., Kainulainen, S., Yamamoto, H., Lagouge, M., Sinclair, D. A., et al. (2010) · Diabetes · doi:10.2337/db09-1191 · Cited by 104
“The mammalian sirtuins (SIRT1–SIRT7) are implicated in gene silencing, mitochondrial function, energy homeostasis, insulin sensitivity, and longevity (5).”
BackgroundSelf-citationKwon, S., Seok, S., Yau, P. M., Li, X., KEMPER, B. W., & Kemper, J. K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778720 · Cited by 102
Metabolic benefits from Sirt1 and Sirt1 activators
Chaudhary, N., & Pfluger, P. T. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32832cdaae · Cited by 100
Resveratrol in mammals: effects on aging biomarkers, age‐related diseases, and life span
Marchal, J., Pifferi, F., & Aujard, F. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12214 · Cited by 101
SIRT2: Tumour suppressor or tumour promoter in operable breast cancer?
McGlynn, L. M., Zino, S., Macdonald, A. I., Curle, J., Reilly, J. E., Mohammed, Z. M. A., McMillan, D. C., Mallon, E., Payne, A. P., Edwards, J., et al. (2013) · European Journal of Cancer · doi:10.1016/j.ejca.2013.10.005 · Cited by 99
LOU, Y., WANG, Z., XU, Y., Zhou, P. H., Cao, J., Li, Y., Chen, Y., Sun, J., & Fu, L. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2291 · Cited by 98
“Sirt1 has been shown to be involved in various cellular functions, ranging from gene silencing, the control of the cell cycle and apoptosis to energy homeostasis (54).”
Jablonska, B., Gierdalski, M., Chew, L., Hawley, T. S., Catron, M. A., Lichauco, A. M., Cabrera‐Luque, J., Yuen, T. J., Rowitch, D. H., & Gallo, V. (2016) · Nature Communications · doi:10.1038/ncomms13866 · Cited by 98
“It has been demonstrated that many cell cycle proteins that control cell proliferation are sirtuin substrates 31 , and sirtuins—including Sirt1—regulate proliferation of different cell types 31 .”
Seizure-Induced Oxidative Stress in Status Epilepticus: Is Antioxidant Beneficial?
Lin, T., Chen, S., Lin, K.-J., & Chuang, Y. (2020) · Antioxidants · doi:10.3390/antiox9111029 · Cited by 96
“In mammals, the sirtuin family include seven sirtuins: sirtuin1–7, and belong to a class of nicotinamide adenine dinucleotide (NAD)-consuming enzymes that are involved in various biological pathways [93].”
BackgroundMuscle mitochondria and insulin resistance: a human perspective
Hoeks, J., & Schrauwen, P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.05.007 · Cited by 94
Sirtuin 1 in malignant transformation: Friend or foe?
Fang, Y., & Nicholl, M. B. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.02.019 · Cited by 94
Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 97
D’Onofrio, N., Prattichizzo, F., Marfella, R., Sardu, C., Martino, E., Scisciola, L., Marfella, L., Grotta, R. L., Frigé, C., Paolisso, G., et al. (2023) · Theranostics · doi:10.7150/thno.80289 · Cited by 93
“Sirtuins (SIRT) are a family of nicotinamide adenine dinucleotide-(NAD+) dependent histone deacetylases involved in the regulation of a range of homeostatic processes [20].”
Gloghini, A., Buglio, D., Khaskhely, N. M., Georgakis, G. V., Orlowski, R. Z., Neelapu, S. S., Carbone, A., & Younes, A. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07887.x · Cited by 93
“Class III are the NAD+-dependant sirtuins (SIRT17)(Yamamoto et al, 2007).”
Zhou, Y., Zhang, H., He, B., Du, J., Lin, H., Cerione, R. A., & Hao, Q. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.384511 · Cited by 91
Age-dependent tissue expression patterns of Sirt1 in senescence-accelerated mice
Gong, H., Pang, J., Han, Y., Dai, Y., Dai, D., Cai, J., & Zhang, T. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2648 · Cited by 90
“Sirt1 has a range of molecular functions and has emerged as an important protein in aging and metabolic regulation (6).”
Sirtuin 1 in Endothelial Dysfunction and Cardiovascular Aging
Ministrini, S., Puspitasari, Y. M., Beer, G., Liberale, L., Montecucco, F., & Camici, G. G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.733696 · Cited by 94
Moderate Wine Consumption and Health: A Narrative Review
Hrelia, S., Renzo, L. D., Bavaresco, L., Bernardi, E., Malaguti, M., & Giacosa, A. (2022) · Nutrients · doi:10.3390/nu15010175 · Cited by 106
HDAC3 Is Negatively Regulated by the Nuclear Protein DBC1
Chini, C. C. S., Escande, C., Nin, V., & Chini, E. N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.153270 · Cited by 89
Katare, P. B., Nizami, H. L., Bugga, P., Dinda, A. K., & Banerjee, S. K. (2020) · Scientific Reports · doi:10.1038/s41598-020-75301-4 · Cited by 87
Regulation of SIRT1 by MicroRNAs
Choi, S., & Kemper, J. K. (2013) · Molecules and Cells · doi:10.1007/s10059-013-0297-1 · Cited by 88
“Levels of SIRT7 are high in metabolically active tissues, such as liver and spleen, but very low in non-proliferating tissues, including heart and brain (Barber et al., 2012; Ford et al., 2006; Yamamoto et al., 2007).”
BackgroundGuo, L., Li, S., Zhao, Y., Qian, P., Ji, F., Qian, L., Wu, X., & Qian, G. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24969 · Cited by 84
“SIRT1 has several functions, including anti-inflammation, lipid metabolism regulation, and the control of cell survival and apoptosis (Yamamoto et al., 2007; Kong et al., 2009).”
Background
Metadata
- Authors
- Yamamoto, H., Schoonjans, K., & Auwerx, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Auwerx, Johan
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2007-08-01
- Volume
- 21
- Issue
- 8
- Pages
- 1745-1755
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W2043932983
- Cited by
- 480
- References
- 121
- Citations by year
- 2026: 11 · 2025: 16 · 2024: 20 · 2023: 22 · 2022: 31 · 2021: 37 · 2020: 41 · 2019: 16 · 2018: 31 · 2017: 10 · 2016: 16 · 2015: 22 · 2014: 21 · 2013: 31 · 2012: 30
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- sirtuins, Sir2, NAD+-dependent deacetylation, ADP-ribosyltransferase, lysine deacetylation, gene silencing, cell cycle regulation, apoptosis, energy homeostasis, metabolic disorders, neurodegenerative diseases, proliferative diseases, aging, therapeutic target
- MeSH terms
- Animals, Humans, Neoplasms, Neurodegenerative Diseases, Sirtuins, Cell Proliferation
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