Cited by 484Sirtuins and Resveratrol in MedicineBiochemical and Molecular ResearchHistone Deacetylase Inhibitors Research

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Sirtuin Functions in Health and Disease

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Yamamoto, Hiroyasu, Schoonjans, Kristina, Auwerx, Johan·2007·Molecular Endocrinology

DOI 10.1210/me.2007-0079

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Abstract

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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Background
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Background
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“…transcription factor in all cell types throughout the body (Suzuki et al., 2014) where different mechanisms including phosphorylation, dephosphorylation, acetylation, and changes in protein conformation have been proposed for regulation of its activity (Reisman et al., 2012; Yamamoto et al., 2007).”
BackgroundResult
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“Sirtuin (Sirt1) is a conserved NAD-dependent histone deacetylase that has been linked to longevity, apoptosis, inflammation and energy homeostasis (Yamamoto et al., 2007).”
Background
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“SIRT1 localizes in the nucleus and cytoplasm and is implicated in the regulation of gene transcription [21].”
Background
Proteomics analysis of human umbilical vein endothelial cells treated with resveratrol
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Background
Metabolomics: On the way to an integration of biochemistry, analytical chemistry, and informatics
Goncharov, N. V., Уколов, А. И., Orlova, T. I., Migalovskaia, E. D., & Войтенко, Н. Г. (2015) · Biology Bulletin Reviews · doi:10.1134/s2079086415040027 · Cited by 10
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Background
Resveratrol-poor Red Wines Modulate SIRT1 in Human Renal Cells
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Background
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“The altered mucosal homeostasis is potentially regulated by sirtuin signalling, which is indicated by the activation of SIRT5 gene in the EF group, that is known to be exclusively located in mitochondria regulating energy metabolism and homeostasis (75, 76) as well as having potential immune regulatory (T cell activat…”
Background
Sirtuins: The Future Insight
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Background
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Mediating a host cell signaling pathway linked to overwinter mortality offers a promising therapeutic approach for improving bee health
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Background
Multiple omics analysis reveals the regulation of SIRT5 on mitochondrial function and lipid metabolism during the differentiation of bovine preadipocytes
Hong, J., Raza, S. H. A., Ma, H., Cao, W., Chong, Y., Wu, J., Xi, D., & Deng, W. (2023) · Genomics · doi:10.1016/j.ygeno.2023.110773 · Cited by 8
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Background
Free fatty acid-induced miR-22 inhibits gluconeogenesis via SIRT-1-mediated PGC-1α expression in nonalcoholic fatty liver disease
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“SIRT1 has been extensively studied since it plays an important role in numerous biological processes, such as cellular senescence, apoptosis, sugar and lipid metabolism, oxidative stress, and inflammation (Haigis and Guarente 2006; Yamamoto et al. 2007; Yang et al. 2022).”
CircWEE1/miR-138 axis promotes the malignant progression of glioma by regulating SIRT1
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“Sirtuin is highly conserved in evolution from bacteria to eukaryotes and plays an important role in a variety of cellular functions in mammals, such as gene silencing, control of cell cycle and apoptosis, and energy balance (13).”
Background
Sirtuin 6 Is a Critical Epigenetic Regulator of Cancer
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“Nicotinamide adenosine dinucleotide-dependent deacetylase sirtuin-1 (SIRT1) regulates a myriad of cellular processes including cellular senescence, metabolism, aging, and inflammation, through its ability to deacetylate a diverse range of target proteins [259–261].”
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Structural modification of 2‐phenylquinoline‐4‐carboxylic acid containing SIRT3 inhibitors for the cancer differentiation therapy
Du, Y., Wang, X., Zhang, L., Qin, H., Xu, G., Li, F., Fang, C., Li, H., & Zhang, L. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14595 · Cited by 6
“Emerged as critical regulators of metabolism, SIRTs are associated with a wide range of intracellular processes including energy and nutrient homoeostasis, longevity, aging, response to stress and especially cancer (Hirschey, 2011; Yamamoto et al., 2007).”
SIRT2 regulates high mobility group protein B1 nucleoplasmic shuttle and degradation via deacetylation in microglia
Xing, W., Piao, X., Han, Q., Shi, H., Wu, W., Si, F., Lu, J., Zhou, T., Guo, J., Li, S., et al. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31364 · Cited by 6
“In mammals, seven members (SIRT1 – 7) have been discovered that act on various substrates and regulate a wide range of cellular processes (Yamamoto et al., 2007; Michan & Sinclair, 2007).”
Diet and SIRT1 Genotype Interact to Modulate Aging-Related Processes in Patients with Coronary Heart Disease: From the CORDIOPREV Study
Hidalgo-Moyano, C., Rangel-Zúñiga, O. A., Gómez-Delgado, F., Alcala-Diaz, J. F., Rodríguez-Cantalejo, F., Yubero‐Serrano, E. M., Torres-Peña, J. D., Larriva, A. P. A.-D., Camargo, A., Perez-Martinez, P., et al. (2022) · Nutrients · doi:10.3390/nu14183789 · Cited by 6
“The SIRT1 gene encodes for the protein sirtuin 1 (Sirt1), which has a range of molecular functions and has emerged as an important protein in aging and metabolic regulation [22].”
Background
Effects of follicle-stimulating hormone, insulin-like growth factor 1, fibroblast growth factor 2, and fibroblast growth factor 9 on sirtuins expression and histone deacetylase activity in bovine granulosa cells
Archilia, E. C., Bello, C. A. P., Batalha, I. M., Wulstein, K., Enriquez, C., & Schütz, L. F. (2023) · Theriogenology · doi:10.1016/j.theriogenology.2023.07.011 · Cited by 6
Sirtuiny – enzymy o wielokierunkowej aktywności katalitycznej
Kratz, E. M., Sołkiewicz, K., Kaczmarek, A., & Piwowar, A. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.7866 · Cited by 6
In Silico Docking of HNF-1a Receptor Ligands
Sridhar, G. R., Rao, P. V. N., Kaladhar, D. S. V. G. K., Tatavarthi, U. D., & Kumar, S. V. (2012) · Advances in Bioinformatics · doi:10.1155/2012/705435 · Cited by 6
Health-Promoting Effects of Grape Bioactive Phytochemicals
Iriti, M., & Faoro, F. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-374228-5.00023-8 · Cited by 6
Alternative Splicing: Emerging Roles in Anti-Aging Strategies
Gao, L., & Jia, R. (2025) · Biomolecules · doi:10.3390/biom15010131 · Cited by 5
“SIRT1 (sirtuin 1) is a member of the sirtuin protein family, which is an NAD + - dependent deacetylase that couples target substrate deacetylation with cellular metabolic status [52,53].”
Insight from sirtuins interactome: topological prominence and multifaceted roles of SIRT1 in modulating immunity, aging and cancer
Zulkifli, N. D., & Zulkifle, N. (2023) · Genomics & Informatics · doi:10.5808/gi.23003 · Cited by 5
Discovery of Novel N-Acylhydrazone Derivatives as Potent Inhibitors of Sirtuin-1
Lipson, V. V., Yaremenko, F. G., Vakula, V. M., Kovalenko, S. V., Kyrychenko, A. V., Desenko, S. M., Borysko, P., & Zozulya, S. O. (2024) · SynOpen · doi:10.1055/s-0043-1763747 · Cited by 5
Malnutrition Risk in Older Adults: Evaluating the Diagnostic Relevance of Serum Biomarkers: SIRT-1, CCK-8, Melatonin, and Total Antioxidant Capacity (TAC)
Kujawowicz, K., Mirończuk-Chodakowska, I., Cyuńczyk, M., & Witkowska, A. M. (2025) · Nutrients · doi:10.3390/nu17040726 · Cited by 5
“Excessive increases in SIRT-1 may contribute to short-term starvation [53,54], as well as increased lipolysis [55] and insulin sensitivity [56,57], resulting in a decrease in energy metabolism and appetite.”
vp1524, a Vibrio parahaemolyticus NAD +-dependent deacetylase, regulates host response during infection by induction of host histone deacetylation
Mishra, P., Beura, S., Sikder, S., Dhal, A. K., Vasudevan, M., Roy, M., Rakshit, J., Budhwar, R., Kundu, T. K., & Modak, R. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac027 · Cited by 5
New sirtuin modulators: their uncovering, pharmacophore, and implications in drug discovery
Chen, P.-T., & Yeong, K. Y. (2024) · Medicinal Chemistry Research · doi:10.1007/s00044-024-03249-5 · Cited by 8
“It may deacetylate the tumor suppressors such as p53 and forkhead box O (FOXO) proteins that respond to oxidative stress and DNA damage, leading to its role as a tumor promoter [14, 15].”
Papel pleiotrópico y homeostático de las Sirtuinas en la función biológica humana.
Hernández-Bedolla, M. A., Barajas‐Espinosa, A. R., Ochoa‐Cortés, F., Alonso, D. E. A., Hernández, A. H., Ostoa, Z. B., & Salguero, I. G. D. (2020) · Ciencias Huasteca Boletín Científico de la Escuela Superior de Huejutla · doi:10.29057/esh.v8i16.5721 · Cited by 5
“3 PAPEL FISIOLÓGICO DE LAS SIRTUINAS Las sirtuinas humanas están involucradas en varios procesos biológicos importantes, tales como el envejecimiento, reparación del ADN, silenciamiento génico, estabilidad cromosómica, respuesta al estrés, viabilidad, diferenciación, metabolismo, apoptosis y supervivencia celular.(58,…”
Background
Transcriptome of Left Ventricle and Sinoatrial Node in Young and Old C57 Mice
Qu, J.-H., Tarasov, K. V., Tarasova, Y. S., Chakir, K., & Lakatta, E. G. (2023) · Fortune Journal of Health Sciences · doi:10.26502/fjhs.134 · Cited by 5
“Sirtuins are class III deacetylases, implicated in influencing metabolism and stress resistance [47,48].”
Background
Dietary Effect on Epigenetics During the Aging Process
Tollefsbol, T. O., & Li, Y. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0639-7_22 · Cited by 5
“has been identified as a member of chromatin modifying factors of class III histone deacetylases with the capability of protecting cells from oxidative and genotoxic stress in stress management and metabolism (Vaquero et al. 2004; Yamamoto et al. 2007 ).”
Background
Probing the Druggability Limits for Enzymes of the NAD Biosynthetic Network in Glioma
Padiadpu, J., Mishra, M., Sharma, E., Mala, U., Somasundaram, K., & Chandra, N. R. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00733 · Cited by 5
Mono-ADP-Ribosylation of Heterotrimeric G Proteins
Girolamo, M. D., & Corda, D. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00204-7 · Cited by 5
Calorie Restriction Mimetics and Aging
Morris, B. J. (2010) · Springer eBooks · doi:10.1007/978-90-481-8556-6_9 · Cited by 5
Nicotinamide promotes differentiation of pancreatic endocrine progenitors from human pluripotent stem cells through poly (ADP-ribose) polymerase inhibitionPreprint
Woodford, C. M., Yin, T., Chang, H. H., Regeenes, R., Vellanki, R. N., Mohan, H., Wouters, B. G., Rocheleau, J. V., Wheeler, M. B., & Zandstra, P. W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.21.052951 · Cited by 5
“The sirtuins are a seven-member family of enzymes with different subcellular localizations such as the nucleus or mitochondria involved in gene and metabolic regulatory pathways [9].”
Background
Pharmacological Approaches to Improve Ageing
Pedro, J., Camello‐Almaraz, C., & Maria, J. (2012) · InTech eBooks · doi:10.5772/33389 · Cited by 4
“…Approaches to Improve Ageing 269 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 (Yamamoto et al., 2007).”
Biomarkers of Mitochondrial Dysfunction and Toxicity
Palmeira, C. M., Teodoro, J. S., Silva, R., & Rolo, A. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814655-2.00055-4 · Cited by 4
Therapeutic Potential of Polyphenols in Parkinson’s Disease
Babu, R., Harish, G., Raghunath, N. R., & Srinivas, M. M. (2011) · InTech eBooks · doi:10.5772/20055 · Cited by 4
“Sirtuins possess NAD+ dependent deacetylase activity and mono-ribosyltransferase activity and are found in most organisms (North & Verdin 2004, Yamamoto et al., 2007).”
Background
Inhibitory effect of AK-7 mediates by apoptosis, increases DNA fragmentation and caspase-3 activity in human glioblastoma multiforme cells
Güçlü, E., Ayan, İ. Ç., & Vural, H. C. (2022) · Bangladesh Journal of Pharmacology · doi:10.3329/bjp.v17i2.59809 · Cited by 4
“…cycle, cell survival, apoptosis, lipid and glucose homeostasis, metabolism, inflammation, DNA repair, genome stability, and mitochondrial functions (Yamamoto et al., 2007; Shoba et al., 2009; Villalba and Alcaín, 2012; Sirtuins (SIRTs) which are nicotinamide adenine dinucleotide (NAD+) dependent…”
Background
Sirtuins and their role as physiological modulators of metabolism
Sygitowicz, G., & Sitkiewicz, D. (2020) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.5247 · Cited by 4
Inhibition of SIRT1 Transcription in Resveratrol-differentiated Medulloblastoma Cells
Ma, J., Li, H., Cheng, X., Wu, M., Li-jun, Y., Kong, Q., Liu, M., & Liu, J. (2013) · Functional Foods in Health and Disease · doi:10.31989/ffhd.v3i5.56 · Cited by 5
“DISCUSSION: Sirtuins are found in all organisms and act as the critical regulators at the crossroads between cancer and aging [31,32].”
Background
Respected Sir(2): magic target for diabetes.
Nerurkar, P. V., & Nerurkar, V. R. (2008) · PubMed · Cited by 4
Recombinant human growth hormone and insulin-like growth factor-1 do not affect mitochondrial derived highly reactive oxygen species production in peripheral blood mononuclear cells under conditions of substrate saturation in-vitro
Keane, J., Tajouri, L., & Gray, B. (2016) · Nutrition & Metabolism · doi:10.1186/s12986-016-0105-y · Cited by 4
“Thus, the autocrine/paracrine activation of GH/IGF-1 pathways may be more relevant to the hormonal effect on the rate of mitochondrial ROS production in these cell types, than local concentrations of the systemic isoforms secreted from the anterior pituitary and the liver, respectively [4].”
BackgroundInfluential
Role of Nicotinamide in the Pathogenesis of Actinic Keratosis: Implications for NAD+/SIRT1 Pathway
Belardi, R., Pacifici, F., Cosio, T., Lambiase, S., Shumak, R. G., Artosi, F., Rivieccio, A., Cavalloro, D., Dellambra, E., Bianchi, L., et al. (2024) · Biomolecules · doi:10.3390/biom14121512 · Cited by 3
“NAD + also regulates various intracellular mechanisms, including cellular senescence, by serving as a substrate for sirtuins (SIRT), class III histone deacetylases that regulate the cell cycle, apoptosis, and energy homeostasis [28].”
Therapeutic Perspectives of SIRT6 Regulation: Computational Analysis of Activation and Inhibition by Bioactive Molecules
Matias, É. G. C., Bezerra, K. S., Clemente, W. S., Oliveira, J. I. N., Galvao, D. S., & Fulco, U. L. (2025) · Journal of Molecular Recognition · doi:10.1002/jmr.70016 · Cited by 3
Gingerol-Enriched Ginger Extract Effects on Anxiety-like Behavior in a Neuropathic Pain Model via Colonic Microbiome-Neuroimmune Modulation
Mendóza, R., Santos, J. M., Liu, X., Elmassry, M. M., Ji, G., Kiritoshi, T., Neugebauer, V., & Shen, C. (2026) · Molecules · doi:10.3390/molecules31010166 · Cited by 3
“Moreover, higher concentrations of NAD + lead to increased activity of the NAD + -dependent deacetylase SIRT1, which is not only critical for epigenetic modification but also functions as a transcription factor in many physiological processes [76].”
The transposon-driven evolutionary origin and basis of histone deacetylase functions and limitations in disease prevention
Peek, G. W., & Tollefsbol, T. O. (2011) · Clinical Epigenetics · doi:10.1007/s13148-011-0020-z · Cited by 3
“SIRT1 has essential roles in chromatin regulation, metabolism, differentiation and cellular response to stress conditions (Vaquero 2009; Yamamoto et al. 2007).”
Background
The Role of Histone Deacetylase and Histone Deacetylase Inhibitors in Rheumatoid Arthritis
Kriswiastiny, R., Partan, R. U., Hermansyah, H., Darma, S., & Reagan, M. (2021) · Bioscientia Medicina Journal of Biomedicine and Translational Research · doi:10.32539/bsm.v5i11.423 · Cited by 4
Identification and molecular modeling of novel endogenous activator proteins of Sirt-1: an in silico study
Shanitha, A., Sudhakar, M., Nair, A. S., & Saja, K. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2132294 · Cited by 3
“SIRT6 is more efficient in removing long-chain fatty acyl groups such as myristoyl and palmitoyl groups (for more details see Davenport et al., 2014; Feldman et al., 2012; Sudhakar et al., 2018; Yamamoto et al., 2007).”
Background
Melatonin as a Chronobiotic and Cytoprotector in Healthy Aging
Cardinali, D. P., Pandi-Perumal, S. R., & Brown, G. M. (2023) · Healthy ageing and longevity · doi:10.1007/978-3-031-22468-3_14 · Cited by 3
Sirtuin3 gene tissue expression profiling, SNP detection and its association with body conformation traits in goats
Silpa, M. V., Thomas, N., Aravindakshan, T. V., Radhika, G., Venkatachalapathy, R. T., & Kurian, E. (2019) · Small Ruminant Research · doi:10.1016/j.smallrumres.2019.11.003 · Cited by 3
SIRT2 Protein Expression in Normal and Aged Rat Brain
Oh, C. S., Lee, E., & Lee, Y. S. (2012) · Journal of the Korean Geriatrics Society · doi:10.4235/jkgs.2012.16.1.27 · Cited by 3
SIRT1: Importance of O-GlcNAc and Phosphorylation Interplay in Aging and Diabetes
Hoessli, D. C., Ghazanfar, F., Kaleem, A., Iqbal, Z., Shakoori, A. R., & Nasir‐ud‐Din (2013) · Pakistan Journal of Zoology · Cited by 3
Biomarkers of mitochondrial dysfunction and toxicity
Palmeira, C. M., Duarte, F. V., Teodoro, J. S., Varela, A. T. I. F., & Rolo, A. P. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404630-6.00051-8 · Cited by 3
Epigenetic remodeling during monolayer cell expansion reduces therapeutic potentialPreprint
Scott, A. K., Casas, E., Schneider, S. E., Swearingen, A. R., Elzen, C. L. V. D., Seelbinder, B., Barthold, J. E., Kugel, J. F., Stern, J. L., Foster, K. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.14.472696 · Cited by 3
Sirt6-Mediated Cell Death Associated with Sirt1 Suppression in Gastric Cancer
Seo, J., Ryu, S., Cheon, S. Y., Lee, S.-J., Won, S., Yim, C. D., Lee, H., Hah, Y., & Park, J. J. (2024) · Cancers · doi:10.3390/cancers16020387 · Cited by 3
“Sirtuins are nicotinamide adenine dinucleotide (NAD+)-dependent signaling proteins that regulate various metabolic processes such as energy metabolism, inflammation, and apoptosis in a wide range of organisms ranging from yeast to mammals [1].”
Background
Role of SIRT7 in Prostate Cancer Progression: New Insight Into Potential Therapeutic Target
Zhang, J., Liu, C., Luo, W., & Sun, B. (2025) · Cancer Medicine · doi:10.1002/cam4.70786 · Cited by 2
“Sirtuins play crucial regulatory roles by interacting with various substrates, including maintaining genomic stability [58], regulating cellular senescence [59–61], modulating metabolism [2], facilitating ribosome biogenesis [62, 63], and influencing tumor biology.”
Sirtuin 1 (SIRT1) and activated caspase 3 expression on rat spinal cord in acute phase after Sciatic nerve injury
Ahsani, D. N., Susilowati, R., & Sumiwi, Y. A. A. (2018) · Bangladesh Journal of Medical Science · doi:10.3329/bjms.v18i1.39548 · Cited by 2
Integrated Ligand and Structure-Based Investigation of Structural Requirements for Silent Information Regulator 1 (SIRT1) Activation
Gupta, A. K., & Choi, S. (2018) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666181220111059 · Cited by 2
“Cardiac specific over expression of SIRT1 has been known to prevent agedependent increase in cardiac hypertrophy, apoptosis, cardiac dysfunction, and expression of senescence markers [6, 12].”
Background

Authors: Yamamoto, H., Schoonjans, K., & Auwerx, J.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Auwerx, Johan
ORCID: Yamamoto, Hiroyasu
Schoonjans, Kristina
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
DOI: 10.1210/me.2007-0079
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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Sirtuin Functions in Health and Disease

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