Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2016 May 25:8:61.
doi: 10.1186/s13148-016-0224-3. eCollection 2016.

Sirtuin functions and modulation: from chemistry to the clinic

Affiliations
Review

Sirtuin functions and modulation: from chemistry to the clinic

Vincenzo Carafa et al. Clin Epigenetics. .

Abstract

Sirtuins are NAD(+)-dependent histone deacetylases regulating important metabolic pathways in prokaryotes and eukaryotes and are involved in many biological processes such as cell survival, senescence, proliferation, apoptosis, DNA repair, cell metabolism, and caloric restriction. The seven members of this family of enzymes are considered potential targets for the treatment of human pathologies including neurodegenerative diseases, cardiovascular diseases, and cancer. Furthermore, recent interest focusing on sirtuin modulators as epigenetic players in the regulation of fundamental biological pathways has prompted increased efforts to discover new small molecules able to modify sirtuin activity. Here, we review the role, mechanism of action, and biological function of the seven sirtuins, as well as their inhibitors and activators.

Keywords: Cancer; Drug discovery; Epigenetics; Neurodegeneration; SIRT modulators; Sirtuins.

PubMed Disclaimer

References

    1. Carafa V, Nebbioso A, Altucci L. Sirtuins and disease: the road ahead. Front Pharmacol. 2012;3:4. doi: 10.3389/fphar.2012.00004. - DOI - PMC - PubMed
    1. Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, Dai L, et al. Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab. 2014;19(4):605–17. doi: 10.1016/j.cmet.2014.03.014. - DOI - PMC - PubMed
    1. Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H, et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science. 2011;334(6057):806–9. doi: 10.1126/science.1207861. - DOI - PMC - PubMed
    1. Araki T, Sasaki Y, Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science. 2004;305(5686):1010–3. doi: 10.1126/science.1098014. - DOI - PubMed
    1. Li XH, Chen C, Tu Y, Sun HT, Zhao ML, Cheng SX, et al. Sirt1 promotes axonogenesis by deacetylation of Akt and inactivation of GSK3. Mol Neurobiol. 2013;48(3):490–9. doi: 10.1007/s12035-013-8437-3. - DOI - PubMed

Publication types