Cited by 246Sirtuins and Resveratrol in MedicinePARP inhibition in cancer therapyBiochemical and Molecular Research

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Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes

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Cantó, Carles, Sauve, Anthony A., Bai, Peter·2013·Molecular Aspects of Medicine

DOI 10.1016/j.mam.2013.01.004PMC PMC3676863

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Abstract

Poly(ADP-ribose) polymerases (PARPs) are NAD(+) dependent enzymes that were identified as DNA repair proteins, however, today it seems clear that PARPs are responsible for a plethora of biological functions. Sirtuins (SIRTs) are NAD(+)-dependent deacetylase enzymes involved in the same biological processes as PARPs raising the question whether PARP and SIRT enzymes may interact with each other in physiological and pathophysiological conditions. Hereby we review the current understanding of the SIRT-PARP interplay in regard to the biochemical nature of the interaction (competition for the common NAD(+) substrate, mutual posttranslational modifications and direct transcriptional effects) and the physiological or pathophysiological consequences of the interactions (metabolic events, oxidative stress response, genomic stability and aging). Finally, we give an overview of the possibilities of pharmacological intervention to modulate PARP and SIRT enzymes either directly, or through modulating NAD(+) homeostasis.

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2 retracted

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Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
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Resistance to endotoxic shock as a consequence of defective NF‐κB activation in poly (ADP‐ribose) polymerase‐1 deficient mice
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Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis
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Age-Associated Changes In Oxidative Stress and NAD+ Metabolism In Human Tissue
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Authors: Cantó, C., Sauve, A. A., & Bai, P.
Affiliations: Nestlé (Switzerland) (CH)
Weill Cornell Medicine (US)
ORCID: Cantó, Carles
Sauve, Anthony A.
Venue: Molecular Aspects of Medicine
Publisher: Elsevier BV
Published: 2013-12
Volume: 34
Issue: 6
Pages: 1168-1201
ISSN: 0098-2997 (ISSN-L)
DOI: 10.1016/j.mam.2013.01.004
PMC: PMC3676863
OpenAlex: W1963982942
Cited by: 246
References: 413
Citations by year: 2026: 12 · 2025: 9 · 2024: 15 · 2023: 14 · 2022: 21 · 2021: 27 · 2020: 37 · 2019: 18 · 2018: 16 · 2017: 26 · 2016: 14 · 2015: 17 · 2014: 12 · 2013: 8
FWCI: 1.61
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Aspects of Medicine (publishedVersion)
PubMed (publishedVersion)
Repository of the Academy's Library (Library of the Hungarian Academy of Sciences) (acceptedVersion)
PubMed Central (acceptedVersion)
University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, cc-by-nc-nd)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073466, R21DK094001)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: poly(ADP-ribose) polymerase, sirtuins, NAD+ metabolism, post-translational modification, transcriptional regulation, oxidative stress response, genome stability, aging, metabolic regulation, pharmacological modulation
MeSH terms: Poly(ADP-ribose) Polymerase Inhibitors, Animals, Gene Expression Regulation, Humans, NAD, Poly(ADP-ribose) Polymerases, Protein Binding, Protein Processing, Post-Translational, Oxidative Stress, Sirtuins, Protein Interaction Domains and Motifs

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Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes

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