Document Detail


Structure and function of poly(ADP-ribose) polymerase-1: role in oxidative stress-related pathologies.
MedLine Citation:
PMID:  16026317     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Poly(ADP-ribosyl) ation is a reversible post-translational protein modification implicated in the regulation of a number of biological functions. Whereas an 18 member superfamily of poly(ADP-ribose) polymerase (PARP) enzymes synthesize poly(ADP-ribose) (PAR), a single protein, PAR glycohydrolase (PARG) is responsible for the catabolism of the polymer. PARP-1 accounts for more than 90% of the poly(ADP-ribosyl)ating capacity of the cells. PARP-1 activated by DNA breaks cleaves NAD(+) into nicotinamide and ADP-ribose and uses the latter to synthesize long branching PAR polymers covalently attached to acceptor proteins including histones, DNA repair enzymes, transcription factors and PARP-1. Whereas activation of PARP-1 by mild genotoxic stimuli may facilitate DNA repair and cell survival, irreparable DNA damage triggers apoptotic or necrotic cell death. In apoptosis, early PARP activation may assist the apoptotic cascade [e.g. by stabilizing p53, by mediating the translocation of apoptosis inducing factor (AIF) from the mitochondria to the nucleus or by inhibiting early activation of DNases]. In most severe oxidative stress situations, excessive DNA damage causes over activation of PARP-1, which incapacitates the apoptotic machinery and switches the mode of cell death from apoptosis to necrosis. Besides serving as a cytotoxic mediator, PARP-1 is also involved in transcriptional regulation, most notably in the NF kappaB and AP-1 driven expression of inflammatory mediators. Pharmacological inhibition or genetic ablation of PARP-1 provided remarkable protection from tissue injury in various oxidative stress-related disease models ranging from stroke, diabetes, diabetic endothelial dysfunction, myocardial ischemia-reperfusion, shock, Parkinson's disease, arthritis, colitis to dermatitis and uveitis. These beneficial effects are attributed to inhibition of the PARP-1 mediated suicidal pathway and to reduced expression of inflammatory cytokines and other mediators (e.g. inducible nitric oxide synthase).
Authors:
László Virág
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Current vascular pharmacology     Volume:  3     ISSN:  1570-1611     ISO Abbreviation:  Curr Vasc Pharmacol     Publication Date:  2005 Jul 
Date Detail:
Created Date:  2005-07-19     Completed Date:  2005-08-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101157208     Medline TA:  Curr Vasc Pharmacol     Country:  United Arab Emirates    
Other Details:
Languages:  eng     Pagination:  209-14     Citation Subset:  IM    
Affiliation:
Department of Medical Chemistry, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Bem tér 18/B, Hungary. lvirag@dote.hu
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MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis
Enzyme Inhibitors / pharmacology
Glycoside Hydrolases / metabolism*
Humans
Necrosis
Oxidative Stress*
Poly Adenosine Diphosphate Ribose / metabolism*
Poly(ADP-ribose) Polymerases / antagonists & inhibitors,  metabolism*
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 26656-46-2/Poly Adenosine Diphosphate Ribose; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.143/poly ADP-ribose glycohydrolase

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