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Vol. 54, Issue 3, 375-430, September 2002
Inotek Pharmaceutical Corp., Beverly, Massachusetts (L.V.,
C.S.); Department of Medical Chemistry, Medical and Health Science
Center, University of Debrecen, Debrecen, Hungary (L.V.); and Institute
of Human Physiology and Clinical Experimental Research, Semmelweis
University, Budapest, Hungary (C.S.)
I. Poly(ADP-Ribose) Metabolism
A. Structure and Function of PARP-1
B. PARP Homologs
Tankyrase-1.
C. Poly(ADP-Ribose) Catabolism: Poly(ADP-Ribose) Glycohydrolase
D. PARP in DNA Repair
E. PARP-1 in Cell Death
1. Apoptosis.
2. Necrosis.
3. Complex Role of PARP-1 in DNA Damage-Induced Cell Death.
F. PARP-1 in the Regulation of Cell Proliferation and
Differentiation
G. PARP in the Regulation of Gene Expression
II. Pharmacological Inhibition of PARP
III. Beneficial Effects of PARP Inhibition in Various
Pathophysiological States
A. Activation of PARP in Pathophysiological Conditions
B. PARP Activation and Cell Necrosis: Implications for
Pathophysiology
C. PARP and Proinflammatory Signal Transduction: Implications for
Pathophysiology
D. PARP in Myocardial Reperfusion Injury
E. PARP in the Pathogenesis of Cardiomyopathy and Toxic Myocardial
Injury
F. PARP in Stroke
G. PARP in Neurotrauma
H. PARP in Reperfusion Injury of the Gut, Eye, Kidney, and Skeletal
Muscle
I. PARP in Arthritis
J. PARP in Inflammatory Bowel Disease
K. PARP in Inflammatory Diseases of the Central Nervous System:
Allergic Encephalomyelitis to Multiple Sclerosis
L. PARP in Systemic Inflammation and Circulatory Shock
M. PARP in the Pathogenesis of Diabetes
N. PARP in the Pathogenesis of Diabetic Cardiovascular Dysfunction
O. PARP Inhibitors as Adjuvant Therapeutics for the Treatment of
Various Forms of Cancer
P. Antiretroviral Effect of PARP Inhibitors
Q. PARP in the Pathogenesis of Other Diseases
IV. Conclusions and Future Directions
Acknowledgments
References
Poly(ADP-ribose) polymerase-1 (PARP-1) is a
member of the PARP enzyme family consisting of PARP-1 and several
recently identified novel poly(ADP-ribosylating) enzymes. PARP-1 is an
abundant nuclear protein functioning as a DNA nick-sensor enzyme. Upon
binding to DNA breaks, activated PARP cleaves NAD+ into
nicotinamide and ADP-ribose and polymerizes the latter onto nuclear
acceptor proteins including histones, transcription factors, and PARP
itself. Poly(ADP-ribosylation) contributes to DNA repair and to the
maintenance of genomic stability. On the other hand, oxidative
stress-induced overactivation of PARP consumes NAD+ and
consequently ATP, culminating in cell dysfunction or necrosis. This
cellular suicide mechanism has been implicated in the pathomechanism of
stroke, myocardial ischemia, diabetes, diabetes-associated cardiovascular dysfunction, shock, traumatic central nervous system injury, arthritis, colitis, allergic encephalomyelitis, and various other forms of inflammation. PARP has also been shown to associate with
and regulate the function of several transcription factors. Of special
interest is the enhancement by PARP of nuclear factor 
B-mediated
transcription, which plays a central role in the expression of
inflammatory cytokines, chemokines, adhesion molecules, and inflammatory mediators. Herein we review the double-edged sword roles
of PARP in DNA damage signaling and cell death and summarize the
underlying mechanisms of the anti-inflammatory effects of PARP
inhibitors. Moreover, we discuss the potential use of PARP inhibitors
as anticancer agents, radiosensitizers, and antiviral agents.
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G. Cipriani, E. Rapizzi, A. Vannacci, R. Rizzuto, F. Moroni, and A. Chiarugi Nuclear Poly(ADP-ribose) Polymerase-1 Rapidly Triggers Mitochondrial Dysfunction J. Biol. Chem., April 29, 2005; 280(17): 17227 - 17234. [Abstract] [Full Text] [PDF]
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 G. Szabo, P. Soos, U. Heger, C. Flechtenmacher, S. Bahrle, Z. Zsengeller, C. Szabo, and S. Hagl Poly(ADP-ribose) polymerase inhibition attenuates biventricular reperfusion injury after orthotopic heart transplantation Eur. J. Cardiothorac. Surg., February 1, 2005; 27(2): 226 - 234. [Abstract] [Full Text] [PDF]
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T. Genovese, E. Mazzon, C. Muia, N. S. A. Patel, M. D. Threadgill, P. Bramanti, A. De Sarro, C. Thiemermann, and S. Cuzzocrea Inhibitors of Poly(ADP-Ribose) Polymerase Modulate Signal Transduction Pathways and Secondary Damage in Experimental Spinal Cord Trauma J. Pharmacol. Exp. Ther., February 1, 2005; 312(2): 449 - 457. [Abstract] [Full Text] [PDF]
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