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Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
Seong-Woon Yu,1*Hongmin Wang,1*Marc F. Poitras,1Carmen Coombs,1William J. Bowers,5Howard J. Federoff,5Guy G. Poirier,6Ted M. Dawson,124Valina L. Dawson1234
Poly(ADP-ribose) polymerase-1 (PARP-1) protects the
genome by functioning in the DNA damage surveillance network. PARP-1 isalso a mediator of cell death after ischemia-reperfusion injury,glutamate excitotoxicity, and various inflammatory processes.We show
that PARP-1 activation is required for translocation ofapoptosis-inducing factor (AIF) from the mitochondria to the nucleusand that AIF is necessary for PARP-1-dependent cell death.
N-methyl-N'-nitro-N-nitrosoguanidine,H2O2, and
N-methyl-D-aspartate induce AIF translocation
and celldeath, which is prevented by PARP inhibitors or genetic
knockoutof PARP-1, but is caspase independent. Microinjection of an
antibodyto AIF protects against PARP-1-dependent cytotoxicity. These
datasupport a model in which PARP-1 activation signals AIF releasefrom mitochondria, resulting in a caspase-independent pathwayof
programmed cell death.
1 Departments of Neurology,
2 Neuroscience, and
3 Physiology;
and
4 the Institute for Cell Engineering, Johns
Hopkins University School of Medicine, Baltimore, MD 21287, USA.
5 Department of Neurology, Center for Aging and
Developmental Biology, University of Rochester, NY 14642, USA.
6 Health and Environment Unit, Laval University
Medical Research Center, CHUQ, Ste-Foy, Quebec G1V 4G2, Canada.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
vdawson{at}jhmi.edu
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Alberto Chiarugi and Michael A. Moskowitz (12 July 2002) Science297 (5579), 200.
[DOI: 10.1126/science.1074592] |Summary »|Full Text »|PDF »
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Ester Derivatives of Tournefolic Acid B Attenuate N-Methyl-D-aspartate-Mediated Excitotoxicity in Rat Cortical Neurons.
Involvement of the ATR- and ATM-Dependent Checkpoint Responses in Cell Cycle Arrest Evoked by Pierisin-1.
B. Shiotani, M. Kobayashi, M. Watanabe, K.-i. Yamamoto, T. Sugimura, and K. Wakabayashi (2006)
Mol. Cancer Res.
4, 125-133
|Abstract »|Full Text »|PDF »
IGF-1 receptor tyrosine kinase inhibition by the cyclolignan PPP induces G2/M-phase accumulation and apoptosis in multiple myeloma cells.
T. Stromberg, S. Ekman, L. Girnita, L. Y. Dimberg, O. Larsson, M. Axelson, J. Lennartsson, U. Hellman, K. Carlson, A. Osterborg, et al. (2006)
Blood
107, 669-678
|Abstract »|Full Text »|PDF »
Poly(ADP-ribose) Polymerase-1-dependent Cardiac Myocyte Cell Death during Heart Failure Is Mediated by NAD+ Depletion and Reduced Sir2{alpha} Deacetylase Activity.
J. B. Pillai, A. Isbatan, S.-i. Imai, and M. P. Gupta (2005)
J. Biol. Chem.
280, 43121-43130
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Metalloporphyrin-Based Superoxide Dismutase Mimic Attenuates the Nuclear Translocation of Apoptosis-Inducing Factor and the Subsequent DNA Fragmentation After Permanent Focal Cerebral Ischemia in Mice.
Apoptosis-Inducing Factor Triggered by Poly(ADP-Ribose) Polymerase and Bid Mediates Neuronal Cell Death after Oxygen-Glucose Deprivation and Focal Cerebral Ischemia.
C. Culmsee, C. Zhu, S. Landshamer, B. Becattini, E. Wagner, M. Pellecchia, K. Blomgren, and N. Plesnila (2005)
J. Neurosci.
25, 10262-10272
|Abstract »|Full Text »|PDF »
"Simple but not simpler": toward a unified picture of energy requirements in cell death.
Tumour necrosis factor-induced death of adult human oligodendrocytes is mediated by apoptosis inducing factor.
A. Jurewicz, M. Matysiak, K. Tybor, L. Kilianek, C. S. Raine, and K. Selmaj (2005)
Brain
128, 2675-2688
|Abstract »|Full Text »|PDF »
Pivotal Role of Akt Activation in Mitochondrial Protection and Cell Survival by Poly(ADP-ribose)polymerase-1 Inhibition in Oxidative Stress.
A. Tapodi, B. Debreceni, K. Hanto, Z. Bognar, I. Wittmann, F. Gallyas Jr., G. Varbiro, and B. Sumegi (2005)
J. Biol. Chem.
280, 35767-35775
|Abstract »|Full Text »|PDF »
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD+ into a nuclear signal.
