原创力文档selective down-regulation of nuclear poly(adp-ribose) glycohydrolase有选择性的核聚(adp-ribose)glycohydrolase下调.pdfVIP
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selective down-regulation of nuclear poly(adp-ribose) glycohydrolase有选择性的核聚(adp-ribose)glycohydrolase下调
Selective Down-Regulation of Nuclear Poly(ADP-Ribose)
Glycohydrolase
David M. Burns¤a, Weihai Ying¤b, Tiina M. Kauppinen, Keqing Zhu¤c, Raymond A. Swanson*
Department of Neurology, University of California at San Francisco and Veterans Affairs Medical Center, San Francisco, California, United States of America
Abstract
Background: The formation of ADP-ribose polymers on target proteins by poly(ADP-ribose) polymerases serves a variety of
cell signaling functions. In addition, extensive activation of poly(ADP-ribose) polymerase-1 (PARP-1) is a dominant cause of
cell death in ischemia-reperfusion, trauma, and other conditions. Poly(ADP-ribose) glycohydrolase (PARG) degrades the
ADP-ribose polymers formed on acceptor proteins by PARP-1 and other PARP family members. PARG exists as multiple
isoforms with differing subcellular localizations, but the functional significance of these isoforms is uncertain.
Methods / Principal Findings: Primary mouse astrocytes were treated with an antisense phosphorodiamidate morpholino
oligonucleotide (PMO) targeted to exon 1 of full-length PARG to suppress expression of this nuclear-specific PARG isoform.
The antisense-treated cells showed down-regulation of both nuclear PARG immunoreactivity and nuclear PARG enzymatic
activity, without significant alteration in cytoplasmic PARG activity. When treated with the genotoxic agent MNNG to
induced PARP-1 activation, the antisense-treated cells showed a delayed rate of nuclear PAR degradation, reduced nuclear
condensation, and reduced cell death.
Conclusions/Significance: These results support a preferentially nuclear localization for full-length PARG, and suggest a key
role for this isoform in the PARP-1 cell death pathway.
Citation: Burns DM, Ying W, Kauppinen TM, Zhu K, Swanson RA (2009) Selective Down-Regulation of Nuclear Poly(ADP-Ribose) Glycohydrolase. PL
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