| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 275, Issue 20, 15504-15511, May 19, 2000
From the ¶ Poly(ADP-ribose) Metabolism Group, Health and
Environment Unit, Laval University Medical Research Center, CHUQ and
Faculty of Medicine, Laval University, Ste-Foy, Quebec, G1V 4G2 Canada
and the Poly(ADP-ribose) polymerase-1 (PARP-1) is an
abundant nuclear enzyme that catalyzes the synthesis of
poly(ADP-ribose) (pADPr) from its substrate NAD+ upon
binding to DNA strand breaks. Poly(ADP-ribosyl)ation has been
implicated in many cellular processes including replication, transcription, and the maintenance of genomic stability. However, studies with mice and cells lacking PARP-1 reveal a critical role for
the enzyme in the maintenance of genomic integrity only. Recently, a
significant level of poly(ADP-ribose) polymerase activity has been
detected in fibroblasts derived from mice lacking PARP-1 following
treatment with genotoxic agents (Shieh, W. M., Amé, J-C.,
Wilson, M. V., Wang, Z-Q., Koh, D. W., Jacobson, M. K., and Jacobson, E. L. (1998) J. Biol. Chem. 273, 30069-30072). We have isolated a cDNA that originates from PARP-1
( The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF126717.
Characterization of sPARP-1
AN ALTERNATIVE PRODUCT OF PARP-1 GENE WITH
POLY(ADP-RIBOSE) POLYMERASE ACTIVITY INDEPENDENT OF DNA STRAND
BREAKS*
¶§,¶,
, and International Agency for Research on Cancer (IARC), 150 Cours Albert-Thomas, 69372 Lyon Cedex 08, France
/) fibroblasts and encodes a polypeptide of 493 amino acid
residues bearing poly(ADP-ribose) polymerase activity. This protein,
that we named sPARP-1 for short poly(ADP-ribose)
polymerase-1, has a calculated mass of 55.3 kDa and is
identical in deduced amino acid sequence to the catalytic domain of
PARP-1. Radiation hybrid analysis assigned the sPARP-1 gene
to the chromosome 1H5-H6 in an immediate proximity to the known
location of PARP-1 gene, indicating that sPARP-1 and PARP-1 are most probably products of the same gene. Active sPARP-1 is present
in both PARP-1 (+/+) and PARP-1 (/) cells as demonstrated by
activity-Western blotting and immunostaining using a specific antibody
developed against sPARP-1. Like PARP-1, sPARP-1 is localized in the
cell nucleus, uses NAD+ as a substrate and is inhibited by
nicotinamide analogues. sPARP-1 produces pADPr of similar length and
structure to that of PARP-1. However, contrary to PARP-1, sPARP-1 does
not require DNA strand breaks for its activation, although it is
stimulated following genotoxic treatments.
*
This work was supported by Medical Research Council of
Canada Grant MT-6128 and National Cancer Institute of Canada Grant 008235.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to the results of this work.
§
Present address: Dept. of Biology 68-371, Massachusetts Institute
of Technology, 77 Massachusetts Ave., Cambridge, MA 02139.
**
To whom correspondence should be addressed: CHUL Research Center,
CHUQ, 2705, Boul. Laurier, Ste-Foy, Quebec, G1V 4G2 Canada. Tel.:
418-654-2267; Fax: 418-654-2159; E-mail:
Guy.Poirier@crchul.ulaval.ca.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  P. O. Hassa, S. S. Haenni, M. Elser, and M. O. Hottiger Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going? Microbiol. Mol. Biol. Rev., September 1, 2006; 70(3): 789 - 829. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Wang, S.-W. Yu, D. W. Koh, J. Lew, C. Coombs, W. Bowers, H. J. Federoff, G. G. Poirier, T. M. Dawson, and V. L. Dawson Apoptosis-Inducing Factor Substitutes for Caspase Executioners in NMDA-Triggered Excitotoxic Neuronal Death J. Neurosci., December 1, 2004; 24(48): 10963 - 10973. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Suzuki, E. Masini, C. Mazzocca, S. Cuzzocrea, A. Ciampa, H. Suzuki, and D. Bani Inhibition of Poly(ADP-Ribose) Polymerase Prevents Allergen-Induced Asthma-Like Reaction in Sensitized Guinea Pigs J. Pharmacol. Exp. Ther., December 1, 2004; 311(3): 1241 - 1248. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Wieler, J.-P. Gagne, H. Vaziri, G. G. Poirier, and S. Benchimol Poly(ADP-ribose) Polymerase-1 Is a Positive Regulator of the p53-mediated G1 Arrest Response following Ionizing Radiation J. Biol. Chem., May 23, 2003; 278(21): 18914 - 18921. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. L. Andreone, M. O'Connor, A. Denenberg, P. W. Hake, and B. Zingarelli Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts J. Immunol., February 15, 2003; 170(4): 2113 - 2120. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Virag and C. Szabo The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors Pharmacol. Rev., September 1, 2002; 54(3): 375 - 429. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Los, M. Mozoluk, D. Ferrari, A. Stepczynska, C. Stroh, A. Renz, Z. Herceg, Z.-Q. Wang, and K. Schulze-Osthoff Activation and Caspase-mediated Inhibition of PARP: A Molecular Switch between Fibroblast Necrosis and Apoptosis in Death Receptor Signaling Mol. Biol. Cell, March 1, 2002; 13(3): 978 - 988. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Perkins, D. Sun, A. Nguyen, S. Tulac, M. Francesco, H. Tavana, H. Nguyen, S. Tugendreich, P. Barthmaier, J. Couto, et al. Novel Inhibitors of Poly(ADP-ribose) Polymerase/PARP1 and PARP2 Identified Using a Cell-based Screen in Yeast Cancer Res., May 1, 2001; 61(10): 4175 - 4183. [Abstract] [Full Text]
|
|
|
|
 |
|
 C. M. Simbulan-Rosenthal, D. S. Rosenthal, R. Luo, J.-H. Li, J. Zhang, and M. E. Smulson Inhibition of poly(ADP-ribose) polymerase activity is insufficient to induce tetraploidy Nucleic Acids Res., February 1, 2001; 29(3): 841 - 849. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. D. Vodenicharov, F. R. Sallmann, M. S. Satoh, and G. G. Poirier Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1 Nucleic Acids Res., October 15, 2000; 28(20): 3887 - 3896. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W.-M. TONG, D. GALENDO, and Z.-Q. WANG Role of DNA Break-sensing Molecule Poly(ADP-ribose) Polymerase (PARP) in Cellular Function and Radiation Toxicity Cold Spring Harb Symp Quant Biol, January 1, 2000; 65(0): 583 - 592. [Abstract] [PDF]
|
|
|
|
|
|
J. M. Pleschke, H. E. Kleczkowska, M. Strohm, and F. R. Althaus Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins J. Biol. Chem., December 22, 2000; 275(52): 40974 - 40980. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. B. Affar, M. Germain, E. Winstall, M. Vodenicharov, R. G. Shah, G. S. Salvesen, and G. G. Poirier Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis J. Biol. Chem., January 19, 2001; 276(4): 2935 - 2942. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
O. I. Lavrik, R. Prasad, R. W. Sobol, J. K. Horton, E. J. Ackerman, and S. H. Wilson Photoaffinity Labeling of Mouse Fibroblast Enzymes by a Base Excision Repair Intermediate. EVIDENCE FOR THE ROLE OF POLY(ADP-RIBOSE) POLYMERASE-1 IN DNA REPAIR J. Biol. Chem., June 29, 2001; 276(27): 25541 - 25548. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
