Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death
Duriez, P.J. and Shah, G.M. (1997) Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death. Biochemistry and Cell Biology, 75, (4), 337-349. (doi:10.1139/bcb-75-4-337). (PMID:9493956).
Full text not available from this repository.
Proteases play a crucial role in apoptosis or programmed cell death. The aim of this review is to highlight the purpose for which these proteases are activated, i.e., to specifically cleave a select subset of cellular proteins at an appropriate time during cell death. Poly(ADP-ribose) polymerase (PARP), a nuclear protein implicated in DNA repair, is one of the earliest proteins targeted for a specific cleavage to the signature 89-kDa fragment during apoptosis. Characterization of the apoptotic cleavage of PARP and other target proteins helped in understanding the role of cysteine aspartic acid specific proteases (caspases) in the apoptotic process. We have recently identified that in some models of cell death, the cleavage pattern for PARP is different from production of the signature 89-kDa fragment. Necrotic death of HL-60 cells and apoptotic death of Jurkat cells mediated by granzyme B and perforin were accompanied by distinct additional fragments, suggesting cleavage of PARP at other sites by caspases or other death proteases. This review summarizes how detection and characterization of PARP cleavage could serve as a sensitive parameter for identification of different types of cell death and as a marker for activation of different death proteases. The putative biological functions for early cleavage of PARP in apoptosis are also discussed.
|Subjects:||Q Science > QE Geology
Q Science > QH Natural history > QH301 Biology
|Divisions:||University Structure - Pre August 2011 > School of Medicine > Cancer Sciences
|Date Deposited:||05 Oct 2010 11:22|
|Last Modified:||01 Jun 2011 15:29|
|Contributors:||Duriez, P.J. (Author)
Shah, G.M. (Author)
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
Actions (login required)