Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

Lazebnik, Y. A., Kaufmann, S. H., Desnoyers, S., Poirier, G. G., Earnshaw, W. C. (1994) Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature, 371 (6495). pp. 346-347. ISSN 0028-0836

URL: http://www.ncbi.nlm.nih.gov/pubmed/8090205
DOI: 10.1038/371346a0

Abstract

Recent studies suggest that proteases of the interleukin 1-beta-converting enzyme (ICE)/ced-3 family are involved in initiating the active phase of apoptosis. Here we identify a novel protease resembling ICE (prICE) that is active in a cell-free system that reproduces the morphological and biochemical events of apoptosis. prICE cleaves the nuclear enzyme poly(ADP-ribose) polymerase (PARP) at a tetrapeptide sequence identical to one of two ICE sites in pro-interleukin-1-beta. However, prICE does not cleave purified pro-interleukin-1-beta, and purified ICE does not cleave PARP, indicating that the two activities are distinct. Inhibition of prICE abolishes all manifestations of apoptosis in the extracts including morphological changes, cleavage of PARP and production of an oligonucleosomal ladder. These studies suggest that prICE might be pivotal in initiating the active phase of apoptosis in vitro and in intact cells.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Apoptosis Caspase 1 Cattle Cell-Free System Chickens Cysteine Endopeptidases HeLa Cells Humans Interleukin-1 Metalloendopeptidases Molecular Sequence Data Poly(ADP-ribose) Polymerases Protein Precursors
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > DNA polymerase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Labeznik lab
Depositing User: Matt Covey
Date: 1994
Date Deposited: 12 Dec 2012 17:32
Last Modified: 12 Dec 2012 17:32
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26404

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