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

Y. A. Lazebnik, S. H. Kaufmann, S. Desnoyers, G. G. Poirier, W. C. Earnshaw

Research output: Contribution to journalArticlepeer-review

2280 Scopus citations


RECENT studies suggest that pro teases of the interleukin 1-β-converting enzyme (ICE)/ced-3 family are involved in initiating the active phase of apoptosis1-3. 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 apoptosis4. prICE cleaves the nuclear enzyme poly(ADP-ribose) polymerase (PARP) at a tetrapeptide sequence identical to one of two ICE sites in pro-inter leu kin-l-β. However, prICE does not cleave purified pro-interleukin- 1-β 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.

Original languageEnglish (US)
Pages (from-to)346-347
Number of pages2
Issue number6495
StatePublished - 1994

ASJC Scopus subject areas

  • General


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