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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-09

AUTHORS

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

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. More... »

PAGES

346-347

Journal

TITLE

Nature

ISSUE

6495

VOLUME

371

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/371346a0

    DOI

    http://dx.doi.org/10.1038/371346a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1048646533

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8090205


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