Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-07

AUTHORS

Donald W. Nicholson, Ambereen Ali, Nancy A. Thornberry, John P. Vaillancourt, Connie K. Ding, Michel Gallant, Yves Gareau, Patrick R. Griffin, Marc Labelle, Yuri A. Lazebnik, Neil A. Munday, Sayyaparaju M. Raju, Mark E. Smulson, Ting-Ting Yamin, Violeta L. Yu, Douglas K. Miller

ABSTRACT

The protease responsible for the cleavage of poly(ADP-ribose) polymerase and necessary for apoptosis has been purified and characterized. This enzyme, named apopain, is composed of two subunits of relative molecular mass (Mr) 17K and 12K that are derived from a common proenzyme identified as CPP32. This proenzyme is related to interleukin-lβ-converting enzyme (ICE) and CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans. A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death. More... »

PAGES

37-43

Journal

TITLE

Nature

ISSUE

6535

VOLUME

376

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/376037a0

    DOI

    http://dx.doi.org/10.1038/376037a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038492988

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7596430


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