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

Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A. (1995) Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature, 376 (6535). pp. 37-43. ISSN 0028-0836

URL: http://www.ncbi.nlm.nih.gov/pubmed/7596430
DOI: 10.1038/376037a0

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 (M(r)) 17K and 12K that are derived from a common proenzyme identified as CPP32. This proenzyme is related to interleukin-1 beta-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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Apoptosis Caenorhabditis elegans Caenorhabditis elegans Proteins Caspase 1 Caspase 3 Caspases Cysteine Endopeptidases Cysteine Proteinase Inhibitors Enzyme Precursors Helminth Proteins Humans Kinetics Mass Spectrometry Molecular Sequence Data Poly(ADP-ribose) Polymerases Tumor Cells, Cultured
Subjects: organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > apoptosis
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions
organs, tissues, organelles, cell types and functions > cell types and functions
CSHL Authors:
Communities: CSHL labs > Labeznik lab
Depositing User: Matt Covey
Date: 1995
Date Deposited: 12 Dec 2012 17:32
Last Modified: 12 Dec 2012 17:32
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26402

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