Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells

Faleiro, L., Kobayashi, R., Fearnhead, H., Lazebnik, Y. (1997) Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. Embo Journal, 16 (9). pp. 2271-2281. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/9171342
DOI: 10.1093/emboj/16.9.2271

Abstract

The activity of ICE-like proteases or caspases is essential for apoptosis. Multiple caspases participate in apoptosis in mammalian cells but how many caspases are involved and what is their relative contribution to cell death is poorly understood. To identify caspases activated in apoptotic cells, we developed an approach to simultaneously detect multiple active caspases. Using tumor cells as a model, we have found that CPP32 (caspase 3) and Mch2 (caspase 6) are the major active caspases in apoptotic cells, and are activated in response to distinct apoptosis-inducing stimuli and in all cell lines analyzed. Both CPP32 and Mch2 are present in apoptotic cells as multiple active species. In a given cell line these species remained the same irrespective of the apoptotic stimulus used. However, the species of CPP32 and Mch2 detected varied between cell lines, indicating differences in caspase processing. The strategy described here is widely applicable to identify active caspases involved in apoptosis.

Item Type: Paper
Uncontrolled Keywords: Affinity Labels Amino Acid Sequence Apoptosis Caspase 3 Caspase 6 Caspases Cysteine Endopeptidases Electrophoresis, Gel, Two-Dimensional Enzyme Activation Enzyme Precursors Humans Jurkat Cells Molecular Sequence Data Protein Processing, Post-Translational
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: 1997
Date Deposited: 12 Dec 2012 17:33
Last Modified: 12 Dec 2012 17:33
PMCID: PMC1169829
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26400

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