Evidence for an interleukin-1β converting enzyme (ICE)-like activity distinct from ICE and responsible for ICE and CPP32 cleavage during apoptosis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-01

AUTHORS

C. Miossec, V. Dutilleul, L. Durand, C. Faucheu, L. Pilatre, J. Golec, F. Fassy, A. Diu-Hercend

ABSTRACT

IL-1beta converting enzyme (ICE) and ICE-related proteases (IRPs) have been suggested to play a central role in apoptosis. We report the use of peptidic ICE inhibitors to reassess the role of this enzyme in the apoptosis induced by Fas or TNFalpha receptor ligation in Jurkat cells, U937 cells or monocytes. Our results show that inhibition of IL-1beta processing can be dissociated from inhibition of apoptosis. Indeed, two out of three com-pounds active on ICE are not inhibitory for apoptosis. This shows that ICE is not required for progression in the apoptotic pathway, but that one or several IRPs are necessary. In addition, Western blot analysis of cell lysates shows that both ICE and CPP32 precursors disappear rapidly after apoptosis induction, while ICH-1L precursor remains intact. Concomitant appearance of cleavage products can be visualized for CPP32, but not for ICE, suggesting that the former is proteolytically activated. In addition, this precursor cleavage can be blocked by an ICE inhibitor active on apoptosis. Altogether, our data support the hypothesis that one or several IRPs are necessary for apoptosis and are responsible for ICE and CPP32 cleavage during this process. More... »

PAGES

125-135

Journal

TITLE

Apoptosis

ISSUE

2

VOLUME

2

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1026404212849

DOI

http://dx.doi.org/10.1023/a:1026404212849

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046560514

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/14646547


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