| Literature DB >> 7797510 |
J Kamens1, M Paskind, M Hugunin, R V Talanian, H Allen, D Banach, N Bump, M Hackett, C G Johnston, P Li.
Abstract
Interleukin-1 beta converting enzyme (ICE) is a cytoplasmic cysteine protease required for generating the bioactive form of the interleukin-1 beta cytokine from its inactive precursor. We report the identification of ICH-2, a novel human gene encoding a member of the ICE cysteine protease family, and characterization of its protein product. ICH-2 mRNA is widely expressed in human tissues in a pattern similar to, but distinct from, that of ICE. Overexpression of ICH-2 in insect cells induces apoptosis. Purified ICH-2 is functional as a protease in vitro. A comparison of the inhibitor profiles and substrate cleavage by ICH-2 and ICE shows that the enzymes share catalytic properties but may differ in substrate specificities, suggesting that the two enzymes have different functions in vivo.Entities:
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Year: 1995 PMID: 7797510 DOI: 10.1074/jbc.270.25.15250
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157