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Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases.

Authors
  • Kamens, J
  • Paskind, M
  • Hugunin, M
  • Talanian, R V
  • Allen, H
  • Banach, D
  • Bump, N
  • Hackett, M
  • Johnston, C G
  • Li, P
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Jun 23, 1995
Volume
270
Issue
25
Pages
15250–15256
Identifiers
PMID: 7797510
Source
Medline
License
Unknown

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.

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