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

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

  • J Biol Chem. 1995 Jun 23;270(25):15250-6. doi: 10.1074/jbc.270.25.15250.
J Kamens 1 M Paskind M Hugunin R V Talanian H Allen D Banach N Bump M Hackett C G Johnston P Li
Affiliations

Affiliation

  • 1 BASF Bioresearch Corporation, Worcester, Massachusetts 01605, USA.
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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