Kamens J, Paskind M, Hugunin M, Talanian R V, Allen H, Banach D, Bump N, Hackett M, Johnston C G, Li P
BASF Bioresearch Corporation, Worcester, Massachusetts 01605, USA.
J Biol Chem. 1995 Jun 23;270(25):15250-6. doi: 10.1074/jbc.270.25.15250.
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.
白细胞介素-1β转化酶(ICE)是一种细胞质半胱氨酸蛋白酶,它对于从无活性前体生成具有生物活性形式的白细胞介素-1β细胞因子是必需的。我们报告了ICH-2的鉴定,这是一个编码ICE半胱氨酸蛋白酶家族成员的新型人类基因,以及对其蛋白质产物的表征。ICH-2 mRNA在人类组织中广泛表达,其模式与ICE相似但又不同。ICH-2在昆虫细胞中的过表达诱导细胞凋亡。纯化的ICH-2在体外作为蛋白酶具有功能。对ICH-2和ICE的抑制剂谱及底物切割的比较表明,这两种酶具有共同的催化特性,但底物特异性可能不同,这表明这两种酶在体内具有不同的功能。