Bump N J, Hackett M, Hugunin M, Seshagiri S, Brady K, Chen P, Ferenz C, Franklin S, Ghayur T, Li P
BASF Bioresearch Corporation, Worcester, MA 01605, USA.
Science. 1995 Sep 29;269(5232):1885-8. doi: 10.1126/science.7569933.
The baculovirus antiapoptotic protein p35 inhibited the proteolytic activity of human interleukin-1 beta converting enzyme (ICE) and three of its homologs in enzymatic assays. Coexpression of p35 prevented the autoproteolytic activation of ICE from its precursor form and blocked ICE-induced apoptosis. Inhibition of enzymatic activity correlated with the cleavage of p35 and the formation of a stable ICE-p35 complex. The ability of p35 to block apoptosis in different pathways and in distantly related organisms suggests a central and conserved role for ICE-like proteases in the induction of apoptosis.
杆状病毒抗凋亡蛋白p35在酶活性测定中抑制了人白细胞介素-1β转换酶（ICE）及其三个同源物的蛋白水解活性。p35的共表达阻止了ICE从前体形式的自蛋白水解激活，并阻断了ICE诱导的细胞凋亡。酶活性的抑制与p35的裂解以及稳定的ICE-p35复合物的形成相关。p35在不同途径和远缘相关生物体中阻断细胞凋亡的能力表明，ICE样蛋白酶在细胞凋亡诱导中具有核心且保守的作用。
