Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35
1995
Bump, N.J. | Hackett, M. | Hugunin, M. | Seshagiri, S. | Brady, K. | Chen, P. | Ferenz, C. | Franklin, S. | Ghayur, T. | Li, P.
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.
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