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Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35

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 apoptosi...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1995-09, Vol.269 (5232), p.1885-1888
Main Authors: Bump, N.J. (BASF Bioresearch Corporation, Worchester, MA.), Hackett, M, Hugunin, M, Seshagiri, S, Brady, K, Chen, P, Ferenz, C, Franklin, S, Ghayur, T, Li, P
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Language:English
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Summary: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
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7569933