Publication Date:
1995-09-29
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bump, N J -- Hackett, M -- Hugunin, M -- Seshagiri, S -- Brady, K -- Chen, P -- Ferenz, C -- Franklin, S -- Ghayur, T -- Li, P -- AI 38262/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1885-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BASF Bioresearch Corporation, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569933" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
*Apoptosis
;
Binding Sites
;
Binding, Competitive
;
Caspase 1
;
Cell Line
;
Cysteine Endopeptidases/*metabolism
;
Cysteine Proteinase Inhibitors/genetics/*metabolism/pharmacology
;
Enzyme Activation/drug effects
;
Humans
;
Inhibitor of Apoptosis Proteins
;
Molecular Sequence Data
;
Recombinant Proteins/pharmacology
;
Transfection
;
Viral Proteins/genetics/*metabolism/pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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