Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis*
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Binding Sites
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Binding, Competitive
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Caspase 1
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Cell Line
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors / genetics
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Cysteine Proteinase Inhibitors / metabolism*
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Cysteine Proteinase Inhibitors / pharmacology
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Enzyme Activation / drug effects
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Humans
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Inhibitor of Apoptosis Proteins
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Molecular Sequence Data
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Recombinant Proteins / pharmacology
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Transfection
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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Viral Proteins / pharmacology
Substances
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Cysteine Proteinase Inhibitors
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Inhibitor of Apoptosis Proteins
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Recombinant Proteins
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Viral Proteins
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inhibitor of apoptosis, Nucleopolyhedrovirus
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Cysteine Endopeptidases
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Caspase 1