Abstract
The protease responsible for the cleavage of poly(ADP-ribose) polymerase and necessary for apoptosis has been purified and characterized. This enzyme, named apopain, is composed of two subunits of relative molecular mass (M(r)) 17K and 12K that are derived from a common proenzyme identified as CPP32. This proenzyme is related to interleukin-1 beta-converting enzyme (ICE) and CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans. A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis / physiology*
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Caenorhabditis elegans
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Caenorhabditis elegans Proteins
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Caspase 1
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Caspase 3
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Caspases*
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Cysteine Endopeptidases / chemistry
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Cysteine Endopeptidases / isolation & purification
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors / pharmacology
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Enzyme Precursors / metabolism*
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Helminth Proteins / antagonists & inhibitors
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Helminth Proteins / metabolism*
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Humans
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Kinetics
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Mass Spectrometry
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Molecular Sequence Data
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Poly(ADP-ribose) Polymerases / metabolism*
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Tumor Cells, Cultured
Substances
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Caenorhabditis elegans Proteins
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Cysteine Proteinase Inhibitors
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Enzyme Precursors
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Helminth Proteins
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Poly(ADP-ribose) Polymerases
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CASP3 protein, human
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Caspase 3
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Caspases
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Cysteine Endopeptidases
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ced-3 protein, C elegans
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Caspase 1