Abstract
As a model to investigate the mechanism of caspase activation we have analysed the processing of pro-caspase-7 by serine proteases with varied specificities. The caspase-7 zymogen was rapidly activated by granzyme B and more slowly by subtilisin and cathepsin G, generating active enzymes with similar kinetic properties. Significantly, cathepsin G activated the zymogen by cleaving at a Gln-Ala bond, indicating that the canonical cleavage specificity at aspartic acid is not required for activation.
MeSH terms
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Amino Acid Sequence
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Caspase 7
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Caspases*
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Cathepsin G
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Cathepsins / metabolism
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Chymotrypsin / metabolism
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism*
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DNA, Complementary / genetics
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Enzyme Activation
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Enzyme Precursors / genetics
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Enzyme Precursors / metabolism*
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Granzymes
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Humans
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Protein Sorting Signals / metabolism
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Recombinant Fusion Proteins / metabolism
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Serine Endopeptidases / metabolism*
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Substrate Specificity
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Subtilisins / metabolism
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Trypsin / metabolism
Substances
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DNA, Complementary
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Enzyme Precursors
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Cathepsins
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GZMB protein, human
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Granzymes
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Serine Endopeptidases
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Subtilisins
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Chymotrypsin
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CTSG protein, human
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Cathepsin G
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Trypsin
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CASP7 protein, human
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Caspase 7
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Caspases
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Cysteine Endopeptidases