Abstract
A papain inhibitor of 22 kDa was isolated from human placenta and shown to be identical to residues Cys246-Leu373 of the third domain of human kininogen. This kininogen domain and recombinant human cystatin C were inactivated by peptide bond cleavages at hydrophobic amino acid residues due to the action of cathepsin D. These results further support the proposed role of cathepsin D in the regulation of cysteine proteinase activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cathepsin D / pharmacology*
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Chromatography, High Pressure Liquid
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Cystatin C
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Cystatins / metabolism*
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Cysteine Endopeptidases / metabolism
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Enzyme Activation / drug effects
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Humans
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Kininogens / chemistry
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Kininogens / metabolism*
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Molecular Sequence Data
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Placenta / enzymology
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Protein Denaturation
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Recombinant Proteins / metabolism
Substances
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CST3 protein, human
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Cystatin C
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Cystatins
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Kininogens
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Recombinant Proteins
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Cysteine Endopeptidases
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Cathepsin D