title: Inactivation of human cystatin C and kininogen by human cathepsin D.
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.
authors.affiliation: Department of Biochemistry, Jozef Stefan Institute, Slovenia, Yugoslavia.
authors.forename: B
authors.initials: B
authors.lastname: Lenarcic
authors.forename: M
authors.initials: M
authors.lastname: Krasovec
authors.forename: A
authors.initials: A
authors.lastname: Ritonja
authors.forename: I
authors.initials: I
authors.lastname: Olafsson
authors.forename: V
authors.initials: V
authors.lastname: Turk
mesh_terms: D000595:Amino Acid Sequence; D002402:Cathepsin D / Q000494:pharmacology*; D002851:Chromatography, High Pressure Liquid; D055316:Cystatin C; D015891:Cystatins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D007704:Kininogens / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010920:Placenta / Q000201:enzymology; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: C525030:CST3 protein, human; D055316:Cystatin C; D015891:Cystatins; D007704:Kininogens; D011994:Recombinant Proteins; D003546:Cysteine Endopeptidases; D002402:Cathepsin D