Inactivation of human cystatin C and kininogen by human cathepsin D.
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.
Lenarcic
B
B
Department of Biochemistry, Jozef Stefan Institute, Slovenia, Yugoslavia.
Krasovec
M
M
Ritonja
A
A
Olafsson
I
I
Turk
V
V
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
C525030:CST3 protein, human; D055316:Cystatin C; D015891:Cystatins; D007704:Kininogens; D011994:Recombinant Proteins; D003546:Cysteine Endopeptidases; D002402:Cathepsin D