INACTIVATION OF HUMAN CYSTATIN-C AND KININOGEN BY HUMAN CATHEPSIN-D

被引:80
作者
LENARCIC, B [1 ]
KRASOVEC, M [1 ]
RITONJA, A [1 ]
OLAFSSON, I [1 ]
TURK, V [1 ]
机构
[1] UNIV LUND HOSP, DEPT CLIN CHEM, S-22185 LUND, SWEDEN
关键词
CYSTATIN-C; KININOGEN; CATHEPSIN-D; PROTEINASE INHIBITOR INACTIVATION;
D O I
10.1016/0014-5793(91)80295-E
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:211 / 215
页数:5
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