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

来源：

FEBS LETTERS | 1991年 / 280卷 / 02期

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

页码：211 / 215

页数：5

共 32 条

[1] EFFICIENT PRODUCTION OF NATIVE, BIOLOGICALLY-ACTIVE HUMAN CYSTATIN-C BY ESCHERICHIA-COLI [J].