INACTIVATION OF HUMAN PLASMA CL-INHIBITOR BY HUMAN-PMN LEUKOCYTE MATRIX METALLOPROTEINASES

被引：17

作者：

KNAUPER, V

TRIEBEL, S

REINKE, H

TSCHESCHE, H

机构：

[1] University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, D-4800 Bielefeld 1

来源：

FEBS LETTERS | 1991年 / 290卷 / 1-2期

关键词：

POLYMORPHONUCLEAR LEUKOCYTE COLLAGENASE; POLYMORPHONUCLEAR LEUKOCYTE GELATINASE; CL-INHIBITOR; PROTEOLYTIC INACTIVATION;

D O I：

10.1016/0014-5793(91)81235-Z

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：

Highly purified human polymorphonuclear (PMN) leucocyte matrix metalloproteinases, collagenase and gelatinase, cleaved human plasma Cl-inhibitor at the carboxyl site of Ala439 (P6). This led to a concomitant loss of Cl-inhibitor activity. An additional cleavage site, at the carboxyl site of Ser441 (P4), was observed during PMN leucocyte gelatinase-induced inactivation, and a minor fragment of the plasma Cl-inhibitor was generated.

引用

页码：99 / 102

页数：4

共 24 条

[1] IDENTIFICATION OF A NEW P1 RESIDUE MUTATION (444ARG-]SER) IN A DYSFUNCTIONAL C1 INHIBITOR PROTEIN CONTAINED IN A TYPE-II HEREDITARY ANGIOEDEMA PLASMA [J].