Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases

被引：12

作者：

Barros, NMT

Puzer, L

Tersariol, ILS

Oliva, MLV

Sampaio, CAM

Carmona, AK

da Motta, G ^{[1
]}

机构：

[1] Univ Fed Sao Paulo, Dept Bioquim, EPM, BR-04044020 Sao Paulo, Brazil

[2] Univ Fed Sao Paulo, Dept Biofes, BR-04044020 Sao Paulo, Brazil

[3] Univ Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, BR-08701970 Mogi das Cruzes, SP, Brazil

来源：

BIOLOGICAL CHEMISTRY | 2004年 / 385卷 / 11期

基金：

巴西圣保罗研究基金会;

关键词：

cathepsins; kallikrein; kinin system; proteolysis;

D O I：

10.1515/BC.2004.141

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：

Plasma kallikrein plays a role in coagulation, fibrinolysis and inflammation. Cathepsins B and L participate in (patho)physiological processes such as peptide antigen processing, tissue remodeling events, protein turnover in cells, hormone processing and tumor invasion. The present work analyzes the processing of prekallikrein/kallikrein by lysosomal cathepsins. Prekallikrein is not hydrolyzed by catB, and catL generates an inactive fragment of prekallikrein. Both kallikrein chains are hydrolyzed by catL and the light chain is mainly hydrolyzed by catB; kallikrein activity is lower after incubation with catL compared to catB. Our data suggest that the plasma kallikrein/kinin system can be controlled by cathepsins.

引用

页码：1087 / 1091

页数：5

共 38 条

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