High molecular weight kininogen as substrate for cathepsin B

被引：14

作者：

Barros, NMT

Tersariol, ILS

Oliva, MLV

Araújo, MS

Sampaio, CAM

Juliano, L

da Motta, G ^{[1
]}

机构：

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

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

[3] Univ Fed Sao Paulo, EPM, Dept Biofis, BR-04044020 Sao Paulo, Brazil

来源：

BIOLOGICAL CHEMISTRY | 2004年 / 385卷 / 06期

基金：

巴西圣保罗研究基金会;

关键词：

cystatins; cysteine peptidase; kinin; zinc;

D O I：

10.1515/BC.2004.066

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：

We investigated the influence of pH and divalent cations (Zn2+, Mg2+ and Ca2+) on high molecular weight kininogen processing by cathepsin B. At pH 6.3, high molecular weight kininogen is hydrolyzed by cathepsin B at three sites generating fragments of 80, 60 and 40 kDa. Cathepsin B has kininogenase activity at this pH which is improved in the absence of divalent cations. At pH 7.35, high molecular weight kininogen is slightly cleaved by cathepsin B into fragments of 60 kDa, and cathepsin B kininogenase activity is impaired. Our results suggest that high molecular weight kininogen is a substrate for cathepsin B under pathophysiological conditions.

引用

页码：551 / 555

页数：5

共 44 条

[1] Cathepsin B activity regulation - Heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation [J].