期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 496, 期 1, 页码 9-20出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2010.01.010
关键词
Metalloproteinase; Snake venom; Atroxlysin; Hemostasis; Platelets
资金
- FAPEMIG [CBB 359/06, APQ-2673-40.1/07]
- DFG [SFB 815, SFB/TR23]
We report the isolation and structure-function relationship of a 23 kDa metalloproteinase named atroxlysin-I from the venom of the Peruvian Bothrops atrox (Jergon). Atroxlysin is a P-I metalloproteinase and contains 204 residues. Its proteolytic activity towards dimethylcasein is enhanced by Ca+2 but inhibited by EDTA, dithiothreitol, excessive Zn+2 and alpha 2-macroglobulin. Unlike other structurally homologous P-I metalloproteinases, atroxlysin-I causes hemorrhages. To examine its hemorrhagic activity mechanistically, we studied its function in vitro and in vivo. It cleaved the Ala(14)-Leu(15) and Tyr(16)-Leu(17) bonds in oxidized insulin B-chain and specifically hydrolyzed the alpha-chains of fibrin(ogen) in a dose- and time-dependent manner. Atroxlysin-I cleaved plasma fibronectin and other extracellular matrix proteins (collagens I and IV) and the triple-helical fragment CB3 of collagen IV. but did not degrade laminin-111. Complementarily, the laminin and collagen binding integrins alpha(7)beta(1) and alpha(1)beta(1) were cleaved by atroxlysin. Even without catalytic activity atroxlysin-I inhibited collagen- and ADP-triggered platelet aggregation. (C) 2010 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据