JARARHAGIN AND JARACETIN - NOVEL SNAKE-VENOM INHIBITORS OF THE INTEGRIN COLLAGEN RECEPTOR, ALPHA(2)BETA(1)

被引：84

作者：

DELUCA, M ^{[1
]}

WARD, CM ^{[1
]}

OHMORI, K ^{[1
]}

ANDREWS, RK ^{[1
]}

BERNDT, MC ^{[1
]}

机构：

[1] BAKER MED RES INST,HAZEL & PIP APPEL VASC BIOL LAB,PRAHRAN,VIC 3181,AUSTRALIA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 206卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1081

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：

Two novel proteins, jararhagin and jaracetin, were purified jararaca viper venom. Jararhagin is a 55-kDa member of the metalloprotease-disintegrin family. Jaracetin is a 60-kDa dimer representing a differently processed form of jararhagin. Like botrocetin, a previously described viper venom protein, jararhagin and jaracetin modulated binding of von Willebrand Factor to the glycoprotein Ib-IX complex on platelets through a specific interaction with the von Willebrand Factor A1 domain. Both jararhagin and jaracetin, but not botrocetin, also blocked alpha(2) beta(1)-dependent platelet adhesion to collagen, a receptor interaction mediated through a homologous A domain on the integrin alpha(2) subunit. (C) 1995 Academic Press, Inc.

引用

页码：570 / 576

页数：7