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Aegyptin inhibits collagen-induced coagulation activation in vitro and thromboembolism in vivo.

Abstract：

:Aegyptin is a mosquito salivary gland protein and potent inhibitor of platelet aggregation. Aegyptin binds to the von Willebrand factor-binding site on collagen and prevents its interaction with platelets. Because collagen also induces plasma clotting by activation of factor XII, we evaluated the effects of aegyptin on collagen-induced coagulation activation and how it interferes with thrombosis in three different in vivo models. Our results demonstrate that aegyptin abolishes collagen-induced clot formation and thrombin generation in platelet-free plasma. Aegyptin has no antithrombotic activity in the arteriovenous shunt model (collagen-independent) but it prevents laser-induced collagen-mediated thrombus formation in rats. Furthermore, aegyptin protects mice from collagen and epinephrine-induced thromboembolism. Therefore, aegyptin has a dual antithrombotic mechanism: inhibition of platelet-collagen interaction and collagen's pro-coagulant activity. This is the first description of a collagen-binding protein that also inhibits collagen-mediated coagulant activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mizurini DM,Francischetti IM,Monteiro RQ

doi

10.1016/j.bbrc.2013.05.082

subject

Has Abstract

pub_date

2013-06-28 00:00:00

pages

235-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)00889-9

journal_volume

436

pub_type

杂志文章

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