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- W3176146123 abstract "Aegyptin is a 30-kDa mosquito salivary gland protein that binds to collagen with high affinity (Kd=6 nM) and inhibits platelet aggregation. It recognizes the von Willebrand factor binding-site in collagen which could partially explain its biological activity. Herein we evaluated: 1. whether this protein could prevent in vitro collagen-induced plasma clotting; 2. the in vivo antithrombotic activity of aegyptin. Aegyptin does not affect collagen-mediated acceleration of plasma clotting. In accordance with this observation, aegyptin has no effect on collagen-induced FXII activation, as indirectly determined by measurement of kallikrein formation in plasma. Aegyptin has no antithrombotic activity in vivo by employing an arteriovenous shunt model in rats. This model is independent of collagen-exposure since presents no vascular surface for thrombus formation. On the other hand, aegyptin delays laser-induced carotid thrombus formation in the presence of Rose Bengal, a model based on vessel injury. Our results demonstrate that aegyptin is an effective antithrombotic agent in vivo and might be regard as an important tool to dissect the hemostatic role of collagen in vivo." @default.
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- W3176146123 date "2011-04-01" @default.
- W3176146123 modified "2023-10-16" @default.
- W3176146123 title "Molecular mechanisms involved in the antithrombotic activity of aegyptin, a novel mosquito‐derived collagen‐binding protein" @default.
- W3176146123 doi "https://doi.org/10.1096/fasebj.25.1_supplement.928.8" @default.
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