作者: S. G. MAGWENZI , R. A. AJJAN , K. F. STANDEVEN , L. A. PARAPIA , K. M. NASEEM
DOI: 10.1111/J.1538-7836.2011.04234.X
关键词:
摘要: Summary. Background: Activated coagulation factor XIII (FXIIIa) is a transglutaminase that crosslinks fibrin at sites of vascular injury. FXIIIa also associates with blood platelets, although its role in platelet function unclear and requires clarification. Objectives: To evaluate the ability to support adhesion spreading under conditions physiologic flow, identify underpinning receptors signaling events. Methods Results: Platelet immobilized was measured by fluorescence microscopy, events were characterized immunoblotting. Immobilized supported static through mechanisms dually differentially dependent on integrins αIIbβ3 αvβ3. Platelet independent or protein disulfide isomerase activity. Moreover, abolished antibodies prevented interaction FXIIIa, but maintained when potential interactions fibrinogen blocked. reduced significantly either specific antagonist tirofiban selective αvβ3-blocking antibody LM609, they used combination. Importantly, preserved venous arterial flow which both played essential roles. In contrast, stimulated formation filopodia lamellipodia adherent platelets mediated exclusively eliminated Src-family inhibitor 4-amino-5-(4-methylphenyl-7-(t-butyl)pyrazolo(3,4-d)pyrimidine, indicating tyrosine kinase-dependent mechanism. Crucially, shear, accentuated recruitment von Willebrand factor collagen. Conclusions: Our data demonstrate for supporting damage, particularly association other thrombogenic matrix proteins.