Polybrene-induced platelet agglutination and reduction in electrophoretic mobility: enhancement by von Willebrand factor and inhibition by vancomycin

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Polybrene-induced platelet agglutination and reduction in electrophoretic mobility: enhancement by von Willebrand factor and inhibition by vancomycin.

It has recently been reported that the polycation Polybrene (hexadimethrine bromide), like ristocetin, agglutinates platelets more extensively in the presence of normal plasma than von Willebrand plasma. Since we have previously proposed that ristocetin may initiate agglutination by reducing platelet surface charge, I investigated the correlation between Polybrene's ability to induce agglutinat...

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Platelet-collagen interaction: inhibition by ristocetin and enhancement by von Willebrand factor-platelet binding.

The contribution of von Willebrand factor (vWF)-platelet binding to platelet-collagen interaction was examined in vitro. The binding of vWF to platelets was mediated and regulated by ristocetin. Subthreshold concentrations of ristocetin (less than or equal to 1 mg/mL), insufficient to cause ristocetin-induced platelet aggregation (RIPA), were added to platelet-rich plasma (PRP) prior to the add...

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Inhibition of ristocetin-induced platelet agglutination by vancomycin.

Ristocetin and vancomycin are structurally similar glycopeptide antibiotics. Both vancomycin and ristocetin in high concentrations (3.0 mg/ml) cause the precipitation of fibrinogen, plasminogen, and IgG from platelet-poor plasma (PPP). In contrast to ristocetin, vanomycin (0.5-1.5 mg/ml) does not agglutinate platelets in normal platelet-rich plasma (PRP) or formalin-treated platelets in the pre...

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The effects of ristocetin and von Willebrand factor on platelet electrophoretic mobility.

Ristocetin will induce the agglutination of platelets in the presence of von Willebrand factor. In previous studies, an electrostatic mechanism was proposed for this phenomenon wherein first the platelet's surface charge is reduced by the binding of ristocetin and then the von Willebrand factor acts as a bridge between platelets. To test this hypothesis, the effects of ristocetin and von Willeb...

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Inhibition of platelet adhesion to fibronectin, fibrinogen, and von Willebrand factor substrates by complex gangliosides.

Gangliosides, which are complex glycosphingolipids containing sialic acid, are found in cell membranes and have been implicated in a variety of cell surface events including cellular adhesion. Complex gangliosides were observed to inhibit the adhesion of thrombin-activated platelets to substrates of fibronectin, von Willebrand factor, and fibrinogen. This adhesion, which is mediated by the glyc...

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ژورنال

عنوان ژورنال: Blood

سال: 1980

ISSN: 0006-4971,1528-0020

DOI: 10.1182/blood.v55.2.276.276