Characterization of the unique mechanism mediating the shear-dependent binding of soluble von Willebrand factor to platelets.
作者： Shinya Goto , Daniel R. Salomon , Yasuo Ikeda , Zaverio M. Ruggeri
关键词: Ristocetin 、 Platelet 、 Fluorescein isothiocyanate 、 Von Willebrand factor 、 Chemistry 、 Biophysics 、 Ligand (biochemistry) 、 Stereochemistry 、 Platelet membrane glycoprotein 、 Fluorescence 、 Glycoprotein Ib-IX-V Receptor Complex
摘要: We have studied the mechanism of interaction between soluble von Willebrand factor (vWF), labeled with fluorescein isothiocyanate (FITC), and platelets exposed to shear in a cone-and-plate viscometer. A flow cytometer calibrated fluorescent bead standards was used calculate number molecules associated each platelet suspension. To validate methods reagents used, binding same vWF assessed presence ristocetin or α-thrombin found be saturable, narrow symmetric distribution on >90% platelets. As expected, essentially all bound ligand interacted exclusively membrane glycoprotein (GP) Ibα GP IIb-IIIa after stimulation α-thrombin. In contrast, only minor proportion (
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