Platelet adhesion to cyanogen-bromide fragments of collagen alpha 1(I) under flow conditions.
作者： EU Saelman , LF Horton , MJ Barnes , HR Gralnick , KM Hese
DOI: 10.1182/BLOOD.V82.10.3029.3029
关键词: Molecular biology 、 Microgram 、 Alpha (ethology) 、 Adhesion 、 Platelet 、 Chemistry 、 Antibody 、 Biochemistry 、 Cyanogen bromide 、 Monoclonal antibody 、 Von Willebrand factor
摘要: The aim of this investigation was to identify domains collagen type I that can support platelet adhesion under flow conditions. Four cyanogen bromide (CB) fragments composing 87% the alpha 1(I)-chain were studied static and Under conditions, bovine human fragment 1(I)CB3 induced aggregate formation, whereas 1(I)CB7 1(I)CB8 supported dendritic contact platelets. Bovine 1(I)CB6 weakly adhesion. At shear rate 300/s, strongly adhesion, lower observed 1(I)CB8. did not Adhesion completely inhibited by a low concentration (0.6 IgG microgram/mL) anti-GPIa monoclonal antibody (MoAb), partially higher concentrations (3 micrograms/mL) anti-glycoprotein Ia (GPIa) further reduced 1(I)CB7. Platelet 1(I)CB3, 1(I)CB7, an anti-GPIb MoAb. A MoAb against GPIb-binding site von Willebrand factor (vWF) 1(I)CB8, inhibited. We conclude conditions GPIa/IIa-dependent GPIb-vWF interaction is important for probably also 1(I)CB3.
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