Binding of coagulation factors IX and X to the endothelial cell surface.
Bovine coagulation factors IX and X bind to independent sites on bovine aortic endothelial cells. Binding studies with cells maintained serum-free showed that there are at least two classes of binding sites for factor IX and factor X with a dissociation constant of 4.9 x 10(-9) M and 2.1 x 10(-8) M for the respective high affinity sites. Ca+2 was required for specific binding and was reversed by addition of EDTA or EGTA. Competition experiments showed that factor IX and factor IXa bind to the same sites, which are different from the factor X binding sites. Neither binding of factor IX or factor X is inhibited by addition of prothrombin or protein C. Indirect immunofluorescence of factor IX indicated that binding was diffuse on the cell surface.
D000818:Animals; D001011:Aorta / Q000378:metabolism*; D001667:Binding, Competitive; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D004533:Egtazic Acid / Q000494:pharmacology; D004727:Endothelium / Q000187:drug effects / Q000378:metabolism; D005164:Factor IX / Q000378:metabolism*; D005170:Factor X / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D013499:Surface Properties
D004533:Egtazic Acid; D005164:Factor IX; D005170:Factor X; D004492:Edetic Acid; D002118:Calcium