Synergistic effects of lectins in the interaction of thrombin with human platelets.
Several lectins have been studied for their effects on the interaction of thrombin with human platelets. Wheat germ agglutinin, concanavalin A and Ricinus communis lectin increased the number of high affinity sites for diisopropylphosphothrombin on washed platelets from 3000 to about 12 000 but the binding affinities were unchanged (Kd approx 4 nM). Two other lectins, Lens culinaris and Bandieria simplicifolia, were without effect. (2) Using formalinized platelets to avoid possible complications of the platelet release reaction, wheat germ agglutinin showed a marked increase (5-fold) in the binding of active thrombin, peanut agglutinin had no effect while Ricinus communis and :Bandieria simplicifolia showed marginal increases (2-fold). Thrombin binding was decreased to about one quarter with Lens culinaris, Phaseolus vulgaris and concanavalin A. (3) Wheat germ agglutinin caused a synergistic increase of platelet aggregation at low concentrations of thrombin (12.5 mU/ml) and ADP (1 microM), both in the absence and presence of added fibrinogen, but had no effect on ristocetin-induced aggregation.
D001665:Binding Sites; D001792:Blood Platelets / Q000378:metabolism; D005340:Fibrinogen; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D010974:Platelet Aggregation / Q000187:drug effects*; D013917:Thrombin / Q000378:metabolism*; D014909:Wheat Germ Agglutinins
D037102:Lectins; D014909:Wheat Germ Agglutinins; D005340:Fibrinogen; D013917:Thrombin