| Abstract: | Using the intracellular Ca2+-specific indicator, Quin 2, it was demonstrated that an addition to platelet suspensions of the GTP-binding protein activator, sodium fluoride, stimulates the Ca2+ and Ba2+ influx from the incubation medium into the cytoplasm via receptor-operated Ca2+ channels (Ca-ROC). The fluoride-induced Ca2+ influx is blocked by the protein kinase C activator, phorbol myristate acetate as well as by the platelet adenylate cyclase activator, prostaglandin E1. A two-dimensional electrophoretic analysis of platelet phosphoproteins revealed that the phorbol ester enhances the phosphorylation of proteins with molecular masses of about 20 and 40 kDa. The experimental results suggest that the participation of the GTP-binding protein in the receptor coupling to Ca-ROC. The mechanism of the blocking effect of phorbol esters and prostaglandin E1 on Ca-ROC consists in an impaired coupling of these channels to the GTP-binding protein that activates them. |
