Plasma membrane signal ATP (psATP) was synthesized in response to the effect insulin (0.4 microgram/ml) in erythrocyte membranes, washed in 0.25 M sucrose and maintained in the mixture containing all the components required for aerobic phosphorylation. Biosynthesis of psATP was completely inhibited by amiloride at a concentration of 2 x 10(-3) M. Ouabain (0.5 x 10(-6) M) inhibited the triphosphate synthesis by 95%. Monensin (0.3 x 10(-6) M) activated ATP formation 2-fold approximately in erythrocyte membranes both stimulated by insulin and free of the hormone effect. Monensin, added into the incubation mixture simultaneously with ouabain, abolished its inhibitory effect on psATP synthesis. In absence of Na+ the psATP biosynthesis was not detected. Protonophore FCCP stimulated the biosynthesis at various concentrations from 10(-7) to 10(-3) M. These data indicated that biosynthesis of psATP is related to Na+/H+ metabolism in plasma membranes of human erythrocytes.
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