The effect of cyclic AMP-dependent protein kinase on the formation of polyphosphoinositides in erythrocyte membranes.
Inside-out vesicles from erythrocyte membrane were phosphorylated in the presence of gamma-32P-ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase increased the 32P-labelling of membrane proteins and polyphosphoinositides in some red blood cell membrane preparations [RBC membrane, type I] while in the majority of membrane preparations the effect of the exogeneous catalytic subunit was insignificant [RBC membrane, type II]. The phosphorylation of type II RBC membrane preparations seemed to be stimulated by the catalytic subunit of endogeneous protein kinase, since the 32P-incorporation into polyphosphoinositides and proteins was decreased by the specific heat stable inhibitor protein of the protein kinase.
D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols / Q000096:biosynthesis / Q000097:blood*; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases / Q000097:blood*
D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases