The regulation of adenylate cyclase activity in turkey erythrocyte membranes by forskolin.
The mechanisms by which forskolin stimulates adenylate cyclase activity in turkey erythrocyte membranes and is influenced by manganese and Gpp(NH)p were studied. Forskolin-dependent adenylate cyclase activity in particulate turkey erythrocyte membranes is enhanced following preincubation of membranes with isoproterenol and GMP (cleared membranes). In contrast, solubilization of turkey erythrocyte membranes, previously cleared, renders them relatively refractory to forskolin but not to Gpp(NH)p. Whereas adenylate cyclase activity due to the simultaneous presence of forskolin and Mn2+ in particulate turkey erythrocyte membranes is additive, their copresence becomes synergistic after solubilization. The apparent Kact for forskolin activation of adenylate cyclase is not influenced by clearance or by the presence of Mn2+ in particulate turkey erythrocyte membranes. Following solubilization, the Vmax for forskolin-dependent adenylate cyclase activation determined in the presence of Mn2+ is also independent of clearance. Forskolin activation of turkey erythrocyte adenylate cyclase appears to be influenced at sites in addition to the catalytic unit.
D000262:Adenylyl Cyclases / Q000097:blood*; D000818:Animals; D005576:Colforsin / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D012995:Solubility; D014422:Turkeys
D005576:Colforsin; D006165:Guanylyl Imidodiphosphate; D008345:Manganese; D000262:Adenylyl Cyclases