Forskolin stabilizes a functionally coupled state between activated guanine nucleotide-binding stimulatory regulatory protein, Ns, and catalytic protein of adenylate cyclase system in rat erythrocytes.
Guanine nucleotide-binding stimulatory regulatory protein of adenylate cyclase system, Ns, in rat erythrocytes was activated by the treatment with guanylyl 5'-imidodiphosphate or NaF-AlCl3 in the presence of Mg2+. The activation was counterbalanced to the basal state either by the removal of Mg2+ or by the addition of beta(gamma)-subunit of N protein of this system. The depression from the activated state was markedly protected by the coexistence of forskolin at the time of the deactivation depending on the dose of forskolin. EC50 of forskolin for the stabilizing effect was much lower than that for the stimulation of adenylate cyclase activity. These data indicate that forskolin has an effect on the interaction between Ns and catalytic unit of adenylate cyclase system in addition to the direct effect on the catalytic unit.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D005576:Colforsin / Q000494:pharmacology*; D004492:Edetic Acid / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006165:Guanylyl Imidodiphosphate / Q000378:metabolism; D046911:Macromolecular Substances; D008274:Magnesium / Q000378:metabolism; D051381:Rats
D046911:Macromolecular Substances; D005576:Colforsin; D006165:Guanylyl Imidodiphosphate; D004492:Edetic Acid; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D008274:Magnesium