The inhibitory effect of methanol on forskolin-activated adenylate cyclase in rat erythrocyte membranes dependent on the state of the guanine nucleotide-binding stimulatory and regulatory protein.
Forskolin-activated adenylate cyclase activity in rat erythrocyte membranes was markedly inhibited by methanol in a concentration dependent manner. On the contrary, no change was observed in the basal cyclase activity in the presence of methanol. The methanol inhibition forskolin-activated cyclase activity was protected by the stimulation of Gs in the presence of NaF in a concentration dependent manner. These data indicate that low- and high-affinity binding sites of forskolin in rat erythrocyte membranes have different sensitivities to methanol.
D000067956:Adenylyl Cyclase Inhibitors; D000818:Animals; D005576:Colforsin / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D000432:Methanol / Q000494:pharmacology*; D051381:Rats; D012969:Sodium Fluoride / Q000494:pharmacology
D000067956:Adenylyl Cyclase Inhibitors; D005576:Colforsin; D012969:Sodium Fluoride; D019204:GTP-Binding Proteins; D000432:Methanol