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

J Pharmacobiodyn. 1988 May;11(5):377-80. doi: 10.1248/bpb1978.11.377.

Abstract

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.

MeSH terms

  • Adenylyl Cyclase Inhibitors*
  • Animals
  • Colforsin / pharmacology*
  • Erythrocyte Membrane / drug effects
  • Erythrocyte Membrane / enzymology*
  • GTP-Binding Proteins / metabolism*
  • In Vitro Techniques
  • Methanol / pharmacology*
  • Rats
  • Sodium Fluoride / pharmacology

Substances

  • Adenylyl Cyclase Inhibitors
  • Colforsin
  • Sodium Fluoride
  • GTP-Binding Proteins
  • Methanol