High-affinity binding of forskolin to rat brain membranes

Adv Cyclic Nucleotide Protein Phosphorylation Res. 1985:19:125-35.

Abstract

High-affinity forskolin binding sites in brain membranes have been identified that have structure-activity characteristics compatible with forskolin's site of action at the adenylate cyclase enzyme. It is proposed that these high-affinity binding sites are associated with an activated complex of the catalytic protein and the alpha s subunit. Quantitation of high-affinity forskolin binding sites may provide a direct measure of the amount of adenylate cyclase that has the potential to be regulated by stimulatory hormones and the Ns subunit.

MeSH terms

  • Adenylyl Cyclases / metabolism*
  • Animals
  • Brain / metabolism*
  • Cations, Divalent / pharmacology
  • Colforsin
  • Diterpenes / metabolism*
  • Edetic Acid / pharmacology
  • Enzyme Activation
  • Fluorides / pharmacology
  • GTP-Binding Proteins / metabolism
  • Guanylyl Imidodiphosphate / pharmacology
  • Kinetics
  • Protein Binding / drug effects
  • Rats
  • Structure-Activity Relationship
  • Synaptosomes / metabolism
  • Temperature

Substances

  • Cations, Divalent
  • Diterpenes
  • Colforsin
  • Guanylyl Imidodiphosphate
  • Edetic Acid
  • GTP-Binding Proteins
  • Adenylyl Cyclases
  • Fluorides