Enkephalin-mediated inhibition of forskolin-stimulated rabbit luteal adenylyl cyclase activity

Biochem Biophys Res Commun. 1983 Oct 31;116(2):574-80. doi: 10.1016/0006-291x(83)90562-4.

Abstract

Forskolin at 25-100 microM elicited 10- to 15-fold stimulation of rabbit luteal adenylyl cyclase activity in the absence of guanine nucleotides. Addition of saturating concentrations of GTP or guanyl-5'-yl imidodiphosphate [GMP-P(NH)P] inhibited forskolin stimulation by 15-25% and 35-45%, respectively, in Na+-free media. The further addition of 8 microM [D-Ala2, Met5] enkephalin amide (Da-ENK) caused an additional 16-24% inhibition of activity in the presence of GTP plus forskolin, but did not alter enzymatic activity in the presence of forskolin alone or forskolin plus GMP-P(NH)P. Inhibition by guanine nucleotide alone or Da-ENK plus GTP was only observed in the presence of forskolin. Maximal inhibition by Da-ENK was observed at 25 microM forskolin. Da-ENK reduced the IC50 for GTP by 2.3-fold but did not alter the IC50 for GMP-P(NH)P. Addition of Na+ above 3 mM attenuated the inhibitory responses to GTP and GTP plus Da-ENK, but not to GMP-P(NH)P or GMP-P(NH)P plus Da-ENK. Above 100 mM, Na+ inhibited enzymatic activity in the presence of forskolin, forskolin plus GTP and forskolin plus GMP-P(NH)P in the absence and presence of Da-ENK. These findings suggest that the rabbit corpus luteum contains an inhibitory receptor for opiate peptides that couples to adenylyl cyclase.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / metabolism*
  • Animals
  • Colforsin
  • Corpus Luteum / drug effects
  • Corpus Luteum / enzymology*
  • Diterpenes / pharmacology*
  • Enkephalin, Methionine / analogs & derivatives*
  • Enkephalin, Methionine / pharmacology
  • Female
  • Guanosine Triphosphate / pharmacology
  • Guanylyl Imidodiphosphate / pharmacology
  • Rabbits

Substances

  • Diterpenes
  • Colforsin
  • Guanylyl Imidodiphosphate
  • Enkephalin, Methionine
  • enkephalinamide-Met, Ala(2)-
  • Guanosine Triphosphate
  • Adenylyl Cyclases