Regulation of adenylyl cyclase isoforms by N-alkanols

J Cell Biochem. 1997 Sep 15;66(4):450-6. doi: 10.1002/(sici)1097-4644(19970915)66:4<450::aid-jcb4>3.0.co;2-k.

Abstract

We examined the effect of n-alkanols on adenylyl cyclase isoforms (types II and V) overexpressed in insect cells. Ethanol stimulated the type II isoform but not the type V isoform. Ethanol stimulated type II adenylyl cyclase greater than GTP gamma S, and the treatment of the membrane with GDP beta S or cholera toxin did not affect this stimulation. Other n-alkanols inhibited type V adenylyl cyclase activity in proportion to their lipophilic potency. In contrast, type II adenylyl cyclase was stimulated by weakly lipophilic n-alkanols and inhibited by strongly lipophilic n-alkanols. When solubilized membranes and purified preparations were used, all the n-alkanols inhibited type II adenylyl cyclase. Our data suggest that n-alkanols regulated adenylyl cyclase isoform-dependently. Stimulation of the type II isoform was independent from the interaction with Gs alpha but required the presence of an intact membrane structure. Our study may provide another step to understanding how membrane protein subtypes are differentially regulated by n-alkanols.

Publication types

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

MeSH terms

  • Adenylyl Cyclase Inhibitors
  • Adenylyl Cyclases / drug effects*
  • Adenylyl Cyclases / metabolism
  • Alcohols / pharmacology*
  • Animals
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Detergents / pharmacology
  • Ethanol / pharmacology
  • GTP-Binding Protein alpha Subunits, Gs / drug effects
  • GTP-Binding Protein alpha Subunits, Gs / metabolism
  • Insecta
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / drug effects*
  • Isoenzymes / metabolism

Substances

  • Adenylyl Cyclase Inhibitors
  • Alcohols
  • Detergents
  • Isoenzymes
  • Ethanol
  • GTP-Binding Protein alpha Subunits, Gs
  • Adenylyl Cyclases