Differential regulation of calmodulin-dependent and -independent cyclic AMP phosphodiesterases from oviduct by fatty acids

Biochem Biophys Res Commun. 1991 May 31;177(1):324-9. doi: 10.1016/0006-291x(91)91986-m.

Abstract

Regulation of calmodulin-independent and -dependent cAMP phosphodiesterases from quail oviduct by various fatty acids was studied. The calmodulin-independent form was slightly activated by low concentrations (20 microM) of oleic, linoleic and arachidonic acid, higher concentrations were inhibitory. The basal activity of the calmodulin-dependent form was activated by linoleic acid and to a lesser extent by arachidonic acid at low concentrations and inhibited by higher concentrations of the two fatty acids. In contrast, arachidonic acid was a potent reversible inhibitor of calmodulin in the activation of this enzyme (IC50: 20 microM) whereas linoleic acid was inactive from 10 to 150 microM. The present results strongly suggest that the differential regulation of cAMP phosphodiesterases by these fatty acids could profoundly influence the level of cAMP in the oviduct and thus its subsequent effects.

Publication types

  • Comparative Study

MeSH terms

  • 3',5'-Cyclic-AMP Phosphodiesterases / metabolism*
  • Animals
  • Arachidonic Acid
  • Arachidonic Acids / pharmacology
  • Calmodulin / pharmacology*
  • Coturnix
  • Cyclic Nucleotide Phosphodiesterases, Type 1
  • Cytosol / enzymology
  • Fatty Acids, Nonesterified / pharmacology*
  • Female
  • Homeostasis
  • Kinetics
  • Linoleic Acid
  • Linoleic Acids / pharmacology
  • Oleic Acid
  • Oleic Acids / pharmacology
  • Oviducts / enzymology*

Substances

  • Arachidonic Acids
  • Calmodulin
  • Fatty Acids, Nonesterified
  • Linoleic Acids
  • Oleic Acids
  • Arachidonic Acid
  • Oleic Acid
  • Linoleic Acid
  • 3',5'-Cyclic-AMP Phosphodiesterases
  • Cyclic Nucleotide Phosphodiesterases, Type 1