Ethanol has no effect on cAMP-dependent protein kinase-, protein kinase C-, or Ca(2+)-calmodulin-dependent protein kinase II-stimulated phosphorylation of highly purified substrates in vitro

Alcohol Clin Exp Res. 1991 Dec;15(6):1040-4. doi: 10.1111/j.1530-0277.1991.tb05208.x.


The actions of ethanol on kinase stimulated phosphorylation were examined using highly purified protein kinases and a variety of purified substrates. Ethanol (25-200 mM) failed to alter the phosphorylation of histone IIa and histone IIIs by cAMP-dependent protein kinase (PKA) and protein kinase C (PKC), respectively. Moreover, ethanol (25-200 mM) did not affect the phosphorylation of synapsin I by Ca(2+)-calmodulin-dependent protein kinase II (CAM kinase II). Finally, neither PKA nor PKC stimulated phosphorylation of the GABAA receptor (GABAA-R) was modulated by ethanol at any concentration of ethanol tested. These results suggest that ethanol, in pharmacological concentrations, has no direct actions on the ability of these kinases to catalyze the phosphorylation of specific substrate proteins. In particular, ethanol does not appear to directly influence GABAA-R phosphorylation by either PKA or PKC.

Publication types

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

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cattle
  • Dose-Response Relationship, Drug
  • Ethanol / pharmacology*
  • Phosphorylation
  • Protein Kinase C / physiology*
  • Protein Kinases / physiology*
  • Receptors, GABA-A / drug effects
  • Receptors, GABA-A / physiology
  • Synapsins / physiology


  • Receptors, GABA-A
  • Synapsins
  • Ethanol
  • Protein Kinases
  • Protein Kinase C
  • Calcium-Calmodulin-Dependent Protein Kinases