Short-term inhibition of carnitine palmitoyltransferase I activity in rat hepatocytes incubated with ethanol

Biochem Biophys Res Commun. 1988 Jul 29;154(2):682-7. doi: 10.1016/0006-291x(88)90193-3.

Abstract

Ethanol decreased the activity of carnitine palmitoyltransferase I and the rate of fatty acid oxidation in rat hepatocytes in short-term incubations. These effects were mimicked by acetaldehyde, the product of hepatic ethanol metabolism, and were absent when ethanol oxidation was prevented by 4-methylpyrazole. Ethanol was also able to increase intracellular malonyl-CoA levels. The results suggest that inhibition of fatty acid translocation into mitochondria may play an important role in the ethanol-induced inhibition of hepatic fatty acid oxidation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetaldehyde / pharmacology
  • Acyltransferases / antagonists & inhibitors*
  • Animals
  • Carnitine O-Palmitoyltransferase / antagonists & inhibitors*
  • Ethanol / pharmacology*
  • Fomepizole
  • Liver / drug effects*
  • Liver / enzymology
  • Male
  • Malonyl Coenzyme A / metabolism
  • Pyrazoles / pharmacology
  • Rats
  • Rats, Inbred Strains

Substances

  • Pyrazoles
  • Ethanol
  • Malonyl Coenzyme A
  • Fomepizole
  • Acyltransferases
  • Carnitine O-Palmitoyltransferase
  • Acetaldehyde