Short-term inhibition of carnitine palmitoyltransferase I activity in rat hepatocytes incubated with ethanol.
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.
Guzmán
M
M
Department of Biochemistry, Faculty of Chemistry, Complutense University, Madrid, Spain.
Geelen
M J
MJ
D000079:Acetaldehyde / Q000494:pharmacology; D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000037:antagonists & inhibitors*; D000431:Ethanol / Q000494:pharmacology*; D000077604:Fomepizole; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D008297:Male; D008316:Malonyl Coenzyme A / Q000378:metabolism; D011720:Pyrazoles / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D011720:Pyrazoles; D000431:Ethanol; D008316:Malonyl Coenzyme A; D000077604:Fomepizole; D000217:Acyltransferases; D002334:Carnitine O-Palmitoyltransferase; D000079:Acetaldehyde