Carnitine acetyltransferase is not a cytosolic enzyme in rat heart and therefore cannot function in the energy-linked regulation of cardiac fatty acid oxidation.
The subcellular location of cardiac carnitine acetyltransferase (CAT) was investigated by measuring the release of carnitine acetyltransferase and of marker enzymes from isolated rat myocytes permeabilized with digitonin. Additionally, the carnitine acetyltransferase activity exposed to the cytosolic compartment was quantified. The results indicate that soluble acetyl transferase is not present in the cytosol, and that only 5% of the cellular carnitine acetyltransferase activity is positioned to catalyse the formation of cytosolic acetyl coenzyme A. This situation makes it unlikely that the energy-linked regulation of cardiac fatty acid oxidation proceeds by mechanisms which require the conversion of acetylcarnitine to acetyl coenzyme A in the cytosol.
Abbas
A S
AS
Department of Chemistry, City College of the City University of New York, NY 10031, USA.
Wu
G
G
Schulz
H
H
D000818:Animals; D002332:Carnitine O-Acetyltransferase / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology*; D005227:Fatty Acids / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology*; D010084:Oxidation-Reduction; D051381:Rats; D017207:Rats, Sprague-Dawley
D005227:Fatty Acids; D002332:Carnitine O-Acetyltransferase