Regulation of triacylglycerol synthesis in permeabilized rat hepatocytes. Role of fatty acid concentration and diacylglycerol acyltransferase.
Isolated hepatocytes from fed and starved rats, permeabilized with Staphylococcus aureus alpha-toxin, were incubated with increasing concentrations of radiolabelled fatty acids, in the presence of a saturating concentration of 3-GP. Incorporation of label into LPA, PA and DAG was lower in cells from starved rats than in cells from fed rats, apparently reflecting the lower activity of GPAT after starvation. This enzyme approached saturation at high fatty acid levels and determined the overall flux through the esterification pathway. TAG synthesis, however, was the same in both nutritional states and could not be saturated with fatty acid under the given conditions. Taken together with the observed accumulation of DAG, these data suggest that the rate of TAG synthesis is controlled by the fatty acid supply and, more particularly, by the affinity of DGAT for acyl-CoA.
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Catholic University of Leuven, Faculty of Pharmaceutical Sciences, Laboratory of Clinical Chemistry, Belgium.
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D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002463:Cell Membrane Permeability; D051048:Diacylglycerol O-Acyltransferase; D005227:Fatty Acids / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D010084:Oxidation-Reduction; D051381:Rats; D017208:Rats, Wistar; D013217:Starvation; D014280:Triglycerides / Q000096:biosynthesis*
D005227:Fatty Acids; D014280:Triglycerides; D000217:Acyltransferases; D051048:Diacylglycerol O-Acyltransferase