Dietary control of the chain elongation of palmityl-CoA in rat liver microsomes.
The rate of chain elongation of palmityl-CoA to stearyl-CoA in rat liver microsomes was studied in connection with the nutritional status of the rats. The microsomal chain elongation activity, which had been decreased by starvation for 48 hr, was rapidly increased to a high level on refeeding. The apparent Km value for malonyl-CoA in both normal and refed rats was the same, 1.2 X 10(4)M. Both cycloheximide and actinomycin D prevented the induction of microsomal chain elongation activity which was associated with refeeding. In addition, the activity of acyl-CoA hydrolase and the rates of esterification of acyl-CoA into phospholipids and neutral lipids in microsomes were not changed by the dietary alteration. These results support the conclusion that changes of the activity of microsomal chain elongation of palmityl-CoA in various nutritional status result from a rapid synthesis of new enzyme(s).
D000818:Animals; D003065:Coenzyme A / Q000378:metabolism*; D003066:Coenzyme A Ligases / Q000378:metabolism; D005260:Female; D008314:Malonates / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology / Q000378:metabolism*; D010169:Palmitic Acids / Q000378:metabolism*; D051381:Rats; D013217:Starvation; D013229:Stearic Acids / Q000378:metabolism*
D008314:Malonates; D010169:Palmitic Acids; D013229:Stearic Acids; D003066:Coenzyme A Ligases; D003065:Coenzyme A