The Relationship Between the Levels of Long-Chain Acyl-CoA and Clofibryl-CoA and the Induction of Peroxisomal β-Oxidation

Abstract

Peroxisomal β-oxidation and palmitoyl-CoA hydrolase activity was induced by a number of non-physiological substanes, all of which were hypolipidaemic. In our experiments, niadenate and tiadenol were considerably more potent than clofibrate in inducing enlargement of the liver, lipid metabolizing enzymes and CoA derivatives associated with the peroxisomes and other subcellular organelles1. The findings were qualitatively similar, however, with all drugs. High-fat diets lead to induction of peroxisomal p-oxidation and palmitoyl-CoA hydrolase2. Starvation and diabetes have the same effect3 4 5. Positive correlations have been observed between the activities of peroxisomal β-oxidation and palmitoyl-CoA hydrolase and the cellular levels of long-chain acyl-CoA both by hypolipidemic drug and high-fat diets. Thus, a common regulation mechanism for these two enzyme systems is reasonable i.e. long-chain acyl-CoA, which is the substrate for both the palmitoyl-CoA hydrolase and peroxisomal (β-oxidation, may regulate the enzyme systems by a substrate-induced mechanism.