Induction of cytosolic clofibroyl-CoA hydrolase activity in liver of rats treated with clofibrate.
Among subcellular fractions of liver homogenates of rats, the clofibroyl-CoA hydrolase activity is found mainly in the cytosolic fraction. It is here shown that the subcellular distribution of clofibroyl-CoA hydrolase appears to be different from the distribution of palmitoyl-CoA hydrolase activity. Thus, in contrast to the case with palmitoyl-CoA, no hydrolysis of clofibroyl-CoA was catalysed by the microsomal fraction. Furthermore, the hydrolysis of palmitoyl-CoA and clofibroyl-CoA in the cytosolic fraction seemed to be catalyzed by two different enzymes. Rats treated with clofibrate (0.3%, w/w) showed a significant increased clofibroyl-CoA hydrolase activity where the cytosolic hydrolase was increased 3.5-fold. Clofibrate administration also elevated the specific clofibroyl-CoA hydrolase activity by factors of 1.7 and 1.5 in the mitochondrial and the light-mitochondrial fractions, respectively. Thus, it is possible that clofibroyl-CoA hydrolase has also a multiorganelle localization.
D000818:Animals; D002994:Clofibrate / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology*; D004790:Enzyme Induction; D006868:Hydrolysis; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure*; D008297:Male; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D051381:Rats; D013869:Thiolester Hydrolases / Q000096:biosynthesis*; D014018:Tissue Distribution
D010171:Palmitoyl Coenzyme A; D007770:L-Lactate Dehydrogenase; D013869:Thiolester Hydrolases; C051748:clofibroyl-CoA hydrolase; D002994:Clofibrate