Peroxisomal fatty acyl-CoA oxidase is not regulated by triiodothyronine.
In studies using primary cultures of adult rat hepatocytes in serum-free medium, peroxisomal fatty acyl-CoA oxidase activity was not altered by the presence of 3,5,3'-triiodothyronine, whereas time- and dose-dependent increases in the thyroid hormone-responsive enzyme mitochondrial glycero-3-phosphate dehydrogenase were seen. Activity of peroxisomal oxidase was stimulated with clofibric acid in the absence of 3,5,3'-triiodothyronine. The results demonstrate that hepatic peroxisomal fatty acyl-CoA oxidase activity is not directly regulated by 3,5,3'-triiodothyronine and that stimulation of peroxisomal fatty acyl-CoA oxidase activity by clofibric acid does not require thyroid hormone.
Shoemaker
R L
RL
Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201.
Yamazaki
R K
RK
D042962:Acyl-CoA Oxidase; D000818:Animals; D002237:Carbohydrate Dehydrogenases / Q000378:metabolism; D002478:Cells, Cultured; D002995:Clofibric Acid / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D008297:Male; D008830:Microbodies / Q000187:drug effects / Q000201:enzymology*; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats; D011916:Rats, Inbred F344; D014284:Triiodothyronine / Q000494:pharmacology*
D014284:Triiodothyronine; D002995:Clofibric Acid; D010088:Oxidoreductases; D002237:Carbohydrate Dehydrogenases; C056470:3-glycerophosphate dehydrogenase; D042962:Acyl-CoA Oxidase