Subcellular localisation and induction of NADH-sensitive acetyl-CoA hydrolase and propionyl-CoA hydrolase activities in rat liver under lipogenic conditions after treatment with sulfur-substituted fatty acids.
The effects of sulfur-substituted fatty acid analogues on the subcellular distribution and activities of acetyl-CoA and propionyl-CoA hydrolases in rats fed a high carbohydrate diet were studied. Among subcellular fractions of liver homogenates from rats fed a high carbohydrate diet (20%), the acetyl-CoA and propionyl-CoA hydrolase activities are found in the mitochondrial, peroxisome-enriched and cytosolic fractions. We have shown that the subcellular distribution of acetyl-CoA hydrolase appears to be different from the distribution propionyl-CoA hydrolase activity. Thus, the highest specific activity of acetyl-CoA hydrolase was found in the mitochondrial fraction, whereas the highest specific activity of propionyl-CoA hydrolase was found in the peroxisome-enriched fraction. Rats treated with sulfur-substituted fatty acids, i.e., 3-thiadicarboxylic acid (400 mg/day per kg body weight), showed a significant increase in acetyl-CoA hydrolase activity where the peroxisomal and cytosolic hydrolases were increased 3.9- and 2.7-fold, respectively, compared to palmitic acid treated rats. Similar results were obtained with tetradecylthioacetic acid treated rats. Propionyl-CoA hydrolase activities, in rats treated with these two peroxisome proliferating fatty acid analogues showed increased activity mainly in the mitochondrial and the cytosolic subcellular fractions. Acetyl-CoA hydrolase activity was sensitive to NADH, whereas no stimulation of the propionyl-CoA hydrolase activity was observed in the presence of NADH. The hepatic amounts of acetyl-CoA, propionyl-CoA, and free CoASH were elevated after sulfur-substituted fatty acid treatment. Sulfur-substituted fatty acids also elevated the specific acetyl-CoA hydrolase activity in the mitochondrial fraction and the propionyl-CoA hydrolase activity in the light-mitochondrial fraction. These results, therefore, suggest that acetyl-CoA hydrolase and propionyl-CoA hydrolase are two distinct proteins and that these two enzymes have a multiorganelle localisation.
Garras
A
A
University of Bergen, Department of Clinical Biology, Haukeland Hospital, Norway.
Asiedu
D K
DK
Berge
R K
RK
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000104:Acetyl-CoA Hydrolase / Q000378:metabolism*; D000214:Acyl Coenzyme A / Q000378:metabolism; D000818:Animals; D003065:Coenzyme A / Q000378:metabolism; D003998:Dicarboxylic Acids / Q000494:pharmacology*; D004040:Dietary Carbohydrates / Q000378:metabolism*; D004790:Enzyme Induction / Q000187:drug effects; D008055:Lipids / Q000096:biosynthesis; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D009243:NAD / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013347:Subcellular Fractions / Q000201:enzymology; D013440:Sulfides / Q000494:pharmacology*; D013869:Thiolester Hydrolases / Q000378:metabolism*
D000214:Acyl Coenzyme A; D003998:Dicarboxylic Acids; D004040:Dietary Carbohydrates; D008055:Lipids; D013440:Sulfides; D009243:NAD; C009061:propionyl-coenzyme A; C062079:1,10-bis(carboxymethylthiodecane); D000105:Acetyl Coenzyme A; C062078:1-(carboxymethylthio)tetradecane; D013869:Thiolester Hydrolases; C061158:propionyl CoA hydrolase; D000104:Acetyl-CoA Hydrolase; D003065:Coenzyme A