Carnitine acyltransferases and acyl-CoA hydrolases in human and rat liver
The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from studies on rats to human metabolism. In human liver, carnitine acetyltransferase activity was 10-14 times higher and carnitine octanoyltransfera...
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Published in | Clinical science (1979) Vol. 73; no. 1; pp. 3 - 10 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
London
Portland Press
01.07.1987
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Subjects | |
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Abstract | The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from studies on rats to human metabolism. In human liver, carnitine acetyltransferase activity was 10-14 times higher and carnitine octanoyltransferase 1.7-2.4 times higher than in rat liver, while carnitine palmitoyltransferase activity was similar in human and rat. Acetyl-CoA hydrolase and octanoyl-CoA hydrolase activities were lower in human (42-57%) than in rat liver, but palmitoyl-CoA hydrolase activity was similar in both species. The activity of citrate synthase was lower (44%) in human than in rat liver. The low citrate synthase activity and the high carnitine acetyltransferase in human liver suggest that in man acetylcarnitine might be more important as a vehicle for export of acetyl units from mitochondria than citrate. The high activity of carnitine acetyltransferase in human liver is consistent with the observation that acetylcarnitine is the predominant acylcarnitine excreted in diabetic ketosis in man. It is concluded that the rat may not be a valid model for carnitine metabolism in man, and that in human liver carnitine may have an important role in transfer of acetyl groups out of mitochondria and possibly also to extra-hepatic tissues. |
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AbstractList | The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from studies on rats to human metabolism. In human liver, carnitine acetyltransferase activity was 10-14 times higher and carnitine octanoyltransferase 1.7-2.4 times higher than in rat liver, while carnitine palmitoyltransferase activity was similar in human and rat. Acetyl-CoA hydrolase and octanoyl-CoA hydrolase activities were lower in human (42-57%) than in rat liver, but palmitoyl-CoA hydrolase activity was similar in both species. The activity of citrate synthase was lower (44%) in human than in rat liver. The low citrate synthase activity and the high carnitine acetyltransferase in human liver suggest that in man acetylcarnitine might be more important as a vehicle for export of acetyl units from mitochondria than citrate. The high activity of carnitine acetyltransferase in human liver is consistent with the observation that acetylcarnitine is the predominant acylcarnitine excreted in diabetic ketosis in man. It is concluded that the rat may not be a valid model for carnitine metabolism in man, and that in human liver carnitine may have an important role in transfer of acetyl groups out of mitochondria and possibly also to extra-hepatic tissues. 1. The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from studies on rats to human metabolism. 2. In human liver, carnitine acetyltransferase activity was 10–14 times higher and carnitine octanoyltransferase 1.7–2.4 times higher than in rat liver, while carnitine palmitoyltransferase activity was similar in human and rat. 3. Acetyl-CoA hydrolase and octanoyl-CoA hydrolase activities were lower in human (42–57%) than in rat liver, but palmitoyl-CoA hydrolase activity was similar in both species. 4. The activity of citrate synthase was lower (44%) in human than in rat liver. The low citrate synthase activity and the high carnitine acetyltransferase in human liver suggest that in man acetylcarnitine might be more important as a vehicle for export of acetyl units from mitochondria than citrate. 5. The high activity of carnitine acetyltransferase in human liver is consistent with the observation that acetylcarnitine is the predominant acylcarnitine excreted in diabetic ketosis in man. 6. It is concluded that the rat may not be a valid model for carnitine metabolism in man, and that in human liver carnitine may have an important role in transfer of acetyl groups out of mitochondria and possibly also to extrahepatic tissues. |
Author | WRIGHT, P. D ALBERTI, K. G. M. M AGIUS, L |
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Keywords | Human Vertebrata Mammalia Rat Liver Rodentia Acyltransferase Metabolism Fatty acids Carnitine |
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Snippet | The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from... 1. The activities of carnitine acyltransferases and acyl-CoA hydrolases were determined in human and rat liver to establish the validity of extrapolating from... |
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SubjectTerms | Acyltransferases - metabolism Adult Aged Aged, 80 and over Animals Biological and medical sciences Carnitine Acyltransferases - metabolism Cytosol - enzymology Detergents - pharmacology Female Fundamental and applied biological sciences. Psychology Humans Kinetics Liver - enzymology Liver. Bile. Biliary tracts Male Middle Aged Mitochondria, Liver - enzymology Palmitoyl-CoA Hydrolase - metabolism Polidocanol Polyethylene Glycols - pharmacology Rats - metabolism Rats, Inbred Strains Species Specificity Thiolester Hydrolases - metabolism Vertebrates: digestive system |
Title | Carnitine acyltransferases and acyl-CoA hydrolases in human and rat liver |
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