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 inClinical science (1979) Vol. 73; no. 1; pp. 3 - 10
Main Authors AGIUS, L, WRIGHT, P. D, ALBERTI, K. G. M. M
Format Journal Article
LanguageEnglish
Published London Portland Press 01.07.1987
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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.
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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Issue 1
Keywords Human
Vertebrata
Mammalia
Rat
Liver
Rodentia
Acyltransferase
Metabolism
Fatty acids
Carnitine
Language English
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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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StartPage 3
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
URI https://www.ncbi.nlm.nih.gov/pubmed/2886246
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Volume 73
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