PMID: 3762329Sep 1, 1986Paper

Rat hepatocyte plasma membrane acyl:CoA synthetase activity

Lipids
B C Davidson, R C Cantrill

Abstract

The presence of long chain acyl:CoA synthetases in mammalian microsomes and mitochondria has been established previously by Aas (Biochim. Biophys. Acta 231, 32-47 [1971] ). The presence of a plasma membrane-associated enzyme was investigated in rat hepatocyte plasma membranes, where an enzyme exhibiting high activity and with a preferred substrate of 18-carbon chain length was discovered. The results are consistent with the presence of a single enzyme. The effect of the degree of unsaturation of the fatty acid substrates was not as pronounced as that arising from the length of the carbon chain. The pattern of substrate preference of the enzyme was omega 3 polyenoic fatty acids greater omega 6 polyenoic acids greater than omega 9 monoenoic acids greater than saturated acids. This may relate to the similar substrate preference pattern exhibited by the fatty acyl desaturase enzymes. The role played by long chain acyl:CoA synthetase in hepatocyte metabolism is uncertain, but it may relate to the incorporation of polyenoic fatty acids from the circulation into cell membranes and the trapping of other fatty acids within the cell for further metabolism.

References

Jun 14, 1985·Biochimica Et Biophysica Acta·O Morand, M S Aigrot
Nov 25, 1985·FEBS Letters·B C Davidson, R C Cantrill
Jan 1, 1974·Methods in Enzymology·P EmmelotW J van Blitterswijk
Mar 1, 1973·The Biochemical Journal·J Bar-Tana, G Rose
Aug 23, 1973·Biochimica Et Biophysica Acta·P H Groot, W C Hülsmann
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Jul 1, 1960·Journal of Applied Physiology·J R NEVILLE

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Citations

Jan 26, 1995·Molecular and Cellular Biochemistry·A Ves-Losada, R R Brenner
Jan 1, 1996·Progress in Lipid Research·R Lehner, A Kuksis
Jan 1, 1995·Journal of Lipid Mediators and Cell Signalling·A B Momchilova-PankovaK S Koumanov
Mar 1, 1997·Progress in Lipid Research·P A Watkins
Dec 1, 1996·Cell Biochemistry and Function·K de GrooteP E Declercq

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