Selectivities of 1-acylglycerophosphorylcholine acyltransferase and acyl-CoA synthetase for n-3 polyunsaturated fatty acids in platelets and liver microsomes

Biochim Biophys Acta. 1984 May 11;793(3):416-22.

Abstract

1- Acylglycerophosphorylcholine acyltransferase in platelets and liver microsomes showed a selectivity for polyunsaturated fatty acids. The acyl-donor specificity of the enzyme for 1- acylglycerophosphorylcholine and also 1- acylglycerophosphorylethanolamine was high for n-3 eicosapentaenoyl -CoA and docosahexaenoyl -CoA, and highest for arachidonyl-CoA. Further, the enzyme activity was higher for n-6 eicosatrienoyl -CoA than for n-3 and n-9 eicosatrienoyl -CoAs. It appears that the acyltransferase has a predominant selectivity for n-6 series, but the selectivity is not limited to this series. Acyl-CoA synthetase of liver microsomes and platelets also exhibited a high selectivity for n-3 polyunsaturated fatty acids as well as n-6. In platelets, the acyl-CoA synthetase activity preferential to polyunsaturated fatty acids (n-3 and n-6) was found by competitive aspects of incorporation, in addition to the activity preferential to palmitic acid. In any case, it is suggested that n-3 polyunsaturated fatty acids are easily incorporated into platelet and liver phospholipids.

MeSH terms

  • 1-Acylglycerophosphocholine O-Acyltransferase
  • Acyltransferases / metabolism*
  • Animals
  • Blood Platelets / enzymology*
  • Coenzyme A Ligases / metabolism*
  • Fatty Acids, Unsaturated / metabolism*
  • Kinetics
  • Liver / enzymology*
  • Male
  • Microsomes / enzymology
  • Rats
  • Substrate Specificity

Substances

  • Fatty Acids, Unsaturated
  • Acyltransferases
  • 1-Acylglycerophosphocholine O-Acyltransferase
  • Coenzyme A Ligases