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Incorporation of arachidonic acid (AA) into phosphatidylcholine molecular species of the human neutrophil (PMN)

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7246126
Recently the authors proposed that the initial incorporation of AA into 1,2 diacylphosphatidylcholine (PC) was mediated by AA-CoA transferase(s) while the subsequent transfer of AA from 1,2-diacyl- into alkyl, acyl-PC was mediated by a CoA-independent transacylase. Studies here provide further evidence for such a two-step mechanism. PMNs were pulse labeled for 5 min with /sup 3/H-AA (.07..mu..M) which was rapidly incorporated into 1,2-diacyl-PC. However, incorporation of AA into 1,2-diacyl-PC was inhibited by incubation with high levels of AA (30 ..mu..M). Similarly PMNs were pulsed labeled with /sup 3/H-AA for 5 min followed by a 120 min incubation. In these cells, /sup 3/H-AA was rapidly transferred from 1,2-diacyl-PC into alkyl, acyl-PC. In the presence of 30 ..mu..M AA redistribution of /sup 3/H-AA from diacyl to alkyl, acyl-PC was observed. This result implied that the initial incorporation of /sup 3/H-AA proceeds via a free acid intermediate while the transfer of /sup 3/H-AA from diacyl to alkyl, acyl-PC does not. Using a cell free system, /sup 14/C-AACoA was incubated for 5 min and found to be incorporated into 1,2-diacyl-PC containing 16:0, 18:0, and 18:1 at the sn-1 position. Furthermore /sup 14/C-AACoA and various 1-radyl, 2-lyso-PC were added to a PMN membrane preparation. The arachidonyl-transferase(s) preferred the 1-acyl, 2-lyso-PC substrate to 1-alkyl, 2-lyso-PC. Thus these studies provide further evidence that AA is initially incorporated into 1,2-diacyl-PC through arachidonyl-CoA transferases.
Research Organization:
Univ. of Colorado Medical School, Denver
OSTI ID:
7246126
Report Number(s):
CONF-8606151-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:6
Country of Publication:
United States
Language:
English