Arachidonic acid mobilization in P388D1 macrophages is controlled by two distinct Ca(2+)-dependent phospholipase A2 enzymes

Macrophage-like P388D1 cells mobilize arachidonic acid (AA) and produce prostaglandin E2 upon stimulation with bacterial lipopolysaccharide and platelet-activating factor. We have now demonstrated that AA mobilization in these cells is composed of two distinct events: a transient phase in which AA a...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-11, Vol.91 (23), p.11060-11064
Main Authors: Balsinde, J, Barbour, S E, Bianco, I D, Dennis, E A
Format: Article
Language:English
Subjects:
Animals
Arachidonic Acid - metabolism
Base Sequence
Cell Line
Dinoprostone - biosynthesis
DNA Primers - chemistry
DNA, Antisense - chemistry
Gene Expression
Macrophages - metabolism
Membrane Lipids - metabolism
Mice
Molecular Sequence Data
Phospholipases A - metabolism
Phospholipases A2
Phospholipids - metabolism
Platelet Activating Factor - pharmacology
RNA, Messenger - genetics
Time Factors
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Summary:Macrophage-like P388D1 cells mobilize arachidonic acid (AA) and produce prostaglandin E2 upon stimulation with bacterial lipopolysaccharide and platelet-activating factor. We have now demonstrated that AA mobilization in these cells is composed of two distinct events: a transient phase in which AA accumulates in the cell and a sustained phase in which the fatty acid accumulates in the incubation medium. Both phases are markedly dependent on the presence of Ca2+ in the extracellular medium. Treatment with an antisense oligonucleotide to group II phospholipase A2 inhibits the accumulation of AA in the incubation medium, but has no effect on the accumulation of this fatty acid in the cell. In addition, treatment with antisense oligonucleotide to group II phospholipase A2 has no effect on the uptake or the esterification of AA. Collectively, these results indicate that, in addition to the previously demonstrated role of group II phospholipase A2 in AA mobilization in activated P388D1 cells, another phospholipase A2, distinct from the group II enzyme, is implicated in raising the levels of intracellular AA during the early steps of P388D1 cell activation and in modulating deacylation/reacylation reactions involving AA. The data suggest that each of the different phospholipase A2 enzymes present in P388D1 cells serves a distinct role in cell function.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.23.11060