Background: The mechanism for rapid biosynthesis of platelet-activating factor (PAF), a potent proinflammatory lipid mediator, is unclear. Results: Phosphorylation of lysophosphatidylcholine acyltransferase 2 (LPCAT2) at Ser-34 via PKCα enhanced rapid PAF biosynthesis following PAF or ATP stimulation. Conclusion: The molecular basis for rapid PAF biosynthesis in response to inflammatory stimuli is elucidated. Significance: These data suggest a better understanding of PAF production in early-phase inflammation. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Morimoto, R., Shindou, H., Tarui, M., & Shimizu, T. (2014). Rapid production of platelet-activating factor is induced by protein kinase Cα-mediated phosphorylation of lysophosphatidylcholine acyltransferase 2 protein. Journal of Biological Chemistry, 289(22), 15566–15576. https://doi.org/10.1074/jbc.M114.558874
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