Study Of Control Of Cytosolic Phospholipase A2 Activity

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Abstract

The activity of cytosolic phospholipase A2 (cPLA2) may be altered by calcium or by phosphorylation of serines in the cPLA2 molecule. Activation of TLR4 receptors or surface receptors by sphingosine 1 phosphate may signal for phosphorylation of cPLA2. Binding of lipopolysaccharide to TLR4 results in phosphorylation of cPLA2 by MAP Kinases. This activation of MAP Kinases is mediated by both MyD88 and by TRIF activated through TLR4. Ongoing studies include the study of cPLA2 activation by low molecular weight fragments of hyaluronic acid, which may be produced at sites of inflammatory events from metabolism of hyaluronan or activation of inflamasome formation. In addition, the effect of the omega-3 fatty acid, docosahexanoic acid (DHA) on cPLA2 activation via the receptor GP120 has been studied. Two manuscripts have been published, one is in revision and one is in preparation submitted.