Abstract
We previously demonstrated that secretory phospholipase A2 (sPLA2) and lysophosphatidylcholine (LPC) exhibit neurotrophin-like neuritogenic activity in the rat pheochromocytoma cell line PC12. In this study, we further analyzed the mechanism whereby sPLA2 displays neurite-inducing activity. Exogenously added mammalian group X sPLA2 (sPLA2-X), but not group IB and IIA sPLA2s, induced neuritogenesis, which correlated with the ability of sPLA2-X to liberate LPC into the culture media. In accordance, blocking the effect of LPC by supplementation of bovine serum albumin or phospholipase B attenuated neuritogenesis by sPLA2 or LPC. Overproduction or suppression of G2A, a G-protein-coupled receptor involved in LPC signaling, resulted in the enhancement or reduction of neuritogenesis induced by sPLA2 treatment. These results indicate that the neuritogenic effect of sPLA2 is mediated by generation of LPC and subsequent activation of G2A.
Highlights
Phospholipase A2 (PLA2)1 is an enzyme that cleaves sn-2 ester linkage of glycerophospholipids thereby releasing fatty acids and 2-lysophospholipids [1,2,3]
We previously demonstrated that secretory phospholipase A2 and lysophosphatidylcholine (LPC) exhibit neurotrophin-like neuritogenic activity in the rat pheochromocytoma cell line PC12
These results suggest that arachidonic acid release and subsequent conversion to eicosanoids is not involved in the neuritogenesis of PC12 cells
Summary
Phospholipase A2 (PLA2)1 is an enzyme that cleaves sn-2 ester linkage of glycerophospholipids thereby releasing fatty acids and 2-lysophospholipids [1,2,3]. When the effect of purified human sPLA2-X was examined, generation of [14C]LPC was observed in the medium, but not in the cell-associated fraction, which is reminiscent of the result with p15 (Fig. 3C).
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