Studies on the novel cellular functions of phospholipases A2

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(1) One of the secretory phospholipases A2 (PLA2s) in Aspergillus oryzae, sPlaB, displayed PLA1, not PLA2, activity.(2) A cytosolic PLA2-like protein in A. oryzae, AoPlaA, displayed phosphatidylethanolamine-specific PLA2 activity. Alanine substitution of putative active-site residues resulted in the loss of PLA2 activity.(3) Nerve growth factor (NGF)-induced mitogen-activated protein kinase (MAPK) phosphorylation in PC12 cells was found to be potentiated by the addition of lysophosphatidylcholine (LPC). Group X PLA2 displayed an effect similar to LPC. LPC augmented NGF-induced activation of TrkA, the receptor for NGF, thereby potentiating the downstream signaling pathways. By domain-swapping experiments, the extracellular domain of NGF was shown to be responsible for the effect of LPC.