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- 1-Kainate receptors mediate regulated exocytosis of secretory phospholipase A 2 in SH-SY 5 Y neuroblastoma cells

Secretory phospholipase A2 isoforms are widely expres sed in the brain and spinal cord. Group IIA secretory phospholipase A2 (sPLA2-IIA) has been shown to stimulate exocytosis and release of neurotransmitters in neuroendocrine PC12 cells and neurons, suggesting a role of the enzyme in synaptic transmission. However, the mechanisms by which sPLA2 is itself released, and a possible relation between glutamate receptors and sPLA2 exocytosis is unknown. This study was carried out to elucidate the effects of glutamate receptor agonists on exocytosis of sPLA2-IIA in transfected SH-SY5Y neuroblastoma cells. sPLA2-IIA enzyme was found to packaged in fusion-competent vesicles and released constitutively or upon stimulation, suggesting regulated secretion. The signal peptide of sPLA2-IIA is required for its vesicular localization and exocytosis. External application of AMPA and kainate, but not NMDA, induced vesicular exocytosis and release of sPLA2-IIA. UBP 302, a GluR5 specific kainate receptor antagonist, abolished the effect of kainate, confirming the role of kainate receptors in mediating sPLA2-IIA secretion. Moreover, kainate-induced sPLA2-IIA secretion is dependent on Ca 2+ and protein kinase C. Together, these findings provide evidence of a link between glutamate receptors and regulated sPLA2 secretion in neurons, that may play an important role in synaptic plasticity, pain transmission, and neurodegenerative diseases.