Supplementary Material for: Kainate Receptors Mediate Regulated Exocytosis of Secretory Phospholipase A2 in SH-SY5Y Neuroblastoma Cells
datasetposted on 19.10.2011 by Than A., Tan Y., Ong W.-Y., Farooqui A.A., Chen P.
Datasets usually provide raw data for analysis. This raw data often comes in spreadsheet form, but can be any collection of data, on which analysis can be performed.
Secretory phospholipase A2 (sPLA2) isoforms are widely expressed in the brain and spinal cord. Group IIA sPLA2 (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 neuronal signaling and synaptic transmission. However, the mechanisms by which sPLA2 is itself released, and a possible relation between glutamate receptors and sPLA2 exocytosis, are 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 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 α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and kainate (KA) induced vesicular exocytosis and release of sPLA2-IIA. UBP 302, a GluR5-specific KA receptor antagonist, abolished the effect of KA, confirming the role of KA receptors in mediating sPLA2-IIA secretion. Moreover, KA-induced sPLA2-IIA secretion is dependent on Ca2+ 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.