Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells
Secretory phospholipase A(2) (sPLA(2)) isoforms are widely expressed in the brain and spinal cord. Group IIA sPLA(2) (sPLA(2)-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 a...
| Main Authors: | , , , , |
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| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/107467 http://hdl.handle.net/10220/16680 |
| _version_ | 1826121935532064768 |
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| author | Farooqui, Akhlaq A. Than, Aung Tan, Yan Ong, Wei-Yi Chen, Peng |
| author2 | School of Chemical and Biomedical Engineering |
| author_facet | School of Chemical and Biomedical Engineering Farooqui, Akhlaq A. Than, Aung Tan, Yan Ong, Wei-Yi Chen, Peng |
| author_sort | Farooqui, Akhlaq A. |
| collection | NTU |
| description | Secretory phospholipase A(2) (sPLA(2)) isoforms are widely expressed in the brain and spinal cord. Group IIA sPLA(2) (sPLA(2)-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 sPLA(2) is itself released, and a possible relation between glutamate receptors and sPLA(2) exocytosis, are unknown. This study was carried out to elucidate the effects of glutamate receptor agonists on exocytosis of sPLA(2)-IIA in transfected SH-SY5Y neuroblastoma cells. sPLA(2)-IIA enzyme was packaged in fusion-competent vesicles and released constitutively or upon stimulation, suggesting regulated secretion. The signal peptide of sPLA(2)-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 sPLA(2)-IIA. UBP 302, a GluR5-specific KA receptor antagonist, abolished the effect of KA, confirming the role of KA receptors in mediating sPLA(2)-IIA secretion. Moreover, KA-induced sPLA(2)-IIA secretion is dependent on Ca(2+) and protein kinase C. Together, these findings provide evidence of a link between glutamate receptors and regulated sPLA(2) secretion in neurons that may play an important role in synaptic plasticity, pain transmission and neurodegenerative diseases. |
| first_indexed | 2024-10-01T05:40:35Z |
| format | Journal Article |
| id | ntu-10356/107467 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T05:40:35Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/1074672023-12-29T06:49:35Z Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells Farooqui, Akhlaq A. Than, Aung Tan, Yan Ong, Wei-Yi Chen, Peng School of Chemical and Biomedical Engineering DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology Secretory phospholipase A(2) (sPLA(2)) isoforms are widely expressed in the brain and spinal cord. Group IIA sPLA(2) (sPLA(2)-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 sPLA(2) is itself released, and a possible relation between glutamate receptors and sPLA(2) exocytosis, are unknown. This study was carried out to elucidate the effects of glutamate receptor agonists on exocytosis of sPLA(2)-IIA in transfected SH-SY5Y neuroblastoma cells. sPLA(2)-IIA enzyme was packaged in fusion-competent vesicles and released constitutively or upon stimulation, suggesting regulated secretion. The signal peptide of sPLA(2)-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 sPLA(2)-IIA. UBP 302, a GluR5-specific KA receptor antagonist, abolished the effect of KA, confirming the role of KA receptors in mediating sPLA(2)-IIA secretion. Moreover, KA-induced sPLA(2)-IIA secretion is dependent on Ca(2+) and protein kinase C. Together, these findings provide evidence of a link between glutamate receptors and regulated sPLA(2) secretion in neurons that may play an important role in synaptic plasticity, pain transmission and neurodegenerative diseases. Accepted version 2013-10-22T01:56:55Z 2019-12-06T22:31:51Z 2013-10-22T01:56:55Z 2019-12-06T22:31:51Z 2011 2011 Journal Article Than, A., Tan, Y., Ong, W. Y., Farooqui, A. A., & Chen P. (2012). Kainate Receptors Mediate Regulated Exocytosis of Secretory Phospholipase A2 in SH-SY5Y Neuroblastoma Cells. Neurosignals, 20(2), 72-85. https://hdl.handle.net/10356/107467 http://hdl.handle.net/10220/16680 10.1159/000330414 en Neurosignals © 2011 S. Karger AG, Basel. application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology Farooqui, Akhlaq A. Than, Aung Tan, Yan Ong, Wei-Yi Chen, Peng Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title | Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title_full | Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title_fullStr | Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title_full_unstemmed | Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title_short | Kainate receptors mediate regulated exocytosis of secretory phospholipase A2 in SH-SY5Y neuroblastoma cells |
| title_sort | kainate receptors mediate regulated exocytosis of secretory phospholipase a2 in sh sy5y neuroblastoma cells |
| topic | DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology |
| url | https://hdl.handle.net/10356/107467 http://hdl.handle.net/10220/16680 |
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