Ca2+ store-independent augmentation of [Ca2+]i responses to G-protein coupled receptor activation in recombinantly TRPC5-expressed rat pheochromocytoma (PC12) cells
Ca2+ store-independent augmentation of [Ca2+]i responses to G-protein coupled receptor activation in recombinantly TRPC5-expressed rat pheochromocytoma (PC12) cells
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DOI:
10.1016/j.neulet.2004.01.028
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发表时间:
2004-04
影响因子:
2.5
通讯作者:
T. Ohta;M. Morishita;Y. Mori;S. Ito
中科院分区:
文献类型:
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作者:
T. Ohta;M. Morishita;Y. Mori;S. Ito
Mammalian homologues of the Drosophila canonical transient receptor potential (trp) protein (TRPC) have been implicated to function as receptor-operated Ca2+channels (ROCs) or store-operated Ca2+channels (SOCs). To determine the role of TRPC5 protein in neural cells, TRPC5 was recombinantly expressed in rat pheochromocytoma cells (PC12) and changes in intracellular Ca2+concentration ([Ca2+]i) and Na+concentration ([Na+]i) were analyzed. TRPC1 and TRPC3 mRNAs were endogenously expressed in PC12 cells. In TRPC5-expressed cells (TRPC5-cells), the resting [Ca2+]iand [Na+]iwere significantly higher than those in control cells. The [Ca2+]iincreases induced by bradykinin and uridine 5′-triphosphate were significantly larger in TRPC5-cells. TRPC5 expression did not change in store-operated Ca2+entry elicited by thapsigarigin. TRPC5-cells showed larger inward current and increase of [Na+]iin response to BK than control cells. These results suggest that TRPC5 channels expressed in PC12 cells function as ROCs activated by G-protein/phospholipase C coupled receptors, but not as SOCs.