Ca2+ store-independent augmentation of [Ca2+]i responses to G-protein coupled receptor activation in recombinantly TRPC5-expressed rat pheochromocytoma (PC12) cells

被引：15

作者：

Ohta, T ^{[1
]}

Morishita, M

Mori, Y

Ito, S

机构：

[1] Hokkaido Univ, Dept Biomed Sci, Pharmacol Lab, Grad Sch Vet Med, Sapporo, Hokkaido 0600818, Japan

[2] Ctr Integ Biosci, Okazaki, Aichi 4448585, Japan

来源：

NEUROSCIENCE LETTERS | 2004年 / 358卷 / 03期

关键词：

bradykinin; receptor-operated Ca2+ entry; store-operated Ca2+ entry; transient receptor potential;

D O I：

10.1016/j.neulet.2004.01.028

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Mammalian homolocues 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+](i) and [Na+](i) were significantly higher than those in control cells. The [Ca2+](i) increases 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 thapsi.garigin. TRPC5-cells showed larger inward current and increase of [Na+]i in 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. (C) 2004 Elsevier Ireland Ltd. All rights reserved.

引用

页码：161 / 164

页数：4

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