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Canonical transient receptor potential (TRPC) channels are Ca²⁺-permeable, non-selective cation channels those are widely expressed in mammalian cells. Various molecules have been found to regulate TRPC both in vivo and in vitro, but it is unclear how heterotrimeric G proteins transmit external stimuli to regulate the activity of TRPC5. Here, we demonstrated that TRPC5 was potentiated by the Gα_s regulatory pathway. Whole-cell TRPC5 current was significantly increased by β-adrenergic receptor agonist, isoproterenol (ISO, 246±36%, n=6), an activator of the adenylate cyclase, forskolin (FSK, 273±6%, n=5), or a membrane permeable cAMP analogue, 8-Br-cAMP (251±63%, n=7). In addition, robust Ca²⁺ transient induced by isoproterenol was observed utilizing a Ca²⁺ imaging technique. When intracellular [Ca²⁺]_i was buffered to 50nM, cAMP-induced potentiation was attenuated. We also found that the Ca …