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Second Messenger-Operated Calcium Entry Through TRPC6

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 898))

Abstract

Canonical transient receptor potential 6 (TRPC6) proteins assemble into heteromultimeric structures forming non-selective cation channels. In addition, many TRPC6-interacting proteins have been identified like some enzymes, channels, pumps, cytoskeleton-associated proteins, immunophilins, or cholesterol-binding proteins, indicating that TRPC6 are engaged into macromolecular complexes. Depending on the cell type and the experimental conditions used, TRPC6 activity has been reported to be controlled by diverse modalities. For instance, the second messenger diacylglycerol, store-depletion, the plant extract hyperforin or H2O2 have all been shown to trigger the opening of TRPC6 channels. A well-characterized consequence of TRPC6 activation is the elevation of the cytosolic concentration of Ca2+. This latter response can reflect the entry of Ca2+ through open TRPC6 channels but it can also be due to the Na+/Ca2+ exchanger (operating in its reverse mode) or voltage-gated Ca2+ channels (recruited in response to a TRPC6-mediated depolarization). Although TRPC6 controls a diverse array of biological functions in many tissues and cell types, its pathophysiological functions are far from being fully understood. This chapter covers some key features of TRPC6, with a special emphasis on their biological significance in kidney and blood cells.

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Acknowledgements

This work was supported by CNRS, l’Agence Nationale de la Recherche (ANR 13-NEUR-0003-02) and MINECO (Grant BFU2013-45564-C2-1-P).

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Bouron, A., Chauvet, S., Dryer, S., Rosado, J.A. (2016). Second Messenger-Operated Calcium Entry Through TRPC6. In: Rosado, J. (eds) Calcium Entry Pathways in Non-excitable Cells. Advances in Experimental Medicine and Biology, vol 898. Springer, Cham. https://doi.org/10.1007/978-3-319-26974-0_10

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