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(Circulation Research. 2006;98:1520.)
© 2006 American Heart Association, Inc.

Cellular Biology

Heteromultimeric TRPC6-TRPC7 Channels Contribute to Arginine Vasopressin-Induced Cation Current of A7r5 Vascular Smooth Muscle Cells

Yoshiaki Maruyama, Yuko Nakanishi, Emma J. Walsh, David P. Wilson, Donald G. Welsh, William C. Cole

From The Smooth Muscle Research Group, Faculty of Medicine, University of Calgary, Alberta, Canada.

Correspondence to Dr William C. Cole, Professor of Pharmacology & Therapeutics, Andrew Family Professor in Cardiovascular Research, Chair, The Smooth Muscle Research Group, Department of Pharmacology & Therapeutics, Faculty of Medicine, University of Calgary, 3330 Hospital Dr, NW, Calgary, Alberta T2N 4N1, Canada. E-mail wcole{at}ucalgary.ca

The molecular identity of receptor-operated, nonselective cation channels (ROCs) of vascular smooth muscle (VSM) cells is not known for certain. Mammalian homologues of the Drosophila canonical transient receptor potential channels (TRPCs) are possible candidates. This study tested the hypothesis that heteromultimeric TRPC channels contribute to ROC current of A7r5 VSM cells activated by [Arg⁸]-vasopressin. A7r5 cells expressed transcripts encoding TRPC1, TRPC4ß, TRPC6, and TRPC7. TRPC4, TRPC6, and TRPC7 protein expression was confirmed by immunoblotting and association of TRPC6 with TRPC7, but not TRPC4ß, was detected by coimmunoprecipitation. The amplitude of arginine vasopressin (AVP)-induced ROC current was suppressed by dominant-negative mutant TRPC6 (TRPC6^DN) but not TRPC5 (TRPC5^DN) mutant subunit expression. These data indicate a role for TRPC6- and/or TRPC7-containing channels and rule a more complex subunit composition including TRPC1 and TRPC4. Increasing extracellular Ca²⁺ concentration ([Ca²⁺]_o) from 0.05 to 1 mmol/L suppressed currents owing to native, TRPC7, and heteromultimeric TRPC6-TRPC7 channels, but not TRPC6 current, which was slightly enhanced. The relative changes in native and heteromultimeric TRPC6-TRPC7 current amplitudes for [Ca²⁺]_o between 0.01 and 1 mmol/L were identical, but the changes in homomultimeric TRPC6 and TRPC7 currents were significantly less and greater, respectively, compared with the native channels. Taken together, the data provide biochemical and functional evidence supporting the view that heteromultimeric TRPC6-TRPC7 channels contribute to receptor-activated, nonselective cation channels of A7r5 VSM cells.

Key Words: TRPC6 • TRPC7 • receptor-operated cation channel • vascular smooth muscle

Related Article:

Molecular Diversity of Receptor Operated Channels in Vascular Smooth Muscle: A Role for Heteromultimeric TRP Channels?

Scott Earley
Circ. Res. 2006 98: 1462-1464. [Full Text] [PDF]

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