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1 Department of Integrative Physiology, University of North Texas Health Science Center, Fort Worth, TX, USA
2 Department of Integrative Physiology, University of North Texas Health Science Center, Fort Worth, TX, USA; Department of Physiology, Anhui Medical University, Hefei, Anhui, China
3 Department of Cell Biology and Genetics, University of North Texas Health Science Center, Fort Worth, TX, USA
4 Department of Pathology, UT Southwestern Medical Center at Dallas, Dallas, TX, USA
* To whom correspondence should be addressed. E-mail: rma{at}hsc.unt.edu.
Mesangial cells are located within glomerular capillary loops and contribute to the physiological regulation of glomerular hemodynamics. Function of mesangial cells is controlled by a variety of ion channels in the plasma membrane, including non-selective cation channels, receptor-operated Ca2+ channels, and recently identified store-operated Ca2+ channels. Although the significance of these channels has been widely acknowledged, their molecular identities are still unknown. Recently, the members of the canonical transient receptor potential (TRPC) protein family have been demonstrated to behave as cation channels. The present study was performed to identify the isoforms of endogenous TRPC proteins in human mesangial cells (HMCs) and their interactions. Western Blotting showed that TRPC1, 3, 4 and 6 were expressed in cultured HMCs. Consistently, immunofluorescent confocal microscopy revealed specific stainings for TRPC1, 3, 4, and 6 with predominant intracellular localization. However, TRPC5 and 7 were not detectable at protein level by either Western blotting or immunofluorescent staining. The expression of TRPC1, 3, 4, and 6 was also observed in rat and human glomeruli using fluorescent immunohistochemistry. Furthermore, co-immunoprecipitation experiments and immunofluorescent double staining displayed that TRPC1 had physical interaction with TRPC4 and 6, while no interactions were detected among other isoforms of TRPCs. Ca2+ fluorescent ratiometry measurement showed that store-operated Ca2+ entry in HMCs was significantly reduced by knocking down TRPC1, but enhanced by over-expressing TRPC1. These results suggest that HMCs specifically express isoforms of TRPC1, 3, 4, and 6 proteins. These isoforms of TRPCs might selectively assemble to form functional complexes.
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