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1 Department of Physiology and Biophysics, University of Nebraska Medical Center, Omaha, NE, USA
* To whom correspondence should be addressed. E-mail: ssansom{at}unmc.edu.
Studies were performed to identify the molecular component responsible for store-operated Ca2+ entry in a mouse mesangial cell line (MMC). Because the canonical transient receptor potential (TRPC) family of proteins was previously shown to comprise calcium selective and nonselective cation channels in a variety of cells, we screened TRPC1-7 using molecular methods and used the fura-2 method to determine their participation as components of the mesangial store-operated channel (SOC). Using TRPC specific primers and RT-PCR, we found that cultured mouse mesangial cells contained mRNA for TRPC1 and TRPC4 but not TRPC2, 3, 5, 6, and 7. Immunocytochemical staining of MMC revealed predominantly cytoplasmic expression of TRPC1 and plasmalemmal expression of TRPC4. The role of TRPC4 in SOC was determined with TRPC4 antisense and fura-2 ratiometric measurements of [Ca2+]i. SOC was measured as the increase in intracellular calcium concentration (
[Ca2+]i) after increasing extracellular Ca2+ from <10 nM to 1 mM in the continued presence of thapsigargin. We found that TRPC4 antisense, which reduced plasmalemmal expression of TRPC4, inhibited SOC by 83%. Incubation with scrambled TRPC4 oligonucleotides did not affect SOC. Immunohistochemical staining identified expressed TRPC4 in the glomeruli of mouse renal sections. RT-PCR performed to distinguish between TRPC4-alpha and TRPC4-beta was consistent with expression of both isoforms in brain, but only TRPC4-alpha expression in MMC. These studies showed that TRPC4-alpha may form the homotetrameric SOC channels in mouse mesangial cells.
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