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Am J Physiol Cell Physiol (December 8, 2004). doi:10.1152/ajpcell.00417.2004
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Submitted on August 24, 2004
Accepted on December 6, 2004

Expression of TRPC 4 channel protein that interacts with NHERF-2 in rat Descending Vasa Recta

Whaseon Lee-Kwon1, James B Wade2, Zhong Zhang1, Thomas L Pallone3, and Edward J Weinman4*

1 Medicine, University of Maryland, School of Medicine, Baltimore, MD, USA
2 Physiology, University of Maryland, School of Medicine, Baltimore, MD, USA
3 Medicine, University of Maryland, School of Medicine, Baltimore, MD, USA; Physiology, University of Maryland, School of Medicine, Baltimore, MD, USA
4 Medicine, University of Maryland, School of Medicine, Baltimore, MD, USA; Physiology, University of Maryland, School of Medicine, Baltimore, MD, USA; Medical Service, 3Department of Veterans Affairs Medical Center, Baltimore, MD, USA

* To whom correspondence should be addressed. E-mail: eweinman{at}medicine.umaryland.edu.

The PDZ domain adaptor protein NHERF-2 is expressed in renal medullary descending vasa recta (DVR) although its function has not been defined. TRPC4 and TRPC5, nonselective cation channels that transport calcium, have recently been demonstrated to complex with the NHERF proteins. We investigated whether TRPC4 and/or TRPC5 are associated with NHERF-2 in DVR. Using RT-PCR, mRNA for TRPC4 and NHERF-2, but not TRPC5 or NHERF-1, was detected in microdissected DVR. Immunohistochemical studies demonstrated expression of TRPC4 and NHERF-2 proteins in both the endothelial cells and pericytes. These proteins co-localized in some cells of the DVR. TRPC4 co-immunoprecipitated with NHERF-2 from renal medullary lysates and NHERF-2 co-immunoprecipitated with TRPC4. TRPC5 was not detected in DVR using immunohistochemistry, or in NHERF-2 immunoprecipitates. We conclude that DVR pericytes and endothelia co-express TRPC4 and NHERF-2 mRNA and protein, and that these proteins co-localize and co-immunoprecipitate indicating a possible physical association. This suggests TRPC4 and NHERF-2 may play a role in interactions related to calcium signaling.




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