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Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene

Foggensteiner, L., Bevan, A. P., Thomas, R., Coleman, N., Boulter, Catherine, Bradley, J., Ibraghimov-Beskrovnaya, O., Klinger, K. and Sandford, R. 2000. Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene. Journal of the American Society of Nephrology 11 (5) , pp. 814-827.

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Abstract

Mutations in the PKD1 and PKD2 genes account for 85 and 15% of cases of autosomal dominant polycystic kidney disease, respectively. Polycystin-2, the product of the PKD2 gene, is predicted to be an integral membrane protein with homology to a family of voltage-activated Ca(2+) channels. In vitro studies suggest that it may interact with polycystin-1, the PKD1 gene product, via coiled-coil domains present in their C-terminal domains. In this study, the cellular and subcellular distribution of polycystin-2 is defined and compared with polycystin-1. A panel of rabbit polyclonal antisera was raised against polycystin-2 and shown to recognize a single band consistent with polycystin-2 in multiple tissues and cell lines by immunoprecipitation and Western blotting. Immunostaining of human and murine renal tissues demonstrated widespread and developmentally regulated expression of polycytin-2, with highest levels in the kidney in the thick ascending limbs of the loop of Henle and the distal convoluted tubule. In contrast, polycystin-1 expression, while localizing to the same tubular segments, was highest in the collecting ducts. Immunohistochemical staining and immunofluorescence microscopy localized polycystin-2 to the basolateral plasma membrane of kidney tubular epithelial cells compared with the junctional localization of polycystin-1. Differences in the developmental, cellular, and subcellular expression of polycystin-1 and polycystin-2 suggest that they may be able to function independently of each other in addition to a potential in vivo interaction via their C-termini.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Lippincott, Williams & Wilkins
ISSN: 1046-6673
Last Modified: 04 Jun 2017 06:49
URI: http://orca-mwe.cf.ac.uk/id/eprint/65093

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