Cellular and Subcellular Distribution of Polycystin-2, the Protein Product of the PKD2 Gene
| Autor: | Ruth Thomas, Richard Sandford, Oxana Ibraghimov-Beskrovnaya, Katherine W. Klinger, L. Foggensteiner, John Bradley, A. P. Bevan, Catherine A. Boulter, N. Coleman |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Pathology
medicine.medical_specialty TRPP Cation Channels Blotting Western Biology Kidney urologic and male genital diseases Antibodies Cell Line Gene product Mice Fetus Loop of Henle medicine Animals Humans Distal convoluted tubule education education.field_of_study Microscopy Confocal PKD1 urogenital system Calcium-Binding Proteins Membrane Proteins Proteins Kidney metabolism General Medicine Basolateral plasma membrane Polycystic Kidney Autosomal Dominant Precipitin Tests female genital diseases and pregnancy complications Cell biology Polycystin 2 medicine.anatomical_structure Microscopy Fluorescence Nephrology embryonic structures Rabbits Immunostaining |
| Zdroj: | Journal of the American Society of Nephrology. 11:814-827 |
| ISSN: | 1046-6673 |
| DOI: | 10.1681/asn.v115814 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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