Co-Regulated Pendrin and Aquaporin 5 Expression and Trafficking in Type-B Intercalated Cells under Potassium Depletion
Author(s) -
Giuseppe Procino,
Serena Milano,
Grazia Tamma,
Silvia Dossena,
Claudia Barbieri,
Maria Celeste Nicoletti,
Marianna Ranieri,
Annarita Di Mise,
Charity Nofziger,
Maria Svelto,
Markus Paulmichl,
Giovanna Valenti
Publication year - 2013
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000356638
Subject(s) - pendrin , apical membrane , chemistry , aquaporin 2 , microbiology and biotechnology , aquaporin , kidney , aquaporin 1 , medicine , endocrinology , intercalated cell , internalization , biology , biochemistry , cell , membrane , water channel , transporter , mechanical engineering , engineering , inlet , gene
We recently reported that aquaporin 5 (AQP5), a water channel never identified in the kidney before, co-localizes with pendrin at the apical membrane of type-B intercalated cells in the kidney cortex. Since co-expression of AQP5 and pendrin in the apical membrane domain is a common feature of several other epithelia such as cochlear and bronchial epithelial cells, we evaluated here whether this strict membrane association may reflect a co-regulation of the two proteins. To investigate this possibility, we analyzed AQP5 and pendrin expression and trafficking in mice under chronic K(+) depletion, a condition that results in an increased ability of renal tubule to reabsorb bicarbonate, often leads to metabolic alkalosis and is known to strongly reduce pendrin expression.
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