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Am J Physiol Renal Physiol (May 22, 2002). doi:10.1152/ajprenal.00037.2002
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Articles in PresS, published online ahead of print May 22, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00037.2002
Submitted on January 28, 2002
Accepted on May 8, 2002

Immunohistochemical and immunoelectron microscopic localization of pendrin in intercalated cell subtypes in rat and mouse kidney

Young-Hee Kim1, Tae-Hwan Kwon2, Sebastian Frische3, Jin Kim4, C. Craig Tisher5, Kirsten M Madsen1, and Soren Nielsen3*

1 Dept of Medicine, University of Florida, Gainesville, FL, USA
2 Dept of Physiology, Dongguk University, Kyungju, Korea, Republic of; The Water and Salt Research Center, Aarhus, Denmark
3 The Water and Salt Research Center, Aarhus, Denmark
4 Dept of Anatomy, Catholic University, Seoul, Korea, Republic of
5 Div of Nephrology, University of Florida, Gainesville, FL, USA

* To whom correspondence should be addressed. E-mail: sn{at}ana.au.dk.

Recent studies have demonstrated that a novel anion exchanger, pendrin, is expressed in the apical domain of type B intercalated cells in the mammalian collecting duct. The purpose of this study was, first, to determine the expression and distribution of pendrin along the collecting duct and connecting tubule of the mouse and rat kidney and establish whether pendrin is expressed in the nonA-nonB intercalated cells, and secondly, to determine the intracellular localization of pendrin in the different populations of intercalated cells by immunoelectron microscopy. A peptidederived affinity-purified antibody was generated that specifically recognized pendrin in immunoblots of rat and mouse kidney. Immunohistochemistry and confocal laser scanning microscopy demonstrated the presence of pendrin in apical domains of all type B intercalated cells in mouse and rat connecting tubule and collecting duct. In addition, strong pendrin immunostaining was observed in nonA-nonB intercalated cells. There was no labeling of type A intercalated cells. Immunoelectron microscopy demonstrated that pendrin was located in the apical plasma membrane and intracellular vesicles of both type B intercalated cells and nonA-nonB cells, the latter identified by the presence of H+-ATPase in the apical plasma membrane. The results of this study demonstrate that both pendrin and H+-ATPase are expressed in the apical plasma membrane of nonA-nonB intercalated cells suggesting that these cells are capable of both bicarbonate and proton secretion. Furthermore, the presence of pendrin in both the apical plasma membrane and apical intracellular vesicles of type B and nonA-nonB intercalated cells suggests that bicarbonate secretion may be regulated by trafficking of pendrin between the two membrane compartments.




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