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Articles in PresS, published online ahead of print August 15, 2001
Am J Physiol Renal Physiol, 10.1152/ajprenal.0021.2001
Submitted on January 26, 2001
Accepted on June 20, 2001
1 Renal Division and Membrane Biology Program, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: ayu{at}rics.bwh.harvard.edu.
The proximal nephron possesses a leaky epithelium with unique paracellular permeability properties that underlie its high rate of passive NaCl and water reabsorption, but the molecular basis is unknown. The claudins are a large family of transmembrane proteins that are part of the tight junction complex and likely form structural components of a paracellular pore. To localize claudin-2 in the mouse kidney, we performed in situ hybridization using an isoform-specific riboprobe, and immunohistochemistry using a polyclonal antibody directed against a C-terminal peptide. Claudin-2 mRNA and protein were found throughout the proximal tubule and in the contiguous early segment of the thin descending limb of long-looped nephrons. The level of expression demonstrated an axial increase from proximal to distal segments. In confocal images, the subcellular localization of claudin-2 protein coincided with that of the tight junction protein, ZO1. Our findings suggest that claudin-2 is a component of the paracellular pathway of the most proximal segments of the nephron, and that it may be responsible for their uniquely leaky permeability properties.
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