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Renal Division and Membrane Biology Program, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115
First published August 15, 2001;
10.1152/ajprenal. 00021.2001.
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 COOH-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 ZO-1. 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.
tight junction; paracellular transport; renal tubule; gene expression
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