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Am J Physiol Cell Physiol (April 16, 2003). doi:10.1152/ajpcell.00547.2002
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Submitted on November 25, 2002
Accepted on January 15, 2003

Claudin Extracellular Domains Determine Paracellular Charge Selectivity and Resistance but not Tight Junction Fibril Architecture

Oscar R Colegio1, Christina Van Itallie2, Christoph Rahner3, and James M Anderson4*

1 Department of Cell Biology, Yale University, School of Medicine, New Haven, CT, USA
2 Department of Medicine, University of North Carolina, Chapel Hill, NC, USA
3 Department of Surgery, Yale University, School of Medicine, New Haven, CT, USA
4 Department of Cell and Molecular Physiology, University of North Carolina, Chapel Hill, NC, USA

* To whom correspondence should be addressed. E-mail: jandersn{at}med.unc.edu.

Tight junctions (TJs) regulate paracellular permeability across epithelia and vary widely in their electrical resistance (TER) and charge selectivity. The claudin family of transmembrane proteins influences these properties. We previously reported claudin-4 increased TER ~300% when expressed in low resistance MDCK II cells and decreased the paracellular permeability for Na+ more than Cl-. In comparison, we report here that expression of claudin-2 increases TER by only ~20% and does not change the ionic selectivity of MDCK II cells from their cation-selective background. To test whether the extracellular domains of claudins -4 and -2 determine their unique paracellular properties, we determined the effects of interchanging these domains between -4 and -2. Inducible expression of wild type claudins and extracellular domain chimeras increased both the number and depth of fibrils, but the characteristic fibril morphologies of claudin-2 or -4 were not altered by switching extracellular domains. Like claudin-4, chimeras expressing the first or both extracellular domains of claudin-4 on claudin-2 increased TER several-fold and profoundly decreased the permeability of Na+ relative to Cl-. In contrast, chimeras expressing the first or both extracellular domains of claudin-2 on claudin-4 increased the TER by only ~60% and ~40%, respectively, and only modestly altered charge selectivity. These results support a model in which the claudins create paracellular channels and the first extracellular domain is sufficient to determine both paracellular charge selectivity and TER.




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