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1 The Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
2 Department of Center for Environmental Medicine and Lung Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
3 The Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
4 The Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Center for Environmental Medicine and Lung Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
5 The Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
* To whom correspondence should be addressed. E-mail: larry_johnson{at}med.unc.edu.
Airway epithelial tight junctions (TJs) serve to separate the external and internal environments of the lung. However, the members of the claudin family that mediate this function have not been fully delineated. We characterized the claudin expression in normal airways removed from human donors during lung transplantation and determined the contribution of each claudin to airway barrier function. Stable cell lines in NIH3T3 and a human airway (IB3.1) cells were constructed expressing the claudin components found in the human airway, claudin-1, -3, or -5. The effects of claudin expression on transepithelial resistance (RT), permeability coefficients (Papp), and claudin-claudin interactions were assessed. Claudins-1 and -3 decreased solute permeability whereas Claudin-5 increased permeability. We also detected oligomerization of claudin-5 in cell lines and in freshly excised human airways. Coimmunoprecipitation studies revealed heterophilic interactions between claudin species in both cell lines and human airway epithelium. These suggest that airway TJs are regulated by claudin-claudin interactions which confer the selectivity of the junction.
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