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1 Department of Medicine, University of North Carolina, Chapel Hill, North Carolina, United States
2 Cell and Molecular Physiology, University of North Carolina, Chapel Hill, North Carolina, United States
3 Department of Nephrology, University of Southern California Keck School of Medicine, Los Angeles, California, United States
4 Cell and Molecular Physiology, UNC at Chapel Hill, School of Medicine, Chapel Hill, North Carolina, United States
* To whom correspondence should be addressed. E-mail: vitallie{at}med.unc.edu.
Members of the large claudin family of tight junction proteins create the differences in paracellular conductance and charge selectivity observed among different epithelia. Previous studies demonstrated that ionic charge selectivity is influenced by acidic or basic amino acids on the first extracellular domain of claudins. We noted two alternatively spliced variants of claudin-10 in the database, 10a and 10b, which are predicted to encode two different first extracellular domains, and asked if this might be a novel mechanism to generate two different permselectivities from a single gene. Using quantitative PCR, we found that claudin-10b is widely expressed among tissues including the kidney; however claudin-10a is unique to the kidney. Using a nondiscriminating antibody we found that claudin-10 (a plus b) is expressed in most segments of the nephron. In situ hybridization, however, showed mRNA for 10a is concentrated in the cortex and mRNA for 10b is more highly expressed in the medulla. Expression in MDCK II and LLC-PK1 cells reveals that both variants form low resistance pores, and that claudin-10b is more selective for cations than claudin-10a. Charge-reversing mutations of cationic residues on 10a reveal positions that contribute to its anion selectivity. We conclude that alternative splicing of claudin-10 generates unique permselectivities and might contribute to the variable paracellular transport observed along the nephron.
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