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1 Cancer Biology Laboratories, Department of Molecular Medicine, Cornell University College of Veterinary Medicine, Ithaca, New York 14853; and 2 Department of Physiology and Biophysics, University of Alabama, Birmingham, Alabama 35294
The CLCA family of
Ca2+-activated
Cl
channels has recently
been discovered, with an increasing number of closely related members isolated from different species. Here we report the cloning of the
second human homolog, hCLCA2, from a human lung cDNA library. Northern
blot and RT-PCR analyses revealed additional expression in trachea and
mammary gland. A primary translation product of 120 kDa was cleaved
into two cell surface-associated glycoproteins of 86 and 34 kDa in
transfected HEK-293 cells. hCLCA2 is the first CLCA homolog for which
the transmembrane structure has been systematically studied.
Glycosylation site scanning and protease protection assays revealed
five transmembrane domains with a large, cysteine-rich, amino-terminal
extracellular domain. Whole cell patch-clamp recordings of
hCLCA2-transfected HEK-293 cells detected a slightly outwardly rectifying anion conductance that was increased in the presence of the
Ca2+ ionophore ionomycin and
inhibited by DIDS, dithiothreitol, niflumic acid, and tamoxifen.
Expression in human trachea and lung suggests that hCLCA2 may play a
role in the complex pathogenesis of cystic fibrosis.
calcium-activated chloride channel; cystic fibrosis
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