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channel and activation
by phorbol ester
Departments of 1 Physiology and Biophysics and 2 Anesthesiology, University of Alabama at Birmingham, Birmingham, Alabama, 35294
We have isolated a niflumic acid-insensitive,
Ca2+-activated
Cl
channel (CaCC) from
bovine trachea that migrates at 38 kDa (p38) on reducing sodium dodecyl
sulfate-polyacrylamide gel electrophoresis. However, a cloned CaCC
isolated from a tracheal cDNA expression library by screening with an
antibody raised against p38 has a primary cDNA transcript of 2712 base
pairs that codes for a 100-kDa protein and is not susceptible to
dithiothreitol reduction. To test the hypothesis that the functional
channel may be a much smaller posttranslationally processed form of the
100-kDa protein, we generated a mutant construct (CaCCX, 42.5-kDa
protein) truncated at the NH2 and
COOH termini. The whole cell currents of wild-type (wt) CaCC and CaCCX
expressed in Xenopus oocytes were
10-fold higher than those of water-injected oocytes and were further
increased by ionomycin or A-23187 and inhibited by
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid and
dithiothreitol. Whole cell currents in wtCaCC- and CaCCX-expressing oocytes could also be activated by phorbol 12-myristate 13-acetate and
could be inhibited by chelerythrine chloride, suggesting that the
cloned CaCC is regulated by protein kinase C. These results suggest
that a smaller form of the full-length CaCC can form a functional
channel.
anions; voltage clamp; ion channel; RNA expression; bovine trachea; Xenopus oocyte; calcium-activated chloride channel
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