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Am J Physiol Gastrointest Liver Physiol 279: G268-G276, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 2, G268-G276, August 2000

Expression and canalicular localization of two isoforms of the ClC-3 chloride channel from rat hepatocytes

Kazuo Shimada1, Xinhua Li1, Guiyan Xu1, David E. Nowak1, Lori A. Showalter1, and Steven A. Weinman1,2

Departments of 1 Physiology and Biophysics and 2 Internal Medicine, University of Texas Medical Branch, Galveston, Texas, 77555

The molecular identities of functional chloride channels in hepatocytes are largely unknown. We examined the ClC-3 chloride channel in rat hepatocytes and found that mRNA for two different isoforms is present. A short form is identical to the previously reported sequence for rat ClC-3, and a long form contains a 176-bp insertion immediately upstream of the translation initiation site. This predicts a 58-amino acid NH2 terminal insertion. Both long and short form mRNA was expressed in diverse tissues of the rat. Transient transfection of the long form in CHO-K1 cells resulted in currents with an I- > B- > Cl- selectivity sequence, outward rectification, and inactivation at positive voltages. Short form currents had identical ionic selectivity but displayed a more extreme outward rectification and showed no voltage-dependent inactivation. Immunofluorescence and immunoblots localized native ClC-3 preferentially but not exclusively to the canalicular membrane. We have therefore identified a new isoform of rat ClC-3 and shown that expression of both isoforms produces functional channels. In hepatocytes, ClC-3 is located in association with the canalicular membrane.

ion channels; liver; CHO-K1 cells; canalicular membrane


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