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Vol. 273, Issue 4, C1176-C1185, October 1997
channel from the
renal cell line A6
1 Departments of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77555; and 2 Laboratoire Jean Maetz, Centre National de la Recherche Scientifique and Commissariat à l'Energie Atomique Unité de Recherche Associée 1855, 06320 Villefranche-sur-Mer, France
Cl
channels are
important for ion transport and cell volume regulation in A6 renal
cells. In the present study, we used reverse transcriptase
(RT)-polymerase chain reaction (PCR) and rapid amplification of cDNA
ends (RACE) to identify proteins homologous to ClC
Cl channel proteins in A6
cells. Using degenerate primers designed on consensus sequences for
members of the ClC family, we amplified an RT-PCR product that had
significant homology to the ClC sequences. RACE-PCR was then used to
isolate several full-length clones that had total lengths from 2,764 to
3,016 base pairs. Although the coding regions were identical, sequence
differences occurred in the 5' noncoding regions. The amino acid
sequences of the clones had high homologies to rat and human ClC-5 (85 and 84%, respectively, if the 5th methionine of the open reading frame
represents the start codon). Three parts of the protein (53, 80, and 63 amino acids in length) were 97-100% homologous to the mammalian
sequences. Ribonuclease protection assay analysis revealed mRNA for
this protein in oocytes, kidney, intestine, liver, brain, and blood, with lower amounts in stomach, muscle, and skin. Expression of the
clones in Xenopus
laevis oocytes resulted in an
outwardly rectifying Cl
current that was inhibited by
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid and
possessed an anion selectivity of
I > Cl >> gluconate.
cultured renal cells; outwardly rectifying chloride current; ClC-5; Xenopus laevis
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