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Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294
The hypothesis that there is a highly
conserved, positively charged region distal to the second transmembrane
domain in
-ENaC (epithelial sodium channel) that acts as a putative
receptor site for the negatively charged COOH-terminal
- and
-ENaC tails was tested in mutagenesis experiments. After expression
in Xenopus oocytes,
-ENaC constructs in which positively
charged arginine residues were converted into negatively charged
glutamic acids could not be inhibited by blocking peptides. These
observations provide insight into the gating machinery of ENaC.
Liddle mutant; amiloride; inside-out patch; voltage clamp; post-M2 region
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