Functional analyses of a N-terminal splice variant of the alpha subunit ofthe epithelial sodium channel

The amiloride-sensitive epithelial sodium channel (ENaC) is the limiting st ep for sodium absorption in epithelial cells of the distal nephron, distal colon, airways and excretory ducts of several glands. In vivo and in vitro studies showed that the alpha subunit of ENaC is necessary for the expressi on of functional channels. Using RT-PCR strategy, a novel N-terminal splice variant has been identified which deletes 49 amino acids in the N-terminal region of the mouse alpha ENaC subunit. In oocytes expressing the alpha EN aC splice variant, together with beta and gamma ENaC subunits, amiloride-se nsitive currents were less than 20% of values obtained with the wild type E NaC. The single channel conductance and the ionic selectivity were similar and there was only a minor decrease in the level of expression of the prote in at the oocyte surface. These findings indicate that the deleted sequence in the N-terminal part of the mouse and rat alpha ENaC subunitmight play a role in the regulation of the activity of expressed ENaC channels. Copyrig ht (C) 2001 S. Karger AG, Basel.