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Originally published In Press as doi:10.1074/jbc.M106919200 on September 17, 2001

J. Biol. Chem., Vol. 276, Issue 45, 42610-42617, November 9, 2001
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Src Family Kinases Mediate Epithelial Na+ Channel Inhibition by Endothelin*

Elaine S. GilmoreDagger , M. Jackson Stutts, and Sharon L. MilgramDagger

From the Cystic Fibrosis/Pulmonary Research and Treatment Center and Dagger  Department of Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599

The epithelial Na+ channel (ENaC) is implicated in the pathogenesis of salt-sensitive hypertension. Recent evidence from animal models suggests that the vasoactive peptide, endothelin (ET-1), may be an important negative regulator of ENaC in vivo. We investigated the signaling pathway involved in endothelin-mediated ENaC inhibition. Experiments were performed in NIH 3T3 cells stably expressing genes for the three (alpha , beta , and gamma ) ENaC subunits. In whole cell patch clamp experiments, we found that ET-1 treatment induced a dose-dependent decrease in amiloride-sensitive currents. Using receptor-specific antagonists, we determined that the effects of ET-1 were attributed to activation of the ETB receptor. Moreover, the inhibitory effect of ET-1 on ENaC could be completely blocked when cells were pretreated with the selective Src family kinase inhibitor, PP2. Further studies revealed that basal Src family kinase activity strongly regulates ENaC whole cell currents and single channel gating. These results suggest that Src family kinases lie in a signaling pathway activated by ET-1 and are components of a novel negative regulatory cascade resulting in ENaC inhibition.

* This work was supported by National Institutes of Health Grant HL63755 (to S. L. M. and M. J. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Cell and Molecular Physiology, University of North Carolina, CB 7545, Chapel Hill, NC 27599. Tel.: 919-966-9792; Fax: 919-966-6927; E-mail: milg@med.unc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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