Peptide block of constituitively activated na+ channels in liddle's disease. Ismailov, Iskander I., Bakhram K. Berdiev, Catherine M. Fuller, Anne Lynn Bradford, Richard P. Lifton, David G. Warnock, James K. Bubien, and Dale J. Benos. Departments of Physiology and Biophysics and Medicine, The University of Alabama at Birmingham and Department of Veteran Affairs, Birmingham VA Medical Center, Birmingham, Alabama 35294 and Howard Hughes Medical Institute, Departments of Medicine and Genetics, Boyer Center for Molecular Medicine, Yale University, New Haven, CT 06510
APStracts 2:0241C, 1995.
Hypertension is a multifactorial disorder that results in an increased risk of cardiovascular and end stage renal disease. Liddle's disease represents a specific hypertensive disease and expresses itself in the human population as an autosomal dominant trait. Recent experimental evidence indicates that patients with Liddle's disease have constituitively active amiloride-sensitive Na+ channels, and that these channels are phenotypically expressed in lymphocytes obtained from normal and affected members of the original Liddle's kindred. Linkage analysis indicates that this disease results from a deletion of the C-terminal region of the [beta]-subunit of a recently cloned epithelial Na+ channel (ENaC). We report the successful immunopurification and reconstitution of both normal and constituitively active lymphocyte Na+ channels into planar lipid bilayers. These channels display all of the characteristics typical of renal Na+ channels, including sensitivity to protein kinase A phosphorylation. We demonstrate that gating of normal Na+ channels is removed by cytoplasmic trypsin digestion, and that the constituitively active Liddle's Na+ channels are blocked by a [beta]- or [delta]-ENaC carboxy-terminal peptide in a GTP-dependent fashion.

Received 17 March 1995; accepted in final form 20 June 1995.
APS Manuscript Number C153-5.
Article publication pending Am. J. Physiol. (Cell Physiology).
ISSN 1080-4757 Copyright 1995 The American Physiological Society.
Published in APStracts on 11 July 1995.