J Physiol Volume 559, Number 3, 715-720, September 15, 2004 DOI: 10.1113/jphysiol.2004.069971
An amiloride-sensitive H+-gated Na+ channel in Caenorhabditis elegans body wall muscle cells
Maëlle Jospin and
Bruno Allard
Physiologie Intégrative, Cellulaire et Moléculaire, UMR CNRS 5123, Université C. Bernard Lyon I, 43 bd du 11 Novembre 1918, 69622 Villeurbanne cedex, France
About 30 genes are predicted to encode degenerin/epithelial sodium channels (DEG/ENaCs) in Caenorhabditis elegans but the gating mode of these channels has not been determined. Using the whole-cell configuration of the patch-clamp technique in acutely dissected C. elegans, we investigated the effects of H+ as a potential activating factor of DEG/ENaCs on electrical properties of body wall muscle cells. Under current-clamp conditions, decreasing external pH from 7.2 to 6.1 led to a reversible depolarization of muscle cells associated with a decrease in input resistance which was partially inhibited by amiloride. Under voltage-clamp conditions, extracellular acidification activated an inward desensitizing current at –60 mV. In the absence of external Ca2+, H+-gated channels were found to be slightly more permeable to Na+ than to K+ and were blocked by amiloride with a K0.5 of 31 µM at –60 mV. An inward current could be also activated by protons in a GABA receptor null mutant in the presence of D-tubocurare and in an unc-105 null mutant. These results demonstrate that ion channels sharing common properties with mammalian acid-sensing ion channels (ASICs) are functional in C. elegans muscle which should prove useful for understanding proton sensing in animals.
(Received 14 June 2004;
accepted after revision 9 July 2004;
first published online 14 July 2004)
Corresponding author B. Allard: Physiologie Intégrative, Cellulaire et Moléculaire, UMR CNRS 5123, Université C. Bernard Lyon I, 43 bd du 11 Novembre 1918, 69622 Villeurbanne cedex, France. Email: bruno.allard{at}univ-lyon1.fr
Copyright © 2004 The Physiological Society.
