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Originally published In Press as doi:10.1074/jbc.M109465200 on December 17, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8395-8405, March 8, 2002
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Up-regulation of Acid-gated Na+ Channels (ASICs) by Cystic Fibrosis Transmembrane Conductance Regulator Co-expression in Xenopus Oocytes*

Hong-Long JiDagger , Biljana JovovDagger , Jian FuDagger §, LaToya R. BishopDagger , Hannah C. MebaneDagger , Catherine M. FullerDagger , Bruce A. Stanton, and Dale J. BenosDagger ||

From the Dagger  Department of Physiology and Biophysics, University of Alabama, Birmingham, Alabama 35294 and  Department of Physiology, Dartmouth Medical School, Hanover, New Hampshire 03755

Cystic fibrosis transmembrane conductance regulator (CFTR) functions as both a chloride channel and an epithelial transport regulator, interacting with Na+ (epithelial sodium channel), Cl-, renal outer medullary potassium channel+, and H2O channels and some exchangers (i.e. Na+/H+) and co-transporters (Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>, Na+-K+-2Cl-). Acid-sensitive ion channels (ASICs), members of the epithelial sodium channel/degenerin superfamily, were originally cloned from neuronal tissue, and recently localized in epithelia. Because CFTR has been immunocytochemically and functionally identified in rat, murine, and human brain, the regulation of ASICs by CFTR was tested in oocytes. Our observations show that the proton-gated Na+ current formed by the heteromultimeric ASIC1a/2a channel was up-regulated by wild type but not by Delta F508-CFTR. In contrast, the acid-gated Na+ current associated with either the homomultimeric ASIC1a or ASIC2a channel was not influenced by wild type CFTR. The apparent equilibrium dissociation constant for extracellular Na+ for ASIC1a/2a was increased by CFTR, but CFTR had no effect on the gating behavior or acid sensitivity of ASIC1a/2a. CFTR had no effect on the pH activation of ASIC1a/2a. We conclude that wild type CFTR elevates the acid-gated Na+ current of ASIC1a/2a in part by altering the kinetics of extracellular Na+ interaction.

* This study was supported by National Institutes of Health Grants DK53468, DK56095, and DK34533 and the Cystic Fibrosis Foundation.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.

§ Present address: Dept. of Pharmacology, University of Washington, Seattle, WA 98195.

|| To whom correspondence should be addressed: Dept. of Physiology and Biophysics, The University of Alabama at Birmingham, 1918 University Blvd., MCLM 704, Birmingham, AL 35294-0005. Tel.: 205-934-6220; Fax: 205-934-2377; E-mail: benos@physiology.uab.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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