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J. Biol. Chem., Vol. 279, Issue 35, 36454-36461, August 27, 2004

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NADPH Oxidase-dependent Acid Production in Airway Epithelial Cells^*

Christian Schwarzer¶, Terry E. Machen, Beate Illek, and Horst Fischer||

From the Children's Hospital Oakland Research Institute, Oakland, California 94609 and the Department of Molecular and Cell Biology, University of California, Berkeley, California 94720

The purpose of this study was to determine the role of NADPH oxidase in H⁺ secretion by airway epithelia. In whole cell patch clamp recordings primary human tracheal epithelial cells (hTE) and the human serous gland cell line Calu-3 expressed a functionally similar zincblockable plasma membrane H⁺ conductance. However, the rate of H⁺ secretion of confluent epithelial monolayers measured in Ussing chambers was 9-fold larger in hTE compared with Calu-3. In hTE H⁺ secretion was blocked by mucosal ZnCl₂ and the NADPH oxidase blockers acetovanillone and 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), whereas these same blockers had no effect in Calu-3. We determined levels of transcripts for the NADPH oxidase transmembrane isoforms (Nox1 through -5, Duox1 and -2, and p22^phox) and found Duox1, -2, and p22^phox to be highly expressed in hTE, as well as the intracellular subunits p40^phox, p47^phox, and p67^phox. In contrast, Calu-3 lacked transcripts for Duox1, p40^phox, and p47^phox. Anti-Duox antibody staining resulted in prominent apical staining in hTE but no significant staining in Calu-3. When treated with amiloride to block the Na⁺/H⁺ exchanger, intracellular pH in hTE acidified at significantly higher rates than in Calu-3, and treatment with AEBSF blocked acidification. These data suggest a role for an apically located Duox-based NADPH oxidase during intracellular H⁺ production and H⁺ secretion, but not in H⁺ conduction.

Received for publication, May 5, 2004 , and in revised form, June 14, 2004.

^* This work was supported in part by National Institutes of Health Grants HL071829, DK51799, and 1P50HL60288 and a Pilot and Feasibility Grant by the Cystic Fibrosis Foundation (Grant FISCHE02I0). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Recipient of an Elizabeth Nash Memorial Fellowship from Cystic Fibrosis Research, Inc.

^|| To whom correspondence should be addressed: Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland CA 94609. Tel.: 510-450-7696; Fax: 510-450-7910; E-mail hfischer{at}chori.org.

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