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Published ahead of print on January 27, 2005, doi:10.1165/rcmb.2004-0302OC

Am. J. Respir. Cell Mol. Biol., Volume 32, Number 5, May 2005, 462-469

A more recent version of this article appeared on May 1, 2005
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Submitted on September 23, 2004
Revised on January 27, 2005

Regulated H2O2 Production By Duox in Human Airway Epithelial Cells

Radia Forteza1, Matthias Salathe2, Francoise Miot3, Rosanna Forteza2, and Gregory E Conner4*

1 Department of Cell Biology and Anatomy, University of Miami School of Medicine, Miami, FL, USA, 2 Division of Pulmonary and Critical Care Medicine, University of Miami School of Medicine, Miami, FL, USA, 3 IRIBHM, Faculte de Medecine, Universite Libre de Bruxelles, Bruxelles, Belgium, 4 Division of Pulmonary and Critical Care Medicine, University of Miami School of Medicine, Miami, FL, USA; Department of Cell Biology and Anatomy, University of Miami School of Medicine, Miami, FL, USA

* To whom correspondence should be addressed. E-mail: gconner{at}miami.edu.

Hydrogen Peroxide (H2O2) is found in exhaled breath and is produced by airway epithelia. In addition, H2O2 is a necessary substrate for the airway lactoperoxidase (LPO) antiinfection system. To investigate the source of H2O2 produced by airway epithelia, PCR was used to screen NADPH oxidase expression in human airway epithelia re-differentiated at the air liquid interface (ALI) and demonstrated the presence of Duox1 and 2. Western blots of culture extracts indicated strong expression of Duox and immunohistochemistry of human tracheal sections localized the protein to the apical portion of epithelial cells. Apical H2O2 production was stimulated by 100 µM ATP or 1 µM thapsigargin but not 100 µM ADP. Diphenyleneiodonium, an NADPH inhibitor, and dimethylthiourea, a reactive oxygen species scavenger both inhibited this stimulation. ATP did not stimulate the basolateral H2O2 production by ALI cultures. ATP and thapsigargin increased intracellular Ca2+ with kinetics similar to increasing H2O2 production and thus, consistent with the expected Ca2+ sensitivity of Duox. These data suggest that Duox is the major NADPH oxidase expressed in airway epithelia and therefore a contributor of H2O2 production in the airway lumen. Additionally, the data suggest that extracellular H2O2 production may be regulated by stimuli that raise intracellular Ca2+.




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