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Articles in PresS, published online ahead of print June 5, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00398.2001
Submitted on October 11, 2001
Accepted on May 23, 2002
1 Department of Pediatrics, Duke University Medical Center, Durham, NC, USA
2 Center for Environmental Medicine and Lung Biology, University of North Carolina, Chapel Hill, NC, USA
3 National Health and Environmental Effects Research Laboratory, Environmental Protection Agency, Research Triangle Park, NC, USA
4 Department of Internal Medicine, Duke University Medical Center, Durham, NC, USA
* To whom correspondence should be addressed. E-mail: turi0002{at}mc.duke.edu.
Anion exchange protein 2 (AE2) is a membrane bound protein that mediates chloride-bicarbonate exchange. In addition to regulating intracellular pH and cell volume, AE2 exports superoxide (O2.-) to the extracellular matrix in a HCO3--dependent process. Given this ability to export O2.-, we hypothesized that the expression of AE2 in the lung is regulated by oxidative stress. AE2 mRNA and protein expression were measured by RT-PCR and Western blot analysis, respectively, in differentiated human bronchial epithelial cells exposed to H2O2 (100µM). Alterations in in vivo AE2 protein expression were evaluated in lung tissue of rats exposed to 70% O2. The role of transcription factor AP-1 in oxidant regulation of AE2 was evaluated by EMSA and by immunoblotting of nuclear phospho-c-jun. Results show increased AE2 mRNA and protein expression after oxidant exposure. This was preceded by a transient increase in DNA binding of AE2-specific AP-1 and phosphorylation of c-jun. This study demonstrates that AE2 expression is regulated by oxidative stress in airway epithelial cells and that this regulation correlates with activation of AP-1.
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