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Am J Physiol Lung Cell Mol Physiol (December 30, 2004). doi:10.1152/ajplung.00432.2004
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Submitted on November 18, 2004
Accepted on December 27, 2004

Variable over-oxidation of peroxiredoxins in human lung cells in severe oxidative stress

Siri T. Lehtonen1, Piia M.H. Markkanen1, Mirva Peltoniemi1, Sang Won Kang2, and Vuokko L. Kinnula3*

1 Department of Internal Medicine, University of Oulu and Oulu University Hospital, Oulu, Finland
2 Center for Cell Signaling Research, Ewha Womans University, Seoul, Korea, Republic of
3 Department of Medicine, Pulmonary Division, University of Helsinki and Helsinki University Hospital, Helsinki, Finland

* To whom correspondence should be addressed. E-mail: vuokko.kinnula{at}helsinki.fi.

Peroxiredoxins (Prxs) are a group of thiol containing proteins that participate both in signal transduction and in the breakdown of hydrogen peroxide (H2O2) during oxidative stress. Six distinct Prxs have been characterised in human cells (Prxs I-VI). Prxs I-IV form dimers held together by disulphide bonds, Prx V forms intramolecular bond, but the mechanism of Prx VI, so called 1-cys Prx, is still unclear. Here we describe the regulation of all six Prxs in cultured human lung A549 and BEAS2B cells. The cells were exposed to variable concentrations of H2O2, menadione, tumor necrosis factor {alpha} or transforming growth factor {beta}. To evoke glutathione depletion the cells were furthermore treated with buthionine sulfomixine. Only high concentrations (300 µM) of H2O2 caused a minor increase (<28%, 4h) in the expression of Prxs I, IV and VI. Severe oxidant stress (250-500 µM H2O2) caused a significant increase in the proportion of the monomeric forms of Prxs I-IV, this was reversible at lower H2O2 concentrations (≤250 µM). This recovery of Prx overoxidation differed among the various Prxs, Prx I was recovered within 24 hours but recovery required 48 hours for Prx III. Overall Prxs are not significantly modulated by mild oxidant stress or cytokines, but there is variable, though reversible, overoxidation in these proteins during severe oxidant exposure.




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