HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 288/5/L997    most recent 00432.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (10) Citing Articles via Google Scholar Google Scholar Articles by Lehtonen, S. T. Articles by Kinnula, V. L. Search for Related Content PubMed PubMed Citation Articles by Lehtonen, S. T. Articles by Kinnula, V. L.

INNOVATIVE METHODOLOGY

Variable overoxidation of peroxiredoxins in human lung cells in severe oxidative stress

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

Submitted 18 November 2004 ; accepted in final form 27 December 2004

ABSTRACT

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 characterized in human cells (Prxs I–VI). Prxs I–IV form dimers held together by disulfide 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 BEAS-2B cells. The cells were exposed to variable concentrations of H₂O₂, menadione, tumor necrosis factor- or transforming growth factor-. To evoke glutathione depletion, the cells were furthermore treated with buthionine sulfoximine. Only high concentrations (300 µM) of H₂O₂ caused a minor increase (<28%, 4 h) 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 h, but recovery required 48 h 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.

peroxiredoxin; lung; oxidant; antioxidant; hydrogen peroxide

This article has been cited by other articles:

				E. Kipnis, K. Hansen, T. Sawa, K. Moriyama, A. Zurawel, A. Ishizaka, and J. Wiener-Kronish Proteomic Analysis of Undiluted Lung Epithelial Lining Fluid Chest, August 1, 2008; 134(2): 338 - 345. [Abstract] [Full Text] [PDF]

				M. P. Smit-de Vries, M. van der Toorn, R. Bischoff, and H. F. Kauffman Resistance of quiescent and proliferating airway epithelial cells to H2O2 challenge Eur. Respir. J., April 1, 2007; 29(4): 633 - 642. [Abstract] [Full Text] [PDF]