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Oxidative Inactivation of Peroxiredoxin Isoforms by H2O2 in Pulmonary Epithelial, Macrophage, and other Cell Lines with their Subsequent Regeneration

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dc.contributor.author오, 윤정-
dc.contributor.author김, 영선-
dc.contributor.author최, 영인-
dc.contributor.author신, 승수-
dc.contributor.author박, 주헌-
dc.contributor.author최, 영화-
dc.contributor.author박, 광주-
dc.contributor.author박, 래웅-
dc.contributor.author황, 성철-
dc.description.abstractBackground : Peroxiredoxins (Prxs) are a relatively newly recognized, novel family of peroxidases that reduce H2O2 and alkylhydroperoxide into water and alcohol, respectively. There are 6 known isoforms of Prxs present in human cells. Normally, Prxs exist in a head-to-tail homodimeric state in a reduced form. However, in the presence of excess H2O2, it can be oxidized on its catalytically active cysteine site into inactive oxidized forms. This study surveyed the types of the Prx isoforms present in the pulmonary epithelial, macrophage, endothelial, and other cell lines and observed their response to oxidative stress.

Materials and Methods : This study examined the effect of exogenous, excess H2O2 on the Prxs of established cell lines originating from the pulmonary epithelium, macrophages, and other cell lines, which are known to be exposed to high oxygen partial pressures or are believed to be subject to frequent oxidative stress, using non-reducing SDS polyacrylamide electrophoresis (PAGE) and 2 dimensional electrophoresis.

Results : The addition of excess H2O2 to the culture media of the various cell-lines caused the immediate inactivation of Prxs, as evidenced by their inability to form dimers by a disulfide cross linkage. This was detected as a subsequent shift to its monomeric forms on the non-reducing SDS PAGE. These findings were further confirmed by 2 dimensional electrophoresis and immunoblot analysis by a shift toward a more acidic isoelectric point (pI). However, the subsequent reappearance of the dimeric Prxs with a comparable, corresponding decrease in the monomeric bands was noted on the non-reducing SDS PAGE as early as 30 minutes after the H2O2 treatment suggesting regeneration after oxidation. The regenerated dimers can again be converted to the inactivated form by a repeated H2O2 treatment, indicating that the protein is still catalytically active. The recovery of Prxs to the original dimeric state was not inhibited by a pre-treatment with cycloheximide, nor by a pretreatment with inhibitors of protein synthesis, which suggests that the reappearance of dimers occurs via a regeneration process rather than via the de novo synthesis of the active protein.

Conclusion : The cells, in general, appeared to be equipped with an established system for regenerating inactivated Prxs, and this system may function as a molecular “on-off switch” in various oxidative signal transduction processes. The same mechanisms might applicable other proteins associated with signal transduction where the active catalytic site cysteines exist.
dc.titleOxidative Inactivation of Peroxiredoxin Isoforms by H2O2 in Pulmonary Epithelial, Macrophage, and other Cell Lines with their Subsequent Regeneration-
dc.title.alternative대식세포를 비롯한 각종 세포주에서 H2O2에 의한 Peroxiredoxin 동위효소들의 산화에 따른 불활성화와 재생-
dc.subject.keywordPulmonary epithelium-
dc.subject.keywordCysteine Oxidation-
dc.type.localJournal Papers-
dc.citation.titleTuberculosis and respiratory diseases-
dc.identifier.bibliographicCitationTuberculosis and respiratory diseases, 58(1):31-42, 2005-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pulmonary & Critical Care Medicine
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