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Peroxiredoxin 6 as an antioxidant enzyme: Protection of lung alveolar epithelial type II cells from H 2 O 2 ‐induced oxidative stress
Author(s) -
Wang Yan,
Feinstein Sheldon I.,
Fisher Aron B.
Publication year - 2008
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21703
Subject(s) - propidium iodide , annexin , tunel assay , microbiology and biotechnology , oxidative stress , chemistry , antioxidant , lipid peroxidation , fragmentation (computing) , apoptosis , dna fragmentation , cytotoxicity , biochemistry , programmed cell death , biology , in vitro , ecology
We evaluated the antioxidant role of peroxiredoxin 6 (Prdx6) in primary lung alveolar epithelial type II cells (AEC II) that were isolated from wild type (WT), Prdx6−/−, or Prdx6 transgenic (Tg) overexpressing mice and exposed to H 2 O 2 at 50–500 µM for 1–24 h. Expression of Prdx6 in Tg AEC II was sevenfold greater than WT. Prdx6 null AEC II exposed to H 2 O 2 showed concentration‐dependent cytotoxicity indicated by decreased “live/dead” cell ratio, increased propidium iodide (PI) staining, increased annexin V binding, increased DNA fragmentation by TUNEL assay, and increased lipid peroxidation by diphenylpyrenylphosphine (DPPP) fluorescence. Compared to Prdx6 null cells, oxidant‐mediated damage was significantly less in WT AEC II and was least in Prdx6 Tg cells. Thus, Prdx6 functions as an antioxidant enzyme in mouse AEC II. Prdx6 has been shown previously to reduce phospholipid hydroperoxides and we postulate that this activity is a major mechanism for the effectiveness of Prdx6 as an antioxidant enzyme. J. Cell. Biochem. 104: 1274–1285, 2008. © 2008 Wiley‐Liss, Inc.