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- W5136333 abstract "Purpose of Study: ERp57 is an ER chaperone protein with protein disulfide isomerase activity. Our previous studies have demonstrated that hyperoxia down-regulates ERp57 protein expression in the neonatal rat lung. In this study, we tested whether over-expression of ERp57 in lung epithelial cells would reduce hyperoxia-induced ER stress. Methods: Human ERp57 cDNA was subcloned into pcDNA3 plasmid and then transfected into A549 lung epithelial cells. ERp57 over-expressing cells (ERp57-A549) were selected by G418 and used for the experiments. Hyperoxia treatment for cultured cells was carried out in a chamber flushed with 95% O2 and 5% CO2. Results: We found that prolonged hyperoxic treatment for 24, 48 and 72 hours significantly increased phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF2α), one of the known ER stress markers, in A549 cells. However, ERp57 over-expression decreased hyperoxia-induced eIF2α phosphorylation in ERp57-A549 cells. In addition, over-expression of human ERp57 decreased reactive oxygen species (ROS) production caused by hyperoxia, suggesting that ERp57 may be involved in regulation of cellular redox. Conclusions: Our results reveal that hyperoxia induces eIF2α phosphorylation and ER stress. Over-expression of ERp57 in human lung epithelial cells reduces ROS generation and ER stress under hyperoxic condition." @default.
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- W5136333 date "2007-01-01" @default.
- W5136333 modified "2023-09-27" @default.
- W5136333 title "ERp57, an Endoplasmic Reticulum (ER) Protein, Reduces Hyperoxia‐Induced ER Stress in Lung Epithelial Cells" @default.
- W5136333 doi "https://doi.org/10.1096/fasebj.21.6.a818" @default.
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