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- W2912273350 abstract "Peroxiredoxin 6 (Prdx6) can reduce lipid hydroperoxides by a unique mechanism employing a single conserved cysteine and also acts as a phospholipase A2. It is highly expressed in lung, both protecting against oxidative stress and regulating pulmonary surfactant phospholipid metabolism. We reported previously that rodent Prdx6 is up-regulated in development and by oxidative stress. A 1524 base pair fragment of proximal upstream DNA from the human Prdx6 gene was cloned into the pSEAP-2 reporter vector (BD Bioscience). Transient transfection of this construct into lung cell lines resulted in measurable production of secreted alkaline phosphatase that was increased 3-4 fold by keratinocyte growth factor (KGF) treatment. β-galactosidase expressed from a co-transfected plasmid was used as a control for transfection efficiency. Using promoter deletions and then site-directed deletion mutagenesis, a consensus Antioxidant Response Element (ARE), located between 357 and 349 nucleotides before the transcriptional start was identified. This element was important in basal and KGF-induced expression in both A549 cells and primary rat alveolar type II cells. We have previously shown that this ARE controls the Prdx6 response to H2O2 treatment. We conclude that KGF and antioxidants, both activate transcription through the ARE, and may act through Nrf2, a transcription factor known to bind to the ARE. [HL P01-75587]." @default.
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- W2912273350 date "2009-04-01" @default.
- W2912273350 modified "2023-10-16" @default.
- W2912273350 title "Human Peroxiredoxin 6 (Prdx6) gene expression is regulated by keratinocyte growth factor (KGF) through the same antioxidant response element (ARE) that controls its response to oxidative stress" @default.
- W2912273350 doi "https://doi.org/10.1096/fasebj.23.1_supplement.617.13" @default.
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