RT PCR detection of human bladder epithelial cell expression of dual-function oxidase_0.doc

RT PCR detection of human bladder epithelial cell expression of dual-function oxidase_0.doc

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RT PCR detection of human bladder epithelial cell expression of dual-function oxidase_0

 PAGE \* MERGEFORMAT 10 RT PCR detection of human bladder epithelial cell expression of dual-function oxidase Of: Gengkuai Zhen Liu Zhen Liu Yanxiang Liu Yan Jun Zhao Ning Huang Wu Qi Wang Boyao [Abstract] Objective: detection of human bladder epithelial cells (T24 cells) whether the expression of dual-function oxidase (Duox 1, Duox 2), and observe the inflammatory cytokines and phorbol ester (PMA) on gene expression. Methods: In vitro cultured human bladder epithelial (T24) cells by phorbol ester (PMA), inflammatory cytokines (TNF @, and IFN γ) after stimulation of total extracted RNA, using semi-quantitative RT PCR to observe the cell Duox 1, Duox 2 mRNA expression levels . Results: Duox 1, Duox 2 mRNA in T24 cells constitutively expressed in phorbol ester (PMA), TNF @ and the effect of IFN γ, Duox 2 gene expression was significantly increased, while Duox 1 no significant changes in gene expression . Conclusion: Dual function oxidase Duox 1 and Duox 2 gene expression in bladder epithelial cells, and by the impact of inflammation, bladder epithelial cells in the physiological functions deserves further research. [Keywords:] bladder epithelial cells; dual function oxidase; gene expression Phagocyte NADPH oxidase is activated, the cell respiratory burst, resulting in a large number of reactive oxygen species (ROS), as an important component of cell kill microorganisms .2000 after the discovery in non-phagocytic cells NADPH oxidase homologue family was named the NOX (NADPH oxidase) family. There are seven human NOX family members, that NOX1, NOX2, NOX3, NOX4, NOX5, Duox 1 and Duox 2 [1-3]. NOX family of widely expressed in body tissues and organs, its biological function as a research focus. dual-function oxidase (Duox 1 and Duox 2) originally found in the thyroid gland, which in addition to the C-terminal with extraterritorial NOX, there is an N terminal extracellular peroxidase-like domain, so called dual-function oxidase. In recent years, respirato

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