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MALP-2 stimulates translocation of Nrf2 to the nucleus and binding to HO-1 ARE in THP-1 cells.

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posted on 2014-07-31, 03:00 authored by Xiaoxing You, Liangzhuan Liu, Yanhua Zeng, Ranhui Li, Jun He, Xiaohua Ma, Chuanhao Jiang, Cuiming Zhu, Liesong Chen, Minjun Yu, Guangli Ou, Yimou Wu

A. Immunofluorescence images of THP-1 cells pretreated with or without LY294002 (25 µM) and MyD88 siRNA in the presence of MALP-2 (5 ng/ml) for 2 h. Cells were fixed and then stained with 4′-6-diamidino-2-phenylindole or anti-Nrf2 antibody, followed by incubation with cy3-conjugated anti-rabbit antibody. Images were obtained using a confocal microscope. B. EMSA was performed using MALP-2-stimulated nuclear THP-1 extracts and biotinylated HO-1-ARE probe. The specificity of Nrf2 was verified by competition analysis with an excess of nonlabeled specific (cold probe) or nonspecific (NF-κB probe) oligonucleotide probe. For supershift analysis, nuclear extracts from MALP-2-treated THP-1 cells were preincubated with 1 µg anti-Nrf2 supershift antibody before EMSA.

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