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- W1964002260 abstract "Nuclear factor κB regulates various genes involved in the immune response, inflammation, cell survival, and development. NF-κB activation is controlled by proteins possessing ankyrin repeats, such as IκBs. A precursor of the NF-κB2 (p52) subunit, p100, contains ankyrin repeats in its C-terminal portion and has been found to act as a cytoplasmic inhibitor of RelA in the canonical pathway of NF-κB activation. Here, we demonstrate that p100 also suppresses c-Rel function in dendritic cells. Expression of the p19 and p40 subunits of IL-23, a c-Rel-dependent cytokine, was enhanced in p100-deficient cells, although expression of a RelA-dependent cytokine, TNF-α, was reduced. Nuclear translocation of c-Rel was enhanced in p100-deficient cells. p100, and not the processed p52 form, associated with c-Rel in the steady state and dissociated immediately after lipopolysaccharide stimulation in wild-type dendritic cells. Four hours after the stimulation, p100 was newly synthesized and associated with c-Rel again. In cells expressing both c-Rel and RelA, c-Rel is preferentially suppressed by p100." @default.
- W1964002260 created "2016-06-24" @default.
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- W1964002260 date "2014-10-01" @default.
- W1964002260 modified "2023-09-26" @default.
- W1964002260 title "p100, a precursor of NF-κB2, inhibits c-Rel and reduces the expression of IL-23 in dendritic cells" @default.
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- W1964002260 doi "https://doi.org/10.1016/j.bbrc.2014.09.143" @default.
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