| First Author | Mise-Omata S | Year | 2014 |
| Journal | Biochem Biophys Res Commun | Volume | 453 |
| Issue | 3 | Pages | 332-7 |
| PubMed ID | 25305492 | Mgi Jnum | J:220199 |
| Mgi Id | MGI:5632454 | Doi | 10.1016/j.bbrc.2014.09.143 |
| Citation | Mise-Omata S, et al. (2014) p100, a precursor of NF-kappaB2, inhibits c-Rel and reduces the expression of IL-23 in dendritic cells. Biochem Biophys Res Commun 453(3):332-7 |
| abstractText | Nuclear factor kappaB regulates various genes involved in the immune response, inflammation, cell survival, and development. NF-kappaB activation is controlled by proteins possessing ankyrin repeats, such as IkappaBs. A precursor of the NF-kappaB2 (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-kappaB 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-alpha, 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. |
