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| http://purl.uniprot.org/citations/12672265 | http://www.w3.org/2000/01/rdf-schema#comment | "The glucocorticoid receptor (GR) acts as an anti-inflammatory factor. To a large extent, this activity is exerted by the interference of pro-inflammatory nuclear factor kappa B (NF-kappa B) activity. In their respective inactive forms, both GR and NF-kappa B reside in the cytoplasm and translocate to the nucleus on relevant stimulation. Previously, p65, a component of the NF-kappa B complex, and GR have been shown to interact physically in vitro, and the interaction is assumed to take place in the nucleus of cells [McKay and Cidlowski (1999) Endocrine Rev. 20, 435-459]. We have studied the interaction between GR and NF-kappa B using in vivo -like conditions. Using immunoaffinity chromatography or immunoprecipitation, combined with Western blotting, we observed that, with endogenous protein levels in cytosolic extracts of rat liver and of H4-II-E-C3 hepatoma cells and in contrast with the current belief, p65, p50 and inhibitory kappa B alpha complex interact with GR, even in the absence of glucocorticoid or an inflammatory signal. The interaction between non-liganded/non-activated GR and p65/p50 has also been verified by both p65 and p50 co-immunoprecipitations. Intracellular localization studies, using Western blotting, revealed that glucocorticoids can decrease tumour necrosis factor alpha (TNFalpha)-induced nuclear entry of p65, whereas glucocorticoid-induced GR translocation was much less affected by TNFalpha. We were also able to demonstrate a nuclear interaction of GR and p65 and p50 using in vivo -like protein concentrations. Furthermore, nuclear GR interaction with heat-shock protein 90 was enhanced distinctly by TNFalpha treatment. In conclusion, our studies suggest a strong interconnectivity between the NF-kappa B and GR-signalling pathways where also, somewhat unexpectedly, a physical interaction in the cytosol constitutes an integral part of GR-NF-kappa B cross-talk."xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20030175"xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/author | "Gustafsson J.A."xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/author | "Widen C."xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/author | "Wikstrom A.C."xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/pages | "211-220"xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/title | "Cytosolic glucocorticoid receptor interaction with nuclear factor-kappa B proteins in rat liver cells."xsd:string |
| http://purl.uniprot.org/citations/12672265 | http://purl.uniprot.org/core/volume | "373"xsd:string |
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