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http://purl.uniprot.org/citations/11381138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11381138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11381138http://www.w3.org/2000/01/rdf-schema#comment"Inflammatory responses in many cell types are coordinately regulated by the opposing actions of NF-kappaB and the glucocorticoid receptor (GR). The human glucocorticoid receptor (hGR) gene encodes two protein isoforms: a cytoplasmic alpha form (GRalpha), which binds hormone, translocates to the nucleus, and regulates gene transcription, and a nuclear localized beta isoform (GRbeta), which does not bind known ligands and attenuates GRalpha action. We report here the identification of a tumor necrosis factor (TNF)-responsive NF-kappaB DNA binding site 5' to the hGR promoter that leads to a 1.5-fold increase in GRalpha mRNA and a 2.0-fold increase in GRbeta mRNA in HeLaS3 cells, which endogenously express both GR isoforms. However, TNF-alpha treatment disproportionately increased the steady-state levels of the GRbeta protein isoform over GRalpha, making GRbeta the predominant endogenous receptor isoform. Similar results were observed following treatment of human CEMC7 lymphoid cells with TNF-alpha or IL-1. The increase in GRbeta protein expression correlated with the development of glucocorticoid resistance."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.org/dc/terms/identifier"doi:10.1073/pnas.121455098"xsd:string
http://purl.uniprot.org/citations/11381138http://purl.org/dc/terms/identifier"doi:10.1073/pnas.121455098"xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Oakley R.H."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Oakley R.H."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Cidlowski J.A."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Cidlowski J.A."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Jewell C.M."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Jewell C.M."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Webster J.C."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/author"Webster J.C."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/pages"6865-6870"xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/pages"6865-6870"xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/title"Proinflammatory cytokines regulate human glucocorticoid receptor gene expression and lead to the accumulation of the dominant negative beta isoform: a mechanism for the generation of glucocorticoid resistance."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/title"Proinflammatory cytokines regulate human glucocorticoid receptor gene expression and lead to the accumulation of the dominant negative beta isoform: a mechanism for the generation of glucocorticoid resistance."xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/volume"98"xsd:string
http://purl.uniprot.org/citations/11381138http://purl.uniprot.org/core/volume"98"xsd:string
http://purl.uniprot.org/citations/11381138http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11381138
http://purl.uniprot.org/citations/11381138http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11381138