The Promoter Context Determines Mutual Repression or Synergism between NF-κB and the Glucocorticoid Receptor
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Abstract
While the biochemical mechanisms mediating repression of NFκB activity by glucocorticoids (GCs) are relatively well studied, the role of promoter architecture for the effects of GCs on NFκB remains poorly characterized. Therefore we constructed a set of synthetic promoter reporter constructs containing various numbers of GCresponsive elements (GREs) in distinct distances to NFκB binding sites. TNFαinduced activity of a synthetic promoter controlled by three NFκB binding sites was repressed by dexamethasone. The presence of only one GRE in the vicinity of the κB sites abolished this repression and allowed synergistic transcriptional activation by NFκB and the glucocorticoid receptor (GR). The synergism identified here was not affected by the number of GREs, but strictly depends on the spacing between GREs and κB sites. These experiments reveal that the functional interplay between NFκB and the GR also involves dependent on the promoter context synergistic stimulation of transcription.
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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- Expression of the Tissue Kallikrein-Kinin Cascade in Granulosa Cells of the Ovary
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- Tyrosinase-Mediated Oxidation of Acetaminophen to 4-Acetamido-o- Benzoquinone
- Properties of Baculovirus Particles Displaying GFP Analyzed by Fluorescence Correlation Spectroscopy
- The Promoter Context Determines Mutual Repression or Synergism between NF-κB and the Glucocorticoid Receptor
- Expression of Hepatocyte Growth Factor Activator Inhibitor Type 2 (HAI-2) in Human Testis: Identification of a Distinct Transcription Start Site for the HAI-2 Gene in Testis
- Identification and Characterization of an IgG Binding Protein in the Secretion of the Rat Coagulating Gland
- Characterization of Different Reactive Lysines in Bovine Heart Mitochondrial Porin
- Determination of the mRNA Sequence of Cathepsin Y, a Cysteine Endopeptidase from Rat Spleen, and Confirmation of Its Ubiquitous
- Acknowledgement
- Content Index
- Author Index
- Subject Index
Articles in the same Issue
- Processing and Activation of Lysosomal Proteinases
- Evidence That E-Box Promoter Elements and MyoD Transcription Factors Play a Role in the Induction of Cathepsin B Gene Expression during Human Myoblast Differentiation
- Transcription Factor Egr-1 Activates Collagen Expression in Immortalized Fibroblasts or Fibrosarcoma Cells
- The Receptor-Bound N-Terminal Ectodomain of the Amyloid Precursor Protein Is Associated with Membrane Rafts
- Evaluation of Similarities in the cis/trans Isomerase Function of Trigger Factor and DnaK
- The Chloroplast Import Receptor Toc34 Functions as Preprotein-Regulated GTPase
- cis-4-Methylsphingosine Phosphate Induces Apoptosis in Neuroblastoma Cells by Opposite Effects on p38 and ERK Mitogen-Activated Protein Kinases
- Evidence for the Involvement of the Unique C-Tail of S100A9 in the Binding of Arachidonic Acid to the Heterocomplex S100A8/A9
- The Primary Structure of Three Hemoglobin Chains from the Indigo Snake (Drymarchon corais erebennus, Serpentes): First Evidence for αD Chains and Two β Chain Types in Snakes
- Expression of the Tissue Kallikrein-Kinin Cascade in Granulosa Cells of the Ovary
- Chondroitin Sulfate Proteoglycan Is a Potent Enhancer in the Processing of Procathepsin L
- Tyrosinase-Mediated Oxidation of Acetaminophen to 4-Acetamido-o- Benzoquinone
- Properties of Baculovirus Particles Displaying GFP Analyzed by Fluorescence Correlation Spectroscopy
- The Promoter Context Determines Mutual Repression or Synergism between NF-κB and the Glucocorticoid Receptor
- Expression of Hepatocyte Growth Factor Activator Inhibitor Type 2 (HAI-2) in Human Testis: Identification of a Distinct Transcription Start Site for the HAI-2 Gene in Testis
- Identification and Characterization of an IgG Binding Protein in the Secretion of the Rat Coagulating Gland
- Characterization of Different Reactive Lysines in Bovine Heart Mitochondrial Porin
- Determination of the mRNA Sequence of Cathepsin Y, a Cysteine Endopeptidase from Rat Spleen, and Confirmation of Its Ubiquitous
- Acknowledgement
- Content Index
- Author Index
- Subject Index