Regulation of subcellular trafficking of the glucocorticoid receptor.
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概要
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Glucocorticoids are not only essential hormones to maintain homeostasis but also effective drugs for controlling inflammatory disorders. Glucocorticoids inhibit expression of proinflammatory genes such as cytokines, chemokines, and adhesion molecules. The actions of glucocorticoids are mediated by the glucocorticoid receptor (GR) . The GR is localized in the cytoplasm in the absence of hormonal ligand. Upon binding ligand, the GR dissociates from molecular chaperones such as heat shock proteins and translocates into the nucleus. The GR interacts with other transcription factors such as NF-κB and AP-1 which activate proinflammatory genes and inhibits inflammation through negative regulation of these transcription factors and/or competition with these transcription factors for association with coactivators. Therefore, nuclear translocation of the GR is an important step for glucocorticoid action and is controlled by nuclear localization signals within the GR molecule and various cellular factors. It is suggested that cellular oxidation-reduction (redox) status also regulates nuclear translocation of GR by targeting the cysteine within the NL1. We demonstrated that various functions of GR are regulated by redox status.<BR>Taken together, it is important to understand the mechanisms of redox dependent regulation of GR function, to aid development of novel drugs and therapies for various disorders including inflammatory diseases.
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