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Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcriptional regulators. Casein kinase 1alpha interacts with retinoid X receptor and interferes with agonist-induced apoptosis. Data suggest that altered localization of retinoid X receptor alpha to the splicing factor compartment may be an important factor for the loss of retinoid responsiveness in MDA-MB-231 breast cancer cells. Decrease of RXRalpha in prostate basal cells may serve as a marker for prostate carcinoma-associated field change, which may represent an early event in the prostate carcinogenic process. Expression of adipophilin is enhanced during trophoblast differentiation and is up-regulated by ligand-activated PPARgamma/retinoid X receptor. May contribute to fatty acid uptake by placenta. IL-3-induced enhancement of retinoic acid receptor activity is mediated through Stat5, which physically associates with recombinant human retinoic acid receptors in an IL-3-dependent manner. Increase in expression of RXRalpha is associated with esophageal squamous cell carcinomas. Interactions that determine the assembly of a retinoid X receptor/corepressor complex. RXR alpha responsive element-dependent expression and RXR alpha-dependent transcriptional activation is regulated in T lymphocytes by cellular Ser/Thr phosphatases PP1 and PP2A. RXR and its agonists have roles in the regulation of beta-catenin turnover and related biological events. RXR could function as a fatty acid receptor in vivo. RXRalpha and RXRgamma immunodetected in all normal, nodular, and basal cell hyperplasia, as well as carcinomatous prostates. In atrophic glands, the expression of both receptors was found in 22.5% of samples. RXRalpha up-regulation was associated with the early stages of laryngeal carcinogenesis. Results demonstrate that human papilloma virus 16 E6 oncoprotein inhibits the RXR(alpha)-mediated transactivation of target genes, implying that perturbation of RXR-mediated transactivation by E6 could contribute to HPV oncogenesis. Results show an increased DNA binding of the retinoic acid receptor alpha/retinoid X receptor alpha heterodimer and the stability of nuclear localization of this heterodimer, which facilitates signal transduction. Retinoid signaling is attenuated by retinoic acid-induced proteasome-mediated degradation of RXRA in human keratocytes. Retinoid x receptor alpha (RXRalpha) may be actively involved in cell proliferation and cell cycle regulation in human hepatocyte cell line Hep3B cells. The receptor, alpha shows abundant expression in the variety of tissues. The role of retinoid X receptor messenger RNA expression in curatively resected non-small cell lung cancer. Transcriptionlal activation driven by the PPARalpha/RXRalpha complex was counteracted by the expression of ERRalpha in HeLa cells. With PPAR-gamma, forms heterodimers in the regulation of human trophoblast invasion. Depletion of vitamin A and retinoid receptors by UV irradiation, together with unchanged or even increased c-Jun levels, might seriously interfere with retinoid signaling and thus promote future tumor development, especially in keratinocytes. In response to retinoic acid and in a manner requiring the activity of RXRalpha, secretes trophic factors which drive fetal cardiomyocyte proliferation and promote ventricular chamber morphogenesis. Nongenotropic function of RXRalpha and its involvement in the regulation of the Nur77-dependent apoptotic pathway. Novel aspect of RXRalpha function: it acts as a carrier for nucleocytoplasmic translocation of orphan receptors. Regulates vitamin D receptor functions in part by regulating subcellular localization. Results suggest a novel function of RNF8 as a regulator of RXR alpha-mediated transcriptional activity through interaction between their respective N-terminal regions. Results suggest specific physiological roles of two novel human RXR alpha splice variants. Results suggest that oxidized phospholipids inhibit transcription of the thrombomodulin gene in vascular endothelium by inhibiting the binding of retinoic acid receptor beta-retinoid x receptor alpha heterodimer and Sp1 and Sp3 to thrombomodulin promoter. Retinoid x receptor alpha structural results support the idea that docosa hexaenoic acid and related fatty acids could be natural agonists of RXRs. Study indicated that the subcellular intratumoral distribution pattern of RXR-alpha could independently predict the survival of RCC patients. The effect of STAT5b-RARalpha on the activity of myeloid transcription factors including RARalpha/retinoid X receptor (RXR) alpha.
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