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dc.contributor.authorWu, Q
dc.contributor.author吴乔
dc.contributor.authorLin, XF
dc.contributor.authorYe, XF
dc.contributor.authorZhang, B
dc.contributor.authorXie, Z
dc.contributor.authorSu, WJ
dc.contributor.author苏文金
dc.date.accessioned2011-10-23T03:04:25Z
dc.date.available2011-10-23T03:04:25Z
dc.date.issued2004
dc.identifier.citationJ Mol Endocrinol. 2004 Jun;32(3):595-613.zh_CN
dc.identifier.issn0952-5041
dc.identifier.urihttp://dx.doi.org/doi:10.1677/jme.0.0320595
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10986
dc.description.abstractRetinoic acid receptor alpha (RARalpha) plays an important role in mediating all-trans retinoic acid (ATRA) signals. In this study, we found that ATRA up-regulated RARalpha mRNA and protein expression in gastric cancer BGC-823 cells. However, in breast cancer MCF-7 cells it down-regulated RARalpha protein expression with no effect on its RARalpha mRNA. Immunoprecipitation/Western blot analysis showed that, although surnoylated and ubiquitinated RARalpha existed simultaneously in both cancer cell lines, ATRA exerted different regulatory effects on surnoylation and ubiquitination of RARalpha. In MCF-7 cells, ATRA treatment enhanced tie ubiquitination of RARalpha and the subsequent degradation of RARalpha through the ubiquitin/proteasome pathway. This resulted in a reduction in the DNA binding activity of RARalpha/retinoid X receptor alpha (RXRalpha) helerodimer, the separation of RXRalpha from RARalpha. and the translocation of RXRalpha from the nucleus to the cytoplasm. By contrast, in BGC-823 cells, ATRA augmented sumoylation, not ubiquitination, of RARalpha. The stability of surnoylated RARalpha was significantly stronger than in non-sumoylated RARalpha. These results also showed an increase in the DNA binding activity of the RARalpha/RXRalpha heterodimer and the stability of nuclear localization of this heterodimer, which normally facilitates the ATRA signal transduction. In conclusion, our results reveal a novel mechanism for the regulation of RARalpha-dependent signal transduction through the ubiquitin/proteasome pathway in breast cancer cells and the sumoylation pathway in gastric cancer cells.zh_CN
dc.language.isoenzh_CN
dc.publisherSOC ENDOCRINOLOGYzh_CN
dc.titleUbiquitinated or sumoylated retinoic acid receptor alpha determines its characteristic and interacting model with retinoid X receptor alpha in gastric and breast cancer cellszh_CN
dc.typeArticlezh_CN


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