De-phosphorylation of GR at Ser203 in nuclei associates with GR nuclear translocation and GLUT5 gene expression in Caco-2 cells |
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Authors: | Takabe Satsuki Mochizuki Kazuki Goda Toshinao |
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Institution: | Laboratory of Nutritional Physiology, Graduate School of Nutritional and Environmental Sciences and Global COE, The University of Shizuoka, 52-1 Yada, Shizuoka-shi, Shizuoka 422-8526, Japan |
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Abstract: | Glucocorticoid hormones and p44/42 mitogen-activated protein kinase (MAPK) inactivation are considered to be important in small-intestinal differentiation/maturation. In this study, we found that co-treatment with glucocorticoid hormone agonist dexamethasone and p44/42 MAPK inhibitor PD98059 in intestinal cell line Caco-2 strongly induced GLUT5 gene expression. Glucocorticoid hormone receptor (GR) was translocated from the cytoplasm to the nucleus and de-phosphorylated at serine residue 203 in the nucleus, by combined treatment with dexamethasone and PD98059. The binding of GR, as well as acetylated histones H3 and H4, to the promoter/enhancer region of GLUT5 gene was enhanced by combined treatment with dexamethasone and PD98059. These results suggest that the inactivation of p44/42 MAP kinase enhances glucocorticoid hormone-induced GLUT5 gene expression, probably through controlling the phosphorylation at serine 203 and nuclear transport of GR, as well as histone acetylation on the promoter/enhancer region of GLUT5 gene. |
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Keywords: | Caco-2 cells De-phosphorylation Glucocorticoid hormone receptor GLUT5 Nuclear translocation p44/42 MAPK |
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