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Department of Radiation Oncology, Arizona Cancer Center, The University of Arizona, Tucson, Arizona 85724 [Q. T., M. G., G. T. B.], and Department of Pharmacology, National Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan [H. I.]
Ultraviolet B (UVB)-induced cyclooxygenase-2 (COX-2) expression plays an important role in UVB tumor promotion. We examined whether Akt and glycogen synthase kinase 3ß (GSK-3ß), components of the phosphatidylinositol 3'-kinase pathway, are involved in UVB induction of COX-2 transcription. UVB caused Akt phosphorylation at both Thr-308 and Ser-473 that was inhibited by LY294002, a phosphatidylinositol 3'-kinase inhibitor. LY294002 also decreased the expression of endogenous COX-2 protein and a luciferase construct driven by COX-2 promoter. Similarly, UVB caused phosphorylation of GSK-3ß (Ser-9) and presumably inactivation of GSK-3ß. Inhibition of GSK-3ß by lithium induced endogenous COX-2 protein expression and COX-2 promoter activity. Finally, overexpression of a dominant-negative Akt mutant or wild-type GSK-3ß suppressed UVB-mediated induction of COX-2 promoter. These studies suggest that inactivation of GSK-3ß through activation of Akt plays an important role in the UVB induction of COX-2 transcription.
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