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• W2023591218 abstract "4-nitroquinoline N-oxide (4-NQO) is a potent mutagen and carcinogen. To elucidate the cellular response to 4-NQO, we studied the transcriptional regulation of human proliferating cell nuclear antigen (hPCNA), an essential protein in DNA replication and repair, after 4-NQO treatment. We found that hPCNA promoter was dose-dependently transactivated by 4-NQO under the concentration of 2 microM via a previously reported p53-binding element located from -236 to -217 upstream of the transcription start site. Based on our western blot analysis, the phosphorylation of serine at the 15th residue (Ser15) of p53 was activated by 4-NQO, whereas the level of p53 in the cells did not change much. It was observed that Staurosporine, a Ser/Thr kinase inhibitor, blocked the Ser15 phosphorylation of p53 and the hPCNA promoter response to 4-NQO simultaneously, suggesting that Ser15 phosphorylated p53 was the 4-NQO-responsive hPCNA regulator. The [3H]-thymidine deoxyribose (TdR) incorporation assay and the comet assay showed that DNA repair was triggered when DNA replication was inhibited after the treatment of 4-NQO, and the hPCNA transactivation seemed to contribute to DNA repair. Taken together, our data indicate that after 4-NQO treatment hPCNA is transactivated by Ser15 phosphorylated p53, and participate in DNA repair." @default.
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• W2023591218 date "2005-02-01" @default.
• W2023591218 modified "2023-09-26" @default.
• W2023591218 title "p53 protein activates the transcription of human proliferating cell nuclear antigen in response to 4-nitroquinoline N-oxide treatment" @default.
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• W2023591218 doi "https://doi.org/10.1016/j.biocel.2004.07.001" @default.
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