ECE2014 Poster Presentations Nuclear receptors and signal transduction (4 abstracts)
Formation of progesterone receptor-NF-κB complex is required for progesterone-induced NF-κB nuclear translocation and binding onto the p53 promoter
Sung-Po Hsu 1 , Ho-Ching Yang 2 , Chun-Ting Kuo 3 , Heng-Ching Wen 3 , Li-Ching Chen 3 , Yen-Nien Huo 3 & Wen-Sen Lee 1,
1Department of Physiology, School of Medicine, College of Medicine, Taipei Medical University, Taipei, Taiwan; 2Graduate Institute of Physiology, College of Medicine, National Taiwan University, Taipei, Taiwan; 3Graduate Institute of Medical Sciences, College of Medicine, Taipei Medical University, Taipei, Taiwan.
We previously showed that progesterone (P4) regulates p53 expression and cell cycle progress in human umbilical venous endothelial cells (HUVEC) through progesterone receptor (PR) activation of extra-nuclear signaling pathways. Here, we showed that P4 activated the PR and hence increased the formation of progesterone receptor A-(PR-A)-NF-κB complex in both the cytosol and the nucleus. Chromatin immunoprecipitation demonstrated an interaction between PR and the NF-κB binding motif on the p53 promoter. Ablation of the NF-κB binding motif on the p53 promoter completely abolished the P4-increased p53 promoter activity. In the absence of P4, over-expression of NF-κB did not cause NF-κB nuclear translocation. Blockade of PR abolished the P4-induced NF-κB nuclear translocation in the NF-κB-overexpressing HUVEC. These results uncover a novel role of PR for P4-induced NF-κB nuclear translocation and p53 up-regulation and suggest that PR-A-NF-κB complex is required for NF-κB nuclear translocation and binding onto the p53 promoter. The findings from the present and our previous studies suggest that both nuclear PR and non-nuclear PR are involved in the P4-regulated p53 expression and cell cycle progress.
Volume 35
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Endocrine Abstracts
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