Li Jie, Koike Junichi, Kugoh Hiroyuki, Arita Michitsune, Ohhira Takahito, Kikuchi Yoshinori, Funahashi Kimihiko, Takamatsu Ken, Boland C Richard, Koi Minoru, Hemmi Hiromichi
Department of Molecular Biology, Toho University School of Medicine, Tokyo, Japan.
Biochim Biophys Acta. 2012 Apr;1823(4):889-99. doi: 10.1016/j.bbamcr.2012.01.017. Epub 2012 Feb 9.
Down-regulation of hMSH3 is associated with elevated microsatellite alterations at selected tetranucleotide repeats and low levels of microsatellite instability in colorectal cancer (CRC). However, the mechanism that down-regulates hMSH3 in CRC is not known. In this study, a significant association between over-expression of glucose transporter 1, a marker for hypoxia, and down-regulation of hMSH3 in CRC tissues was observed. Therefore, we examined the effect of hypoxia on the expression of hMSH3 in human cell lines. When cells with wild type p53 (wt-p53) were exposed to hypoxia, rapid down-regulation of both hMSH2 and hMSH3 occurred. In contrast, when null or mutated p53 (null/mut-p53) cells were exposed to hypoxia, only hMSH3 was down-regulated, and at slower rate than wt-p53 cells. Using a reporter assay, we found that disruption of the two putative hypoxia response elements (HREs) located within the promoter region of the hMSH3 abrogated the suppressive effect of hypoxia on reporter activity regardless of p53 status. In an EMSA, two different forms of HIF-1α complexes that specifically bind to these HREs were detected. A larger complex containing HIF-1α predominantly bound to the HREs in hypoxic null/mut-p53 cells whereas a smaller complex predominated in wt-p53 cells. Finally, HIF-1α knockdown by siRNA significantly inhibited down-regulation of hMSH3 by hypoxia in both wt-p53 and mut-p53 cells. Taken together, our results suggest that the binding of HIF-1α complexes to HRE sites is necessary for down-regulation of hMSH3 in both wt-p53 and mut-p53 cells.
人错配修复蛋白3(hMSH3)的下调与结直肠癌(CRC)中特定四核苷酸重复序列处微卫星改变的增加及微卫星不稳定性水平降低有关。然而,CRC中下调hMSH3的机制尚不清楚。在本研究中,观察到缺氧标志物葡萄糖转运蛋白1的过表达与CRC组织中hMSH3的下调之间存在显著关联。因此,我们研究了缺氧对人细胞系中hMSH3表达的影响。当具有野生型p53(wt-p53)的细胞暴露于缺氧环境时,hMSH2和hMSH3均迅速下调。相比之下,当p53缺失或突变(null/mut-p53)的细胞暴露于缺氧环境时,只有hMSH3被下调,且下调速度比wt-p53细胞慢。通过报告基因检测,我们发现位于hMSH3启动子区域内的两个假定缺氧反应元件(HREs)的破坏消除了缺氧对报告基因活性的抑制作用,而与p53状态无关。在电泳迁移率变动分析(EMSA)中,检测到两种特异性结合这些HREs的不同形式的缺氧诱导因子-1α(HIF-1α)复合物。一个包含HIF-1α的较大复合物主要在缺氧的null/mut-p53细胞中与HREs结合,而一个较小的复合物在wt-p53细胞中占主导。最后,通过小干扰RNA(siRNA)敲低HIF-1α显著抑制了wt-p53和mut-p53细胞中缺氧诱导的hMSH3下调。综上所述,我们的结果表明,HIF-1α复合物与HRE位点的结合对于wt-p53和mut-p53细胞中hMSH3的下调是必要的。