Oleinik Natalia V, Krupenko Natalia I, Krupenko Sergey A
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Genes Cancer. 2011 Feb;2(2):130-9. doi: 10.1177/1947601911405841.
FDH (10-formyltetrahydrofolate dehydrogenase, the product of the ALDH1L1 gene), a major folate-metabolizing enzyme in the cytosol, is involved in the regulation of cellular proliferation. We have previously demonstrated that FDH is strongly and ubiquitously down-regulated in malignant human tumors and cancer cell lines. Here, we report that promoter methylation is a major mechanism controlling FDH levels in human cancers. A computational analysis has identified an extensive CpG island in the ALDH1L1 promoter region. It contains 96 CpG pairs and covers the region between -525 and +918 bp of the ALDH1L1 gene including the promoter, the entire exon 1, and a part of intron 1 immediately downstream of the exon. Bisulfite sequencing analysis revealed extensive methylation of the island (76%-95% of CpGs) in cancer cell lines. In agreement with these findings, treatment of FDH-deficient A549 cells with the methyltransferase inhibitor 5-aza-2'-deoxycytidine restored FDH expression. Analysis of the samples from patients with lung adenocarcinomas demonstrated methylation of the ALDH1L1 CpG island in tumor samples and a total lack of methylation in respective normal tissues. The same phenomenon was observed in liver tissues: the CpG island was methylation free in DNA extracted from normal hepatocytes but was extensively methylated in a hepatocellular carcinoma. Levels of ALDH1L1 mRNA and protein correlated with the methylation status of the island, with tumor samples demonstrating down-regulation of expression or even complete silencing of the gene. Our studies have also revealed that exon 1 significantly increases transcriptional activity of ALDH1L1 promoter in a luciferase reporter assay. Interestingly, the exon is extensively methylated in samples with a strongly down-regulated or silenced ALDH1L1 gene.
FDH(10-甲酰四氢叶酸脱氢酶,由ALDH1L1基因产生)是胞质溶胶中一种主要的叶酸代谢酶,参与细胞增殖的调节。我们之前已证明,FDH在人类恶性肿瘤和癌细胞系中强烈且普遍下调。在此,我们报告启动子甲基化是控制人类癌症中FDH水平的主要机制。一项计算分析在ALDH1L1启动子区域鉴定出一个广泛的CpG岛。它包含96个CpG对,覆盖ALDH1L1基因从-525到+918 bp的区域,包括启动子、整个外显子1以及外显子下游紧邻的内含子1的一部分。亚硫酸氢盐测序分析显示癌细胞系中该岛存在广泛甲基化(76%-95%的CpG)。与这些发现一致,用甲基转移酶抑制剂5-氮杂-2'-脱氧胞苷处理FDH缺陷的A549细胞可恢复FDH表达。对肺腺癌患者样本的分析表明,肿瘤样本中ALDH1L1 CpG岛发生甲基化,而相应正常组织中完全没有甲基化。在肝脏组织中也观察到同样的现象:从正常肝细胞提取的DNA中CpG岛无甲基化,但在肝细胞癌中广泛甲基化。ALDH1L1 mRNA和蛋白质水平与该岛的甲基化状态相关,肿瘤样本显示基因表达下调甚至完全沉默。我们的研究还表明,在荧光素酶报告基因检测中,外显子1显著增加ALDH1L1启动子的转录活性。有趣的是,在ALDH1L1基因强烈下调或沉默的样本中,该外显子广泛甲基化。