Browse > Article
http://dx.doi.org/10.7314/APJCP.2013.14.5.2915

3-Deazaneplanocin A is a Promising Therapeutic Agent for Ovarian Cancer Cells  

Shen, Liang (Department of Obstetrics and Gynaecology, Provincial Hospital Affiliated to Shandong University)
Cui, Jing (Department of Oral and Maxillofacial Surgery, Jinan Stomatologic Hospital)
Pang, Ying-Xin (Department of Obstetrics and Gynecology, Qilu Hospital, Shandong University)
Ma, Yan-Hui (Department of Obstetrics and Gynecology, Qilu Hospital, Shandong University)
Liu, Pei-Shu (Department of Obstetrics and Gynecology, Qilu Hospital, Shandong University)
Publication Information
Asian Pacific Journal of Cancer Prevention / v.14, no.5, 2013 , pp. 2915-2918 More about this Journal
Abstract
Background: Recent studies have shown that 3-deazaneplanocin A (DZNep), a well-known histone methyltransferase inhibitor, disrupts polycomb-repressive complex 2 (PRC2), and induces apoptosis, while inhibiting proliferation and metastasis, in cancer cells, including acute myeloid leukemia, breast cancer and glioblastoma. However, little is known about effects of DZNep on ovarian cancer cells. Materials and Methods: We here therefore studied DZNep-treated A2780 ovarian cancer cells in vitro. Proliferation of ovarian cancer cells under treatment of DZNep was assessed by MTT and apoptosis by flow cytometry. Cell wound healing was applied to detect the migration. Finally, we used q-PCR to assess the migration-related gene, E-cadherin. Results: DZNep could inhibit the proliferation of A2780 and induce apoptosis Furthermore, it inhibited migration and increased the expression of E-cadherin (P<0.05). Conclusion: DZNep is a promising therapeutic agent for ovarian cancer cells, with potential to inhibite proliferation, induce apoptosis and decrease migration.
Keywords
DZNep; ovarian cancer cells; proliferation; apoptosis; migration;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Kikuchi J, Takashina T, Kinoshita I, et al (2012). Epigenetic therapy with 3-deazaneplanocin A, an inhibitor of the histone methyltransferase EZH2, inhibits growth of non-small cell lung cancer cells. Lung Cancer, 78, 138-43.   DOI   ScienceOn
2 Kuzmichev A, Nishioka K, Erdjument-Bromage H, et al (2002). Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev, 16, 2893-905.   DOI   ScienceOn
3 Landen CN Jr, Birrer MJ, Sood AK (2008). Early events in the pathogenesis of epithelial ovarian cancer. J Clin Oncol, 26, 995-1005.   DOI   ScienceOn
4 Liu S, Wolfe MS, Borchardt RT (1992). Rational approaches to the design of antiviral agents based on S-adenosyl-Lhomocysteine hydrolase as a molecular target. Antiviral Res, 19, 247-65.   DOI   ScienceOn
5 Orrenius S, Zhivotovsky B, Nicotera P (2003). Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol, 4, 552-65.   DOI   ScienceOn
6 Rao ZY, Cai MY, Yang GF, et al (2010). EZH2 supports ovarian carcinoma cell invasion and/or metastasis via regulation of TGF-beta1 and is a predictor of outcome in ovarian carcinoma patients. Carcinogenesis, 31, 1576-83.   DOI   ScienceOn
7 Rizzo S, Hersey JM, Mellor P, et al (2011). Ovarian cancer stem cell-like side populations are enriched following chemotherapy and overexpress EZH2. Mol Cancer Ther, 10, 325-35.   DOI
8 Sasaki D, Imaizumi Y, Hasegawa H, et al (2011). Overexpression of Enhancer of zeste homolog 2 with trimethylation of lysine 27 on histone H3 in adult T-cell leukemia/lymphoma as a target for epigenetic therapy. Haematologica, 96, 712-19.   DOI
9 Tan J, Yang X, Zhuang L, et al (2007). Pharmacologic disruption of Polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells. Genes Dev, 21, 1050-63.   DOI   ScienceOn
10 Glazer RI, Hartman KD, Knode MC, et al (1986). 3-Deazaneplanocin: a new and potent inhibitor of S-adenosylhomocysteine hydrolase and its effects on human promyelocytic leukemia cell line HL-60. Biochem Biophys Res Commun, 135, 688-94.   DOI   ScienceOn
11 Guo J, Cai J, Yu L, et al (2011). EZH2 regulates expression of p57 and contributes to progression of ovarian cancer in vitro and in vivo. Cancer Sci, 102, 530-9.   DOI   ScienceOn
12 Hudson LG, Zeineldin R, Stack MS (2008). Phenotypic plasticity of neoplastic ovarian epithelium: unique cadherin profiles in tumor progression. Clin Exp Metastasis, 25, 643-55.   DOI
13 Bristow RE, Palis BE, Chi DS, et al (2010). The National Cancer Database report on advanced-stage epithelial ovarian cancer: impact of hospital surgical case volume on overall survival and surgical treatment paradigm. Gynecol Oncol, 118, 262-7.   DOI   ScienceOn
14 Cao R, Wang L, Wang H, et al (2002). Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science, 298, 1039-43.   DOI   ScienceOn
15 Danial NN, Korsmeyer SJ (2004). Cell death: critical control points. Cell, 116, 205-19.   DOI   ScienceOn
16 Davies BR, Worsley SD, Ponder BA (1998). Expression of E-cadherin, alpha-catenin and beta-catenin in normal ovarian surface epithelium and epithelial ovarian cancers. Histopathology, 32, 69-80.   DOI   ScienceOn
17 Imai T, Horiuchi A, Shiozawa T, et al (2004). Elevated expression of E-cadherin and alpha-, beta-, and gamma-catenins in metastatic lesions compared with primary epithelial ovarian carcinomas. Hum Pathol, 35, 1469-76.   DOI   ScienceOn
18 Kalushkova A, Fryknas M, Lemaire M, et al (2010). Polycomb target genes are silenced in multiple myeloma. PLoS One, 5, e11483.   DOI   ScienceOn