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KW-2478对肿瘤细胞增殖作用的影响

Influence of KW-2478 on the Proliferation of Tumor Cells
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摘要 目的:研究KW-2478对Eca109和KYSE-150食管癌细胞株、SGC-7901胃癌细胞株、HepG2肝癌细胞株、MCF-7乳腺癌细胞株5种肿瘤细胞体外增殖作用的影响,同时观察KW-2478对HL-7702正常肝细胞的作用。方法:体外培养HL-7702,Eca109,KYSE-150,SGC-7901,MCF-7和HepG2细胞,给予不同浓度的KW-2478,24h和48h后采用四甲基偶氮唑盐微量酶反应比色法(MTT法)检测细胞增殖情况。结果:不同浓度KW-2478作用于肿瘤细胞24h和48h后,5种肿瘤细胞的增殖能力均降低,呈现剂量和时间依赖性,且在Eca109细胞和HepG2细胞呈现剂量与时间交互作用,但HL-7702细胞的增殖情况未受明显影响。结论:KW-2478对Eca109,KYSE-150,SGC-7901,MCF-7和HepG2细胞有抑制作用,对HL-7702正常肝细胞的增殖无明显影响。 Objective: To study the effect on proliferation of KW-2478 to Eca109 and KYSE-150 esophageal cancer cell line,SGC-7901 gastric cancer cell line,HepG2 hepatoma cell line and MCF-7 breast cancer cell in vitro. And to observe the effect of KW-2478 to HL-7702 normal hepatocytes. Methods: HL-7702,Eca109,KYSE-150,SGC-7901,MCF-7 and HepG2 cell lines were cultured in vitro,give different concentrations of KW-2478,MTT assay test cell proliferation after 24 h and 48 h. Results: After 24 h and 48 h different concentrations of KW-2478 to the tumor cells,the proliferation of five tumor cells were reduced in dose-dependent and time-dependent,and showed dose and time interaction on Eca109 cells and HepG2 cells,but HL-7702 was not significantly affected. Conclusion: KW-2478 have inhibitory effect to Eca109,KYSE-150,SGC-7901,MCF-7 and HepG2 cells,and had no significant effect on the proliferation of HL-7702 normal hepatocytes.
出处 《河北医学》 CAS 2018年第1期11-16,共6页 Hebei Medicine
基金 河北省病原生物学重点学科 承德医学院免疫学重点学科 河北省教育厅重点项目,(编号:ZD2014003)
关键词 KW-2478 MTT 增殖 肿瘤细胞 KW-2478 MTT Proliferation Tumor cells
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  • 1文萍,胡卫华,窦骏.Wnt/β-catenin信号通路在肿瘤干细胞中作用研究进展[J].中国医药生物技术,2007,2(6):455-457. 被引量:5
  • 2陈奕,丁健.热休克蛋白90——癌症治疗的新靶点[J].癌症,2004,23(8):968-974. 被引量:17
  • 3Maloney A, Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds[J]. Expert Opin Biol Ther, 2002, 2(1): 3-24.
  • 4Stebbins C E, Russo A A, Schneider C, et al. Crystal structure of an Hsp90-geldanamycin complex; targeting of a protein chaperone by an antitumor agent[J]. Cell, 1997, 89(2): 239-250.
  • 5Bergerat A, De-Massy B, Gadelle D, et al. An atypical toposomeerase II from Archaea with implications for meiotic recombination[J]. Nature, 1997, 386(6623): 414-417.
  • 6Obermann W M, Sondermann H, Russo A A, et al. In vivofunction of hsp90 is dependent on ATP binding and ATP hydrolysis[J]. J CellBiol, 1998, 143(4): 901-910.
  • 7Meyer P, Prodromou C, Hu B, et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions[J]. Mol Cell, 2003, 11(3): 647-658.
  • 8Harris S F, Shiau A K, Agard D A. The crystal structure of the earboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site[J]. Structure, 2004, 12(6): 1087-1097.
  • 9Langer T, Schlatter H, Fasold H. Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90(HSP90) is necessary for its autophosphorylation[J]. Cell Biol lnt, 2002, 26(7): 653-657.
  • 10Ochel H J, Schulte T W, Nguyen P, et al. The benz0quinone ansamycin geldanamycin stimulates proteolytic degradation of focal adhesion kinase[J]. Mol Genet Metab, 1999, 66(1): 24-30.

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