期刊文献+

丙戊酸钠诱导Siha细胞周期阻滞的实验观察

Cell cycle block induced by sodium valproate in Siha cells
原文传递
导出
摘要 目的:研究丙戊酸钠对人宫颈癌Siha细胞增殖和细胞周期的影响。方法:MTT检测生长抑制,流式细胞仪检测细胞周期,蛋白质印迹法检测p21WAF1/CIP1、p-CDK2和cyclin E蛋白。结果:丙戊酸钠以剂量依赖性方式抑制Siha细胞生长IC20和IC50分别为2.0 mmol/L和8.0 mmol/L;丙戊酸钠上调G0/G1期比例由(74.92±0.60)%升高至(84.475±1.11)%,P=0.001,下调S期(13.19±0.70)%降为(7.72±1.40)%,P=0.004和G2/M(11.89±1.30)%降为(7.81±0.31)%期比例,P=0.006。丙戊酸钠上调p21WAF1/CIP1蛋白,下调cyclin E和p-CDK2蛋白。结论:丙戊酸钠上调p21WAF1/CIP1表达和抑制cyclin E表达,使细胞阻滞于G0/G1期,抑制Siha细胞生长。 OBJECTIVE: To explore the effect of sodium val- proate on proliferation and cell cycle in Siha cells. METHODS: Growth inhibition rates were determined by MTT assay. Cell cycles were assessed by flowcytometry,p21WAF1/CIP1, p-CDK2, and cyclin E protein were examined by Western blot. RESULTS: Sodium val- proate inhibited the proliferation of Siha ceils in a dose dependent manner IC20 and IC50 were 2.0 mmol/L and 8.0 mmol/L, signifi- cantly. Siha cells showed a G0/G1 phase block, increased from (74. 92± 0. 60) % to (84.475±1.11)%(P=0.001), and S and G2/M phase decreased in response to sodium valproate. The per- centage of S stage decreased from (13.19±0.70)% to (7.72± 1.40)%(P=0.004). The percentage of G2/M stage decreased from (11.89±1.30)% to (7.81±0.31)%(P=0.006). Sodium valproate up-regulated p21WAF1/CIP1 and down-regulated eyclin E and p-CDK2 protein. CONCLUSION: Sodium valproate may play an an- ti-proliferation role by raising p21WAF1/CIP1 protein, reducing cylinE and inducing G0/G1 phase arrest.
作者 李娜 于世英
出处 《中华肿瘤防治杂志》 CAS 2009年第11期834-836,共3页 Chinese Journal of Cancer Prevention and Treatment
基金 湖北省科技攻关计划项目(2005AA304B07)
关键词 丙戊酸钠 宫颈肿瘤 细胞周期 P21WAF1/CIP1 CYCLIN E sodium valproate cervical carcinoma cell cycle p21WAF1/CIP1 cyclin E
  • 相关文献

参考文献11

  • 1Mottet D, Castronovo V. Histone deacetylases: target enzymes for cancer therapy[J]. Clin Exp Metastasis,2008, 25(2): 183-189.
  • 2Phiel C J, Zhang F, Huang E Y, et al. Histone deacetylase is a direct target of valproie acid, a potent anticonvulsant, mood stabilizer, and teratogen[J]. J Biol Chem, 2001, 276(39) :36734-36741.
  • 3Gottlicher M, Minucci S, Zhu P, et al. Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells[J]. EMBOJ, 2001, 20(24): 6969-6978.
  • 4安丽娜,王树人.组蛋白乙酰化/去乙酰化与染色质结构及基因转录调控的关系[J].国外医学(遗传学分册),2005,28(3):133-137. 被引量:4
  • 5Huang B H, Laban M, Leung C W, et al. Inhibition of histone deaeetylase 2 increases apoptosis and p21^Cip1/WAF1 expression, independent of histone deacetylase 1[J]. Cell Death and Differenti ation,2005,12(4):395-404.
  • 6Gurvieh N, Tsygankova O M, Meinkoth J L, et al. Histone deacetylase is a target of valproie acid-mediated cellular differentiation[J]. Cancer Res, 2004,64 (3) : 1079-1086.
  • 7Hoffmann K, Brosch G, Loidl P, et ah First non-radioactive assay for in vitro screening of histone deacetylase inhibitors[J]. Pharmazie, 2000, 55(8) :601-606.
  • 8Richon V M, Sandhog T W, Rifkind R A, et al. Histone deacetylase inhibitor selectively induces p21^WAF1 expression and gene-associ ated histone aeetylation[J]. Proc Natl Acad Sci, 2000, 97 (18) :10014-10019.
  • 9Ocker M, Schneider S R. Histone deacetylase inhibitors: signalling towards p21^cip1/waf1[J]. Int J Biochem Cell Biol, 2007, 39 (7-8): 1367-1374.
  • 10Kim Y B, Ki S W, Yoshida M, et al. Mechanism of cell cycle arrest eaused by histone deacetylase inhibitors in human carcinoma cells[J]. J Antibiot,2000,53(10):1191-1200.

二级参考文献30

  • 1Fu XH, Liu DP, Liang CC. Chromatin structure and transcriptional regulation of the β3-globin locus. Exp Cell Res, 2002,278( 1 ): 1-11.
  • 2Berger SL. Histone modifications in transcriptional regulation. Curr Opin Genet, 2002,12:142-148.
  • 3Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes, 2001, 15: 2343-2360.
  • 4Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev, 2000,64(2):435-459.
  • 5Herceg Z, Li H, Cuenin C, et al. Genome-wide analysis of gene expression regulated by the HAT cofactor trrap in conditional knockout cells. Nucleic Acids Res, 2003,31 (23): 7011-7023.
  • 6Qi D, Larsson J, Mannervik M. Drosophila Ada2b is required for viability and normal histone H3 acetylation. Mol Cell Biol,2004,24( 18 ): 8080-8089.
  • 7Doyon Y, Cote J. The highly conserved and multifunctional NuA4 HAT complex. Curr Opin Genet Det,2004,14(2): 147-154.
  • 8An W, Kim J, Roeder RG. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53.Cell, 2004,117(6) :735-748.
  • 9Annunziato AT, Hansen JC. Role of histone acetylation in the assembly and modulation of chromatin structures. Gene Expr, 2000,9(1-2) :37-61.
  • 10Sewack GF,Elis TW, Hansen U. Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation. Mol Cell Biol, 2001,21:1404-1415.

共引文献3

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部