中文摘要：

<正>Objective To investigate the role of tyrosine 23(Tyr23) phosphorylation of Annexin A2(Anxa2) in regulating the proliferation and invasion of human breast cancer SK-BR-3 cells. Methods A panel of lentivirus plasmids expressing Anxa2-wide type(Ana2-WT),Anxa2-Y23A,and Anxa2-Y23D was generated and infected with SK-BR-3 cells.The monoclonal strains were screened.The expression of Anxa2-WT,Anxa2-Y23A,and Anxa2-Y23D was determined by Western blot analysis.The ability of the cells to proliferate was detected through an MTT[3-(4,5-Dimethylthiazol- 2-yl)-2,5-diphenyltetrazolium bromide]test.Boyden chamber assays were employed to examine migration and invasion abilities. The interaction between Anxa2 and Stat3 was analyzed by immunoprecipitation analyses.Nucleoprotein and cytosolic protein were extracted from SK-BR-3,Anxa2-WT,Anxa2-Y23A,and Anxa2-Y23D cells to analyze the expression and localization of Stat3 phosphorylation. Results The monoclonal strains constitutively expressing Anxa2-WT,Anxa2-Y23A,and Anxa2-Y23D were screened.Both Anxa2-W and Anxa2-Y23D enhanced the proliferation,migration and invasion abilities of SK-BR-3 cells(P<0.05).Immunoprecipitation analy revealed that Anxa2 and Stat3 interacted with each other,and the expression of Stat3 phosphorylation in the nucleus was enhanced Anxa2-Y23D. Conclusions Tyr23 phosphorylation of Anxa2 promotes the proliferation and invasion of human breast cancer SK-BR-3 cells and phosphorylation of Stat3 in the nucleus.

英文摘要：

Objective To investigate the role of tyrosine 23 （Tyr23） phosphorylation of Annexin A2 （Anxa2） in regulating the proliferation and invasion of human breast cancer SK-BR-3 cells. Methods A panel of lentivirus plasmids expressing Anxa2-wide type （Ana2-WT）, Anxa2-Y23A, and Anxa2-Y23D was generated and infected with SK-BR-3 cells. The monoclonal strains were screened. The expression of Anxa2-WT, Anxa2-Y23A, and Anxa2-Y23D was determined by Western blot analysis. The ability of the cells to proliferate was detected through an MTT [3-（4,5-Dimethylthiazol- 2-yl）-2,5-diphenyltetrazolium bromide] test. Boyden chamber assays were employed to examine migration and invasion abilities. The interaction between Anxa2 and Stat3 was analyzed by immunoprecipitation analyses. Nucleoprotein and cytosolic protein were extracted from SK-BR-3, Anxa2-WT, Anxa2-Y23A, and Anxa2-Y23D cells to analyze the expression and localization of Stat3 phosphorylation. Results The monoclonal strains constitutively expressing Anxa2-WT, Anxa2-Y23A, and Anxa2-Y23D were screened. Both Anxa2-WT and Anxa2-Y23D enhanced the proliferation, migration and invasion abilities of SK-BR-3 cells （P〈0.05）. Immunoprecipitation analysis revealed that Anxa2 and Stat3 interacted with each other, and the expression of Stat3 phosphorylation in the nucleus was enhanced by Anxa2-Y23D. Conclusions Tyr23 phosphorylation of Anxa2 promotes the proliferation and invasion of human breast cancer SK-BR-3 cells and the phosphorylation of Stat3 in the nucleus.