中文摘要：

目的探讨钙结合蛋白S100A8／A9复合物对人宫颈癌上皮细胞癌细胞系CasK／细胞骨架及表面超微结构的影响。方法应用20μg／ml S100A8／A9复合物作用于CasKi细胞，对细胞骨架F-肌动蛋白进行染色，应用快速共聚焦荧光显微镜观察细胞骨架的改变。在生理条件下，应用原子力显微镜（atomic force microscopy，AFM）对活体细胞进行高分辨成像，观察细胞表面超微结构及应力纤维。结果S100A8／A9复合物作用24h后宫颈癌细胞系CasKi细胞的F-肌动蛋白排列出现紊乱，主要分布于细胞的周边，细胞中央F-肌动蛋白含量明显减少。CasKi细胞经过20μg／ml S100A8／A9蛋白复合物处理前细胞核部位F-肌动蛋白光密度为92．42±5．16，经过S100A8／A972h处理后，F-肌动蛋白的光密度降为57．67±3．70，两者相比较差异具有显著的统计学意义（t=5．268，P=0．000）。AFM成像显示S100A8／A9复合物作用后细胞边缘卷曲，高度增加，伪足减少，细胞膜下应力纤维结构遭到破坏。结论S100A8／A9蛋白复合物可以对宫颈癌细胞系CasKi细胞表面的超微结构及应力纤维产生影响，并且这种影响主要是通过肌动蛋白的重新分布实现的。

英文摘要：

Objective To investigate the effect of SI00A8/A9 protein complex on the surface morphology and the F-actin network in human cervical carcinoma cell line, CasKi cells. Methods After being cultured with 20 μg/ml S100A8/A9 protein complex, the cell skeleton of the CasKi cells were observed under a confoeal scanning fluorescence microscope by staining the F-aetin network. Atomic force microscopy （AFM） was employed to reveal the change of ultrastrueture of the cell surface in vivo. Results After being cultured with the S100A8/A9 protein complex for 24 hours, the F-aetin network disorder was revealed. Most of the F-actins distributed peripherally. The OD value of the F-aetin decreased significantly from 92.42 ± 5.16 to 57.67 ± 3.70 after been treated with the S100A8/A9 （t = 5. 268, P = 0. 000）. The AFM showed a withdrawing morphology with reduced pseudopodia and destruction of stress fibers. Conclusion S100A8/A9 protein complex can change the ultrastructure of the surface of CasKi cells and its stress fibers by re-distributing of the F-actin in the cells.