Phosphorylated vasodilator-stimulated phosphoprotein is localized on mitotic spindles of the gastric cancer cell line SGC-7901

AIM： To elucidate the localization of vasodilator stimulated phosphoprotein （VASP）, a cytoskeletal organizing protein and a substrate of protein kinases A and G in mitotic gastric cancer cells. METHODS： Immunofluorescence microscopy was used to observe the localization of α-tubulin, VASP and Ser157...

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Published in:World journal of gastroenterology : WJG 2006-12, Vol.12 (46), p.7478-7481
Main Authors: Tao, Yan, Chen, Yong-Chang, Wang, Ying, Zhang, Zhi-Jian, Xu, Wen-Rong
Format: Article
Language:English
Subjects:
Cell Adhesion Molecules - chemistry
Cell Adhesion Molecules - metabolism
Cell Line, Tumor
Gastric Cancer
Humans
Microfilament Proteins - chemistry
Microfilament Proteins - metabolism
Microscopy, Fluorescence
Phosphoproteins - chemistry
Phosphoproteins - metabolism
Phosphorylation
Spindle Apparatus - metabolism
Stomach Neoplasms - metabolism
Tubulin - metabolism
有丝分裂
磷酸化
纺锤体
胃癌细胞系
血管扩张剂刺激磷蛋白
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Summary:AIM： To elucidate the localization of vasodilator stimulated phosphoprotein （VASP）, a cytoskeletal organizing protein and a substrate of protein kinases A and G in mitotic gastric cancer cells. METHODS： Immunofluorescence microscopy was used to observe the localization of α-tubulin, VASP and Ser157 phosphorylated VASP （p-VASP） in interphase of mitotic gastric cancer of the cell line SGC-7901. RESULTS： Immunofluorescence staining showed that p-VASP but not VASP was co-localized with α-tubulin on spindle poles and fibers in prophase, metaphase and anaphase of the mitotic process of the gastric cancer cell line SGC-7901. H89, an inhibitor of protein kinases A and G, had no effect on the localization of p-VASP on the spindles. CONCLUSION： VASP may play a role in assembling and stabilizing the mitotic spindle of cells, and phosphorylation of the protein is the precondition for it to exert this function.
ISSN:1007-9327
2219-2840
DOI:10.3748/wjg.v12.i46.7478