瞄准:为了阐明,血管扩张药的本地化刺激了邻蛋白质(VASP ) ,组织蛋白质的一具细胞骨架和在有丝分裂的胃的癌症房间的蛋白质家族 ases A 和 G 的底层。方法:Immunofluorescence 显微镜学被用来观察到在房间的有丝分裂的胃的癌症的分裂期间的本地化 ofalpha 导管素, VASP 和 Ser157 phosphorylated VASP (p-VASP ) 衬里 SGC-7901。结果:染色的 Immunofluorescence 证明 p-VASP 然而并非与在胃的癌症房间的有丝分裂的过程的前期,中期和后期的锭子杆和纤维上的 alpha 导管素 wasco 局部性的 VASP 衬里 SGC-7901。H89,蛋白质家族 ases Aand G 的一个禁止者,没在锭子上在 p-VASP 的本地化上有效果。结论:VASP 可以在装配并且稳定房间的有丝分裂的锭子起一个作用,并且蛋白质的 phosphorylation 是前提让它施加这功能。
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.