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首页> 外文期刊>International Journal of Radiation Biology: Covering the Physical, Chemical, Biological, and Medical Effects of Ionizing and Non-ionizing Radiations >Ionizing radiation modules of the expression and tyrosine phosphorylation of the focal adhesion-associated proteins focal adhesion kinase (FAK) and its substrates p130cas and paxillin in A549 human lung carcinoma cells in vitro.
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Ionizing radiation modules of the expression and tyrosine phosphorylation of the focal adhesion-associated proteins focal adhesion kinase (FAK) and its substrates p130cas and paxillin in A549 human lung carcinoma cells in vitro.

机译：电离辐射模块在体外对A549人肺癌细胞中黏着斑相关蛋白局灶性粘附激酶（FAK）及其底物p130cas和paxillin的表达和酪氨酸磷酸化的影响。

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PURPOSE: Focal adhesion kinase (FAK) is involved in the regulation of many cellular processes, including cell survival and death, proliferation and migration. The same endpoints are influenced by ionizing radiation (IR). Therefore, study was performed to determine the effect of IR on the expression and phosphorylation of FAK and two of its substrates, p130cas and paxillin, in vitro. MATERIALS AND METHODS: Exponentially growing A549 lung carcinoma cells were exposed to 6 Gy X-rays. Protein expression and the extent of tyrosine phosphorylation were investigated by immunoprecipitation experiments and Western blotting analysis using specific or unspecific phosphotyrosine antibodies. Immunofluorescence staining in combination with confocal laser scanning microscopy was done to localize the proteins within the cell. RESULTS: Tyrosine phosphorylation, of Mr 110 000 150 000 and 65 000-75 000 protein bands, was induced within 30 min after exposure to IR. Three of these proteins were identified as FAK, p130cas and paxillin. IR induced phosphorylation of FAK (tyr397 and tyr925) but did not change FAK expression. Additionally, IR induced phosphorylation of paxillin (tyr31 and tyr181) within 30 min and an up-regulation of paxillin expression 2-6 h after exposure. Furthermore, a higher amount of phosphorylated p130cas was found in irradiated cells. Immunofluorescence staining demonstrated that in A549 cells, all three proteins colocalize at sites of focal adhesions at the cytoplasmic face of the cell membrane and to lamellopodia. CONCLUSIONS: The data indicate that these focal adhesion-associated proteins are modulated by IR and thus are likely to play a role in the cellular response to IR. These proteins might represent attractive targets to modulate FAK-initiated signalling pathways, which may be involved in improved radioresistance and, furthermore, in important pathological phenomena such as tumour growth and metastatic phenotypes.
机译：目的：黏着斑激酶（FAK）参与许多细胞过程的调节，包括细胞存活和死亡，增殖和迁移。相同的端点受电离辐射（IR）的影响。因此，进行了研究以确定IR对FAK及其两种底物p130cas和paxillin的表达和磷酸化的影响。材料与方法：指数生长的A549肺癌细胞暴露于6 Gy X射线。使用特异性或非特异性磷酸酪氨酸抗体，通过免疫沉淀实验和蛋白质印迹分析研究了蛋白质表达和酪氨酸磷酸化程度。结合共聚焦激光扫描显微镜进行了免疫荧光染色，以定位细胞内的蛋白质。结果：酪氨酸磷酸化，先生先生1100 000 150 000和65 000-75 000蛋白带，被暴露于红外后30分钟内。这些蛋白质中的三个被鉴定为FAK，p130cas和paxillin。红外诱导FAK（tyr397和tyr925）磷酸化，但不改变FAK表达。此外，IR在暴露后30分钟内诱导了paxillin（tyr31和tyr181）的磷酸化，并且paxillin表达上调。此外，在受辐照的细胞中发现了大量的磷酸化p130cas。免疫荧光染色表明，在A549细胞中，所有这三种蛋白共定位在细胞膜细胞质表面粘膜和粘膜病的粘着斑部位。结论：数据表明这些黏着斑相关蛋白受IR调节，因此可能在细胞对IR的反应中发挥作用。这些蛋白质可能代表了调节FAK起始信号通路的诱人靶标，可能参与了增强的抗辐射性，而且还参与了重要的病理现象，例如肿瘤生长和转移表型。

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