Yu Guangchuang, Xiao Chuan-Le, Lu Chun-Hua, Jia Hai-Tao, Ge Feng, Wang Wei, Yin Xing-Feng, Jia Hong-Ling, He Jian-Xing, He Qing-Yu
Institute of Life and Health Engineering, Jinan University, Guangzhou 510632, China.
Mol Biosyst. 2011 Feb;7(2):472-9. doi: 10.1039/c0mb00055h. Epub 2010 Nov 9.
As an in vitro model for type II human lung cancer, A549 cells resist cytotoxicity via phosphorylation of proteins as demonstrated by many studies. However, to date, no large-scale phosphoproteome investigation has been conducted on A549. Here, we performed a systematical analysis of the phosphoproteome of A549 by using mass spectrometry (MS)-based strategies. This investigation led to the identification of 337 phosphorylation sites on 181 phosphoproteins. Among them, 67 phosphoproteins and 230 phosphorylation sites identified appeared to be novel with no previous characterization in lung cancer. Based on their known functions as reported in the literature, these phosphoproteins were functionally organized into highly interconnected networks. Western blotting and immunohistochemistry analyses were performed to validate the expression of a bottleneck phosphoprotein YAP1 in cancer cell lines and tissues. This dataset provides a valuable resource for further studies on phosphorylation and lung carcinogenesis.
作为II型人类肺癌的体外模型，许多研究表明，A549细胞通过蛋白质磷酸化来抵抗细胞毒性。然而，迄今为止，尚未对A549进行大规模的磷酸化蛋白质组研究。在此，我们使用基于质谱（MS）的策略对A549的磷酸化蛋白质组进行了系统分析。该研究鉴定出181种磷酸化蛋白质上的337个磷酸化位点。其中，67种磷酸化蛋白质和230个磷酸化位点似乎是新发现的，此前在肺癌中未有过表征。根据文献报道的已知功能，这些磷酸化蛋白质在功能上被组织成高度互联的网络。进行了蛋白质免疫印迹和免疫组织化学分析，以验证癌细胞系和组织中瓶颈磷酸化蛋白质YAP1的表达。该数据集为进一步研究磷酸化和肺癌发生提供了宝贵资源。
