Department of Proteomics and Signal Transduction, Max-Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Amino Acids. 2011 Jul;41(2):223-33. doi: 10.1007/s00726-010-0796-8.
Analysis of plasma membrane proteins and their posttranslational modifications is considered as important for identification of disease markers and targets for drug treatment. Due to their insolubility in water, studying of plasma membrane proteins using mass spectrometry has been difficult for a long time. Recent technological developments in sample preparation together with important improvements in mass spectrometric analysis have facilitated analysis of these proteins and their posttranslational modifications. Now, large scale proteomic analyses allow identification of thousands of membrane proteins from minute amounts of sample. Optimized protocols for affinity enrichment of phosphorylated and glycosylated peptides have set new dimensions in the depth of characterization of these posttranslational modifications of plasma membrane proteins. Here, I summarize recent advances in proteomic technology for the characterization of the cell surface proteins and their modifications. In the focus are approaches allowing large scale mapping rather than analytical methods suitable for studying individual proteins or non-complex mixtures.
分析质膜蛋白及其翻译后修饰对于鉴定疾病标志物和药物治疗靶点非常重要。由于它们在水中不溶，因此很长一段时间以来，使用质谱法研究质膜蛋白一直很困难。最近在样品制备方面的技术发展以及质谱分析方面的重要改进促进了这些蛋白质及其翻译后修饰的分析。现在，大规模蛋白质组学分析可以从微量样品中鉴定数千种膜蛋白。优化的用于亲和富集磷酸化和糖基化肽的方案为质膜蛋白的这些翻译后修饰的深度特征分析开辟了新的维度。在这里，我总结了用于表征细胞表面蛋白及其修饰的蛋白质组学技术的最新进展。重点是允许大规模映射的方法，而不是适用于研究单个蛋白质或非复杂混合物的分析方法。
