Comparative proteomics based on stable isotope labeling and affinity selection
Comparative proteomics based on stable isotope labeling and affinity selection
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DOI：
10.1002/jms.290
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发表时间：
2002-02-01
影响因子：
2.3
通讯作者：
Thompson, RA
中科院分区：
文献类型：
--
作者：
Regnier, FE;Riggs, L;Thompson, RA
疾病，外部刺激（例如药物和毒素）以及突变会导致蛋白质合成速率，翻译后修饰，室内运输和蛋白质在生物系统中的降解。认识和识别涉及的少数蛋白质的复杂性使生物提取物的复杂性以及蛋白质的翻译后改变可以在许多部位以多种方式发生。这里显示的是，现在正在开发基于内标技术的各种新工具和方法，以编码全球所有肽，用于对照和实验样品进行定量。这些稳定的同位素标记策略的最大优势在于，质谱仪可以迅速针对浓度变化的蛋白质以进行进一步分析。当耦合到稳定的同位素定量时，可以根据特定的结构特征的色谱选择肽类选择，以进一步关注靶向。当靶向结构特征在调节类型或疾病的类型中是特征特别有用的。靶向肽的差异显示表明，刺激特异性标记相对容易识别，并且可能是有价值的工具。版权所有（C）2002 John Wiley Sons，Ltd。
Disease, external stimuli (such as drugs and toxins), and mutations cause changes in the rate of protein synthesis, post-translational modification, inter-compartmental transport, and degradation of proteins in living systems. Recognizing and identifying the small number of proteins involved is complicated by the complexity of biological extracts and the fact that post-translational alterations of proteins can occur at many sites in multiple ways. It is shown here that a variety of new tools and methods based on internal standard technology are now being developed to code globally all peptides in control and experimental samples for quantification. The great advantage of these stable isotope-labeling strategies is that mass spectrometers can rapidly target those proteins that have changed in concentration for further analysis. When coupled to stable isotope quantification, targeting can be further focused through chromatographic selection of peptide classes on the basis of specific structural features. Targeting structural features is particularly useful when they are unique to types of regulation or disease. Differential displays of targeted peptides show that stimulus-specific markers are relatively easy to identify and will probably be diagnostically valuable tools. Copyright (C) 2002 John Wiley Sons, Ltd.