Relative quantification: characterization of bias, variability and fold changes in mass spectrometry data from iTRAQ-labeled peptides.
Relative quantification: characterization of bias, variability and fold changes in mass spectrometry data from iTRAQ-labeled peptides.
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DOI：
10.1021/pr2001308
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发表时间：
2011-09-02
影响因子：
4.4
通讯作者：
Oberg, Ann L.
中科院分区：
文献类型：
--
作者：
Mahoney, Douglas W.;Therneau, Terry M.;Heppelmann, Carrie J.;Higgins, LeeAnn;Benson, Linda M.;Zenka, Roman M.;Jagtap, Pratik;Nelsestuen, Gary L.;Bergen, H. Robert, III;Oberg, Ann L.
关键词：
鸟枪式质谱蛋白质组学是一种发现生物标志物的强大技术，有可能导致非侵入性疾病筛查机制。基于MS的蛋白质组学技术在生物标志物发现中的成功应用需要对所选分析平台的偏倚、再现性、方差和真实可检测差异的准确预期。表征MS测定中固有的变异性至关重要，并且应影响生物样品中观察到的差异的测量结果的解释。在此，我们描述了观察到的偏倚、方差结构和检测加标数据集中已知差异的能力，其中已知定义样本之间的真实相对丰度，随后在两个MS平台上使用iTRAQ®技术进行测量。在这些数据集中观察到了全球偏差。测量的变异性是平均丰度的函数。倍数变化偏向零，倍数变化的方差是蛋白质质量和丰度的函数。本文提供的信息将是有价值的实验设计和分析所得数据。
Shotgun proteomics via mass spectrometry (MS) is a powerful technology for biomarker discovery which has the potential to lead to non-invasive disease screening mechanisms. Successful application of MS-based proteomics technologies for biomarker discovery requires accurate expectations of bias, reproducibility, variance, and the true detectable differences in platforms chosen for analyses. Characterization of the variability inherent in MS assays is vital and should affect interpretation of measurements of observed differences in biological samples. Here we describe observed biases, variance structure and the ability to detect known differences in spike-in data sets for which true relative abundance among defined samples were known and were subsequently measured with the iTRAQ® technology on two MS platforms. Global biases were observed within these data sets. Measured variability was a function of mean abundance. Fold changes were biased towards the null and variance of a fold change was a function of protein mass and abundance. The information presented herein will be valuable for experimental design and analysis of the resulting data.
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