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Specific mixing facilitates the comparative quantification of phosphorylation sites with significant dysregulations
Liu, Jing1,2; Xu, Bo1; Liu, Zheyi1,2; Dong, Mingming1,2; Mao, Jiawei1,2; Zhou, Ye1,2; Chen, Jin1,2; Wang, Fangjun1; Zou, Hanfa1
关键词Mass Spectrometry Comparative Phosphoproteome Quantification Stable Isotope Labeling Mixing At Specific rAtio Extreme Relative Abundance
刊名ANALYTICA CHIMICA ACTA
2017-01-15
DOI10.1016/j.aca.2016.10.044
950页:129-137
收录类别SCI
文章类型Article
WOS标题词Science & Technology ; Physical Sciences
类目[WOS]Chemistry, Analytical
研究领域[WOS]Chemistry
关键词[WOS]GROWTH-FACTOR RECEPTOR ; QUANTITATIVE PROTEOMICS ; MASS-SPECTROMETRY ; IN-VIVO ; SILAC ; MECHANISMS ; EXPRESSION ; THROUGHPUT ; VANADATE ; PROTEINS
英文摘要Mass spectrometry (MS) based quantitative analyses of proteome and proteome post-translational modifications (PTMs) play more and more important roles in biological, pharmaceutical and clinical studies. However, it is still a big challenge to accurately quantify the proteins or proteins PTM sites with extreme relative abundances in comparative protein samples, such as the significantly dysregulated ones. Herein, a novel quantification strategy, Mixing at Specific Ratio (MaSR) before isotope labeling, had been developed to improve the quantification accuracy and coverage of extreme proteins and protein phosphorylation sites. Briefly, the comparative protein samples were firstly mixed together at specific ratios of 9:1 and 1:9 (w/w), followed with mass differentiate light and heavy isotope labeling, respectively. The extreme proteins and protein phosphorylation sites, even if the newly expressed or disappeared ones, could be accurately quantified due to all of the proteins' relative abundances had been adjusted to 2 orders of magnitude (1/9-9) by this strategy. The number of quantified phosphorylation sites with more than 20 folds changes was improved about 10 times in comparative quantification of pervanadate stimulated phosphoproteome of HeLa cells, and 134 newly generated and 21 disappeared phosphorylation sites were solely quantified by the MaSR strategy. The significantly up-regulated phosphorylation sites were mainly involved in the key phosphoproteins regulating the insulin-related pathways, such as PI3K-AKT and RAS-MAPK pathways. Therefore, the MaSR strategy exhibits as a promising way in elucidating the biological processes with significant dysregulations. (C) 2016 Elsevier B.V. All rights reserved.
语种英语
WOS记录号WOS:000390629500014
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文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/151834
专题中国科学院大连化学物理研究所
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
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Liu, Jing,Xu, Bo,Liu, Zheyi,et al. Specific mixing facilitates the comparative quantification of phosphorylation sites with significant dysregulations[J]. ANALYTICA CHIMICA ACTA,2017,950:129-137.
APA Liu, Jing.,Xu, Bo.,Liu, Zheyi.,Dong, Mingming.,Mao, Jiawei.,...&Zou, Hanfa.(2017).Specific mixing facilitates the comparative quantification of phosphorylation sites with significant dysregulations.ANALYTICA CHIMICA ACTA,950,129-137.
MLA Liu, Jing,et al."Specific mixing facilitates the comparative quantification of phosphorylation sites with significant dysregulations".ANALYTICA CHIMICA ACTA 950(2017):129-137.
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