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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
KeywordMass Spectrometry Comparative Phosphoproteome Quantification Stable Isotope Labeling Mixing At Specific rAtio Extreme Relative Abundance
Source PublicationANALYTICA CHIMICA ACTA
2017-01-15
DOI10.1016/j.aca.2016.10.044
Volume950Pages:129-137
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordGROWTH-FACTOR RECEPTOR ; QUANTITATIVE PROTEOMICS ; MASS-SPECTROMETRY ; IN-VIVO ; SILAC ; MECHANISMS ; EXPRESSION ; THROUGHPUT ; VANADATE ; PROTEINS
AbstractMass 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.
Language英语
WOS IDWOS:000390629500014
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/151834
Collection中国科学院大连化学物理研究所
Affiliation1.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
Recommended Citation
GB/T 7714
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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