DICP OpenIR
Proteomics Analysis of O-GaINAc Glycosylation in Human Serum by an Integrated Strategy
Qin, Hongqiang; Cheng, Kai; Zhu, Jun; Mao, Jiawei; Wang, Fangjun; Dong, Mingming; Chen, Rui; Guo, Zhimou; Liang, Xinmiao; Ye, Mingliang; Zou, Hanfa
Source PublicationANALYTICAL CHEMISTRY
2017-02-07
ISSN0003-2700
DOI10.1021/acs.analchem.6b02887
Volume89Issue:3Pages:1469-1476
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordSITE-SPECIFIC CHARACTERIZATION ; HUMAN CEREBROSPINAL-FLUID ; SOLID-PHASE EXTRACTION ; LINKED GLYCOPEPTIDES ; MASS-SPECTROMETRY ; N-GLYCOSYLATION ; PLASMA-PROTEINS ; OVARIAN-CANCER ; LC-MS/MS ; IDENTIFICATION
AbstractThe diversity of O-linked glycan structures has drawn increasing attention due to its vital biological roles. However, intact O-glycopeptides with different glycans are typically not well elucidated using the current methods. In this work, an integrated strategy was developed for comprehensive analysis of O-GalNAc glycosylation by combining hydrophilic interaction chromatography (HILIC) tip enrichment, beam-type collision induced decomposition (beam-CID) detection, and in silico deglycosylation method for spectra interpretation. In this strategy, the intact O-GalNAc glycopeptides were selectively enriched and the original spectra obtained by time-of-flight (TOF)-CID were preprocessed using an in silico deglycosylation method, enabling direct searching without setting multiple glycosylation modifications, which could significantly decrease the search space. This strategy was applied to analyze the O-GalNAc glycoproteome of human serum, leading to identification of 407 intact O-GalNAc glycopeptides from 93 glycoproteins. About 81% of the glycopeptides contained at least one sialic acid, which could reveal the microheterogeneity of O-GalNAc glycosylation. Up until now, this is the largest data set of intact O-GalNAc glycoforms from complex biological samples at the proteome level. Furthermore, this method is readily applicable to study O-glycoform heterogeneity in other complex biological systems.
Language英语
WOS IDWOS:000393738300014
PublisherAMER CHEMICAL SOC
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/169607
Collection中国科学院大连化学物理研究所
Corresponding AuthorYe, Mingliang
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog Res & Anal Ctr, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Qin, Hongqiang,Cheng, Kai,Zhu, Jun,et al. Proteomics Analysis of O-GaINAc Glycosylation in Human Serum by an Integrated Strategy[J]. ANALYTICAL CHEMISTRY,2017,89(3):1469-1476.
APA Qin, Hongqiang.,Cheng, Kai.,Zhu, Jun.,Mao, Jiawei.,Wang, Fangjun.,...&Zou, Hanfa.(2017).Proteomics Analysis of O-GaINAc Glycosylation in Human Serum by an Integrated Strategy.ANALYTICAL CHEMISTRY,89(3),1469-1476.
MLA Qin, Hongqiang,et al."Proteomics Analysis of O-GaINAc Glycosylation in Human Serum by an Integrated Strategy".ANALYTICAL CHEMISTRY 89.3(2017):1469-1476.
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