PXD015987 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | An integrated MS data processing strategy for fast identification, in-depth and reproducible quantification of protein O-glycosylation in large cohorts of human urine samples |
Description | Protein O-glycosylation has long been recognized to be closely associated with many diseases, particularly with tumor proliferation, invasion and metastasis. The ability to efficiently profile the variation of O-glycosylation in large-scale clinical samples provides an important approach for the development of biomarkers for cancer diagnosis and for therapeutic response evaluation. Therefore, mass spectrometry (MS)-based techniques for high throughput, in-depth and reliable elucidation of protein O-glycosylation in large clinical cohorts are in high demand. However, the wide existence of serine and threonine residues in the proteome and the tens of mammalian O-glycan types lead to extremely large searching space composed of millions of theoretical combinations of peptides and O-glycans for intact O-glycopeptide database searching. As a result, exceptionally long time is required for database searching which is a major obstacle in O-glycoproteome studies of large clinical cohorts. More importantly, due to the low abundance and poor ionization of intact O-glycopeptides and the stochastic nature of data-dependent MS2 acquisition, substantially elevated missing data levels are inevitable as the sample number increases, which undermines the quantitative comparison across samples. Therefore, we report a new MS data processing strategy that integrates glycoform-specific database searching, reference library-based MS1 feature matching and MS2 identification propagation for fast identification, in-depth and reproducible label-free quantification of O-glycosylation of human urinary proteins. This strategy increases the database searching speeds by up to 20-fold and leads to a 30-40% enhanced intact O-glycopeptide quantification in individual samples with an obviously improved reproducibility. In total, we obtained quantitative information for 1068 intact O-glycopeptides across 36 healthy human urine samples with a 30-40% reduction in the amount of missing data. This is currently the largest dataset of urinary O-glycoproteome and demonstrates the application potential of this new strategy in large-scale clinical investigations. |
HostingRepository | PRIDE |
AnnounceDate | 2020-02-04 |
AnnouncementXML | Submission_2020-02-04_09:12:05.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Xinyuan Zhao |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; complex glycosylation; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-10-23 06:12:00 | ID requested | |
⏵ 1 | 2020-02-04 09:12:07 | announced | |
Publication List
Zhao X, Zheng S, Li Y, Huang J, Zhang W, Xie Y, Qin W, Qian X, -Glycosylation in a Large Cohort of Human Urine Samples. Anal Chem, 92(1):690-698(2020) [pubmed] |
Keyword List
submitter keyword: O-glycopeptide |
urine |
sialic acid |
Contact List
Weijie Qin |
contact affiliation | National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing 102206, PR China |
contact email | aunp_dna@126.com |
lab head | |
Xinyuan Zhao |
contact affiliation | National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing 102206, PR China |
contact email | zhaoxinyuan@foxmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD015987
- Label: PRIDE project
- Name: An integrated MS data processing strategy for fast identification, in-depth and reproducible quantification of protein O-glycosylation in large cohorts of human urine samples