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- Title
A quantitative N-glycoproteomics study of cell-surface N-glycoprotein markers of MCF-7/ADR cancer stem cells.
- Authors
Wang, Yue; Xu, Feifei; Chen, Yun; Tian, Zhixin
- Abstract
Isotopic-labeling quantitative N-glycoproteomics characterization of cell-surface differentially expressed N-glycosylation in MCF-7/ADR cancer stem cells (CSCs) relative to MCF-7/ADR cells was carried out at the intact N-glycopeptide level with trypsin digestion, ZIC-HILIC enrichment, isotopic diethyl labeling, RPLC-MS/MS analysis of the 1:1 mixture, and GPSeeker DB search. With a spectrum-level false discovery rate of ≤ 1%, 1,336 intact N-glycopeptides from the combination of 301 unique peptide backbones and 169 putative N-glycan linkages (52 monosaccharide compositions) were identified; the corresponding intact N-glycoproteins and N-glycosites were 289 and 305, respectively, among which 176 N-glycosites were confirmed with GlcNAc-containing site-determining b/y fragment ion pairs. The N-glycan moieties in 546 intact N-glycopeptide IDs were identified with more than one structure-diagnostic fragment ions where multiple linkage structures exist for each of the monosaccharide compositions. With the criteria of ≥ 1.5-fold change and p value < 0.05, 72 cell-surface differentially expressed intact N-glycopeptides (DEGPs) were found in MCF-7/ADR CSCs relative to MCF-7/ADR cells, where 8 and 64 were downregulated and upregulated, respectively.
- Subjects
CANCER stem cells; TUMOR markers; FALSE discovery rate; DAUGHTER ions; ION pairs; GLYCOPROTEINS; TRYPSIN
- Publication
Analytical & Bioanalytical Chemistry, 2020, Vol 412, Issue 11, p2423
- ISSN
1618-2642
- Publication type
Article
- DOI
10.1007/s00216-020-02453-7