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Quantitative Site- and Structure-specific N-glycoproteomics Characterization of Differential N-glycosylation in MCF-7/ADR Cancer Stem Cells

Overview
Journal Clin Proteomics
Publisher Biomed Central
Date 2020 Feb 12
PMID 32042278
Citations 12
Authors
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Abstract

Background: Cancer stem cells (CSCs) are reported to be responsible for tumor initiation, progression, metastasis, and therapy resistance where P-glycoprotein (P-gp) as well as other glycoproteins are involved. Identification of these glycoprotein markers is critical for understanding the resistance mechanism and developing therapeutics.

Methods: In this study, we report our comparative and quantitative site- and structure-specific N-glycoproteomics study of MCF-7/ADR cancer stem cells (CSCs) vs. MCF-7/ADR cells. With zic-HILIC enrichment, isotopic diethyl labeling, RPLC-MS/MS (HCD) analysis and GPSeeker DB search, differentially expressed N-glycosylation was quantitatively characterized at the intact N-glycopeptide level.

Results: 4016 intact N-glycopeptides were identified with spectrum-level FDR ≤ 1%. With the criteria of ≥ 1.5 fold change and p value < 0.05, 247 intact N-glycopeptides were found differentially expressed in MCF-7/ADR CSCs as putative markers. Raw data are available via ProteomeXchange with identifier PXD013836.

Conclusions: Quantitative site- and structure-specific N-glycoproteomics characterization may help illustrate the cell stemness property.

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