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pmid:32042278

Quantitative site- and structure-specific N-glycoproteomics characterization of differential N-glycosylation in MCF-7/ADR cancer stem cells.

Feifei Xu · Yue Wang · Kaijie Xiao · Yechen Hu · Zhixin Tian · Yun Chen

Clinical proteomics · 2020 doi:10.1186/s12014-020-9268-7

Paper

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Experiment

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Data

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Execution

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Quantitative site- and structure-specific N-glycoproteomics characterization of differential N-glycosylation in MCF-7/ADR cancer stem cells.
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10.1186/s12014-020-9268-7
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Feifei Xu
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Yue Wang
[2]
Kaijie Xiao
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Yechen Hu
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Zhixin Tian
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Yun Chen
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Clinical proteomics
year
2020
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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Human Breast LC-MSMS - Quantitative site- and structure-specific N-glycoproteomics characterization of differential N-glycosylation in MCF-7/ADR cancer stem cells
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Complete file
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