ArticleClinical proteomics2017
Simultaneous analyses of N-linked and O-linked glycans of ovarian cancer cells using solid-phase chemoenzymatic method.
Article in Clinical proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 45 citations in OpenAlex.
- Identification and characterization of inulinases by bioinformatics analysis of bacterial glycoside hydrolases family 32 (GH32).Engineering in life sciences · 2023Article
- A MATLAB-based app to improve LC-MS/MS data analysis for N-linked glycan peak identification.BMC bioinformatics · 2023Article
- Site-specific glycosylation of SARS-CoV-2: Big challenges in mass spectrometry analysis.Proteomics · 2022Review
- Mass Spectrometry Imaging for Glycome in the Brain.Frontiers in neuroanatomy · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- RNAi-Mediated Silencing of Pgants Shows Core 1Frontiers in physiology · 2021Article
- Deep Structural Analysis and Quantitation of O-Linked Glycans on Cell Membrane Reveal High Abundances and Distinct Glycomic Profiles Associated with Cell Type and Stages of Differentiation.Analytical chemistry · 2020Article
- Mass Spectrometry Imaging of N-Glycans from Formalin-Fixed Paraffin-Embedded Tissue Sections Using a Novel Subatmospheric Pressure Ionization Source.Analytical chemistry · 2019Article
- Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses.Chemical reviews · 2018Review
- Identification of Sialic Acid Linkages on Intact Glycopeptides via Differential Chemical Modification Using IntactGIG-HILIC.Journal of the American Society for Mass Spectrometry · 2018Article
- Overexpression of Exportin-5 Overrides the Inhibitory Effect of miRNAs Regulation Control and Stabilize Proteins via Posttranslation Modifications in Prostate Cancer.Neoplasia (New York, N.Y.) · 2017Article
- Simultaneous quantification of N- and O-glycans using a solid-phase method.Nature protocols · 2017Article
- Protein glycosylation in lung cancer from a mass spectrometry perspective.Mass spectrometry reviewsReview
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
backgroundGlycans play critical roles in a number of biological activities. Two common types of glycans, N-linked and O-linked, have been extensively analyzed in the last decades. N-glycans are typically released from glycoproteins by enzymes, while O-glycans are released from glycoproteins by chemical methods. It is important to identify and quantify both N- and O-linked glycans of glycoproteins to determine the changes of glycans.
methodsThe effort has been dedicated to study glycans from ovarian cancer cells treated with O-linked glycosylation inhibitor qualitatively and quantitatively. We used a solid-phase chemoenzymatic approach to systematically identify and quantify N-glycans and O-glycans in the ovarian cancer cells. It consists of three steps: (1) immobilization of proteins from cells and derivatization of glycans to protect sialic acids; (2) release of N-glycans by PNGase F and quantification of N-glycans by isobaric tags; (3) release and quantification of O-glycans by β-elimination in the presence of 1-phenyl-3-methyl-5-pyrazolone (PMP).
resultsWe used ovarian cancer cell lines to study effect of O-linked glycosylation inhibitor on protein glycosylation. Results suggested that the inhibition of O-linked glycosylation reduced the levels of O-glycans. Interestingly, it appeared to increase N-glycan level in a lower dose of the O-linked glycosylation inhibitor. The sequential release and analyses of N-linked and O-linked glycans using chemoenzymatic approach are a platform for studying N-glycans and O-glycans in complex biological samples.
conclusionThe solid-phase chemoenzymatic method was used to analyze both N-linked and O-linked glycans sequentially released from the ovarian cancer cells. The biological studies on O-linked glycosylation inhibition indicate the effects of O-glycosylation inhibition to glycan changes in both O-linked and N-linked glycan expression.
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