ArticleMolecular & cellular proteomics : MCP2012
How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Global O-glycoproteome enrichment and analysis enabled by a combinatorial enzymatic workflow.Cell reports methods · 2024Article
- Review
- In-Depth Site-Specific O-Glycosylation Analysis of Glycoproteins and Endogenous Peptides in Cerebrospinal Fluid (CSF) from Healthy Individuals, Mild Cognitive Impairment (MCI), and Alzheimer's Disease (AD) Patients.ACS chemical biology · 2022Article
- The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Recent Advances in Lectin-Based Affinity Sorbents for Protein Glycosylation Studies.Frontiers in molecular biosciences · 2021Review
- Large-scale site-specific mapping of the O-GalNAc glycoproteome.Nature protocols · 2020Article
- Finding the Sweet Spot in ERLIC Mobile Phase for Simultaneous Enrichment of N-Glyco and Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2019Article
- Fluorometric visualization of mucin 1 glycans on cell surfaces based on rolling-mediated cascade amplification and CdTe quantum dots.Mikrochimica acta · 2019Article
- Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries.Nature methods · 2019Article
- Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples.Trends in analytical chemistry : TRAC · 2019Article
- Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).Molecular systems biology · 2018Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Analysis of Mammalian O-Glycopeptides-We Have Made a Good Start, but There is a Long Way to Go.Molecular & cellular proteomics : MCP · 2018Review
- Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization.Journal of the American Society for Mass Spectrometry · 2017Article
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides.Glycoconjugate journal · 2016Review
- O-glycosylation sites identified from mucin core-1 type glycopeptides from human serum.Glycoconjugate journal · 2016Article
- Site-specific O-Glycosylation Analysis of Human Blood Plasma Proteins.Molecular & cellular proteomics : MCP · 2016Article
- Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.Molecular & cellular proteomics : MCP · 2015Article
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3 authors.
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Abstract
Two different workflows were tested in order to develop methods that provide deeper insight into the secreted O-glycoproteome. Bovine serum samples were subjected to lectin affinity-chromatography both at the protein- and peptide-level in order to selectively isolate glycopeptides with the most common, mucin core-1 sugar. This enrichment step was implemented with either protein-level mixed-bed ion-exchange chromatography or with peptide-level electrostatic repulsion hydrophilic interaction chromatography. Both methods led to at least 65% of the identified products being glycopeptides, in comparison to ≈ 25% without the additional chromatography steps [Darula, Z., and Medzihradszky, K. F. (2009) Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum. Mol. Cell. Proteomics 8, 2515-2526]. In order to improve not only the isolation but also the characterization of the glycopeptides exoglycosidases were used to eliminate carbohydrate extensions from the directly peptide-bound GalNAc units. Consequent tandem MS analysis of the mixtures using higher-energy collision-dissociation and electron-transfer dissociation led to the identification of 124 glycosylation sites in 51 proteins. While the electron-transfer dissociation data provided the bulk of the information for both modified sequence and modification site assignment, the higher-energy collision-dissociation data frequently yielded confirmation of the peptide identity, and revealed the presence of some core-2 or core-3 oligosaccharides. More than two-thirds of the sites as well as the proteins have never been reported modified.
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