ArticleLife (Basel, Switzerland)2021
The Analysis of Human Serum N-Glycosylation in Patients with Primary and Metastatic Brain Tumors.
Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Solvent Interaction Analysis: A New Lens for Protein Structure and Diagnostics.International journal of molecular sciences · 2026Review
- Automation of N-glycan purification using amine-functionalized NiFeScientific reports · 2026Article
- Serum N-Glycomics with Nano-LC-QToF LC-MS/MS Reveals N-Glycan Biomarkers for Glioblastoma, Meningioma, and High-Grade Meningioma.Journal of proteome research · 2025Article
- Medical Relevance, State-of-the-Art and Perspectives of "Sweet Metacode" in Liquid Biopsy Approaches.Diagnostics (Basel, Switzerland) · 2024Review
- Association between immunoglobulin G N-glycosylation and lupus nephritis in female patients with systemic lupus erythematosus: a case-control study.Frontiers in immunology · 2023Article
- High-Throughput Glycomic Methods.Chemical reviews · 2022Review
- Sonochemical Combined Synthesis of Nickel Ferrite and Cobalt Ferrite Magnetic Nanoparticles and Their Application in Glycan Analysis.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The identification of patients with different brain tumors is solely built on imaging diagnostics, indicating the need for novel methods to facilitate disease recognition. Glycosylation is a chemical modification of proteins, reportedly altered in several inflammatory and malignant diseases, providing a potential alternative route for disease detection. In this paper, we report the quantitative analysis of serum N-glycosylation of patients diagnosed with primary and metastatic brain tumors. PNGase-F-digested and procainamide-labeled serum glycans were purified by magnetic nanoparticles, followed by quantitative liquid chromatographic analysis. The glycan structures were identified by the combination of single quad mass spectrometric detection and exoglycosidase digestions. Linear discriminant analysis provided a clear separation of different disease groups and healthy controls based on their N-glycome pattern. Altered distribution of biantennary neutral, sialylated but nonfucosylated, and sialylated-fucosylated structures were found to be the most significant changes. Our results demonstrate that serum glycosylation monitoring could improve the detection of malignancy.
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