ArticleFrontiers in oncology2021
Serum Protein N-Glycosylation Signatures of Neuroblastoma.
Article in Frontiers in oncology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Review
- Engineered Protein Modification: A New Paradigm for Enhancing Biosensing Sensitivity and Diagnostic Accuracy.Biosensors · 2025Review
- Review
- Reduction of N-Acetylglucosaminyltransferase-I Activity Promotes Neuroblastoma Invasiveness and EGF-Stimulated Proliferation In Vitro.International journal of translational medicine (Basel, Switzerland) · 2024Article
- Glycosylation: mechanisms, biological functions and clinical implications.Signal transduction and targeted therapy · 2024Review
- Elevated level of multibranched complex glycan reveals an allergic tolerance status.Clinical proteomics · 2024Article
- Limited N-Glycan Processing Impacts Chaperone Expression Patterns, Cell Growth and Cell Invasiveness in Neuroblastoma.Biology · 2023Article
- Sialic Acid-Siglec Axis in Human Immune Regulation, Involvement in Autoimmunity and Cancer and Potential Therapeutic Treatments.International journal of molecular sciences · 2021Review
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNeuroblastoma is the most common extracranial childhood solid tumor which accounts for 10% of the malignancies and 15% of the cancer fatalities in children. N-glycosylation is one of the most frequent post-translation protein modification playing a vital role in numerous cancers. N-glycosylation changes in neuroblastoma patient serum have not been studied in existing reports. The comprehensive analyses of serum N-glycomics in neuroblastoma can provide useful information of potential disease biomarkers and new insights of the pathophysiology in neuroblastoma.
methodsThe total serum protein N-glycosylation was analyzed in 33 neuroblastoma patients and 40 age- and sex-matched non-malignant controls. N-glycans were enzymatically released, derivatized to discriminate linkage-specific sialic acid, purified by HILIC-SPE, and identified by MALDI-TOF-MS. Peak areas were acquired by the software of MALDI-MS sample acquisition, processed and analyzed by the software of Progenesis MALDI.
resultsThree glyco-subclasses and six individual N-glycans were significantly changed in neuroblastoma patients compared with controls. The decreased levels of high mannose N-glycans, hybrid N-glycans, and increased levels of α2,3-sialylated N-glycans, multi-branched sialylated N-glycans were observed in neuroblastoma patients. what is more, a glycan panel combining those six individual N-glycans showed a strong discrimination performance, with an AUC value of 0.8477.
conclusionsThis study provides new insights into N-glycosylation characteristics in neuroblastoma patient serum. The analyses of total serum protein N-glycosylation could discriminate neuroblastoma patients from non-malignant controls. The alterations of the N-glycomics may play a suggestive role for neuroblastoma diagnosis and advance our understanding of the pathophysiology in neuroblastoma.
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