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Updated: Feb 21, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Glycosylation Changes in Brain Cancer
Lucas Veillon1, Christina Fakih2, Hadi Abou-El-Hassan2
1Department of Chemistry and Biochemistry, Texas Tech University , Lubbock Texas 79409, United States.
Abstract:
Protein glycosylation is a posttranslational modification that affects more than half of all known proteins. Glycans covalently bound to biomolecules modulate their functions by both direct interactions, such as the recognition of glycan structures by binding partners, and indirect mechanisms that contribute to the control of protein conformation, stability, and turnover. The focus of this Review is the discussion of aberrant glycosylation related to brain cancer. Altered sialylation and fucosylation of N- and O-glycans play a role in the development and progression of brain cancer. Additionally, aberrant O-glycan expression has been implicated in brain cancer. This Review also addresses the clinical potential and applications of aberrant glycosylation for the detection and treatment of brain cancer. The viable roles glycans may play in the development of brain cancer therapeutics are addressed as well as cancer-glycoproteomics and personalized medicine. Glycoprotein alterations are considered as a hallmark of cancer while high expression in body fluids represents an opportunity for cancer assessment.
Insights
Aberrant protein glycosylation, particularly altered sialylation and fucosylation, significantly impacts brain cancer development and progression. Understanding these glycan changes offers new avenues for early detection and targeted cancer therapeutics.
Area of Science:
- Biochemistry and Molecular Biology
- Oncology
- Glycoscience
Background:
- Protein glycosylation is a critical posttranslational modification influencing over half of all proteins.
- Glycans modulate protein function, conformation, stability, and turnover through direct and indirect mechanisms.
- Aberrant glycosylation patterns are increasingly recognized in various pathologies, including cancer.
Purpose of the Study:
- To review the role of aberrant glycosylation in brain cancer development and progression.
- To explore the clinical potential of aberrant glycosylation in brain cancer detection and treatment.
- To discuss the implications of cancer-glycoproteomics and personalized medicine in the context of brain cancer.
Main Methods:
- Literature review focusing on studies investigating protein glycosylation in brain cancer.
- Analysis of N- and O-glycan alterations, including sialylation and fucosylation.
- Examination of glycoproteomics data and its application in personalized medicine for brain cancer.
Main Results:
- Altered sialylation and fucosylation of N- and O-glycans are implicated in brain cancer initiation and advancement.
- Aberrant O-glycan expression is specifically linked to the pathogenesis of brain tumors.
- Glycoprotein alterations serve as a hallmark of cancer, with elevated expression in body fluids indicating potential for assessment.
Conclusions:
- Aberrant glycosylation represents a significant factor in brain cancer biology.
- Targeting aberrant glycans holds promise for developing novel diagnostic and therapeutic strategies for brain cancer.
- Glycoproteomics and personalized medicine approaches are crucial for leveraging glycosylation changes in clinical applications.
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