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Updated: May 26, 2026

11:36
Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Glycans as cancer biomarkers
Barbara Adamczyk1, Tharmala Tharmalingam, Pauline M Rudd
1Dublin-Oxford Glycobiology Laboratory, NIBRT-The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland.
Biochimica Et Biophysica Acta
|December 20, 2011
Summary
Serum glycoprotein changes, including fucosylation and sialylation, show promise as novel cancer biomarkers. Advanced glycan analysis and high-throughput platforms enable efficient biomarker discovery for improved cancer prognosis and monitoring.
Area of Science:
- Glycoscience
- Biomarker Discovery
- Cancer Research
Background:
- Non-invasive serum biomarkers are crucial for disease management.
- Glycosylation changes are increasingly recognized as significant in disease progression.
Purpose of the Study:
- To review potential serum glycoprotein biomarkers for various cancers.
- To discuss advancements in glycan analysis methods and future trends.
Main Methods:
- Analysis of serum glycoproteins for aberrant glycan structures.
- Application of high-throughput platform technologies for large-scale sample analysis.
- Review of glycosylation analysis evolution and future directions.
Main Results:
- Aberrant glycans are consistently found in association with cancer.
- Fucosylation and sialylation are significantly modified in most cancers.
- Glycosylation differences distinguish cancer patients from controls.
Conclusions:
- Glycobiology offers a promising avenue for cancer biomarker identification.
- High-throughput glycomics, integrated with other -omics, facilitates systems glycobiology.
- Modified glycan structures can enhance existing cancer biomarkers.
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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