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Protein Glycosylation

Protein Glycosylation

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.
Glycosylation occurs in...

Proteoglycans

Proteoglycans

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,...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Related Experiment Video

Updated: Feb 21, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics

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.

ACS Chemical Neuroscience

|October 6, 2017

Summary

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.

Keywords:

Brain cancer aberrant glycosylation bone marrow-derived human mesenchymal stem cells cancer stem cells carcinoembryonic antigen central nervous system glioblastoma glioma stem cells glycosylation human mucin family posttranslational modification of proteins small cell lung carcinomas

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Quantitative Immunohistochemistry of the Cellular Microenvironment in Patient Glioblastoma Resections

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Published on: July 31, 2017

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.