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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...

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: Jun 26, 2026

Spatial Molecular Imaging of the Glycome Using Mass Spectrometry

Spatial Molecular Imaging of the Glycome Using Mass Spectrometry

Published on: November 28, 2025

Imaging the glycome.

Scott T Laughlin¹, Carolyn R Bertozzi

¹Department of Chemistry, University of California, Berkeley, CA 94720, USA.

Proceedings of the National Academy of Sciences of the United States of America

|December 24, 2008

Summary

This summary is machine-generated.

Molecular imaging can now visualize glycans in vivo using metabolic labeling and chemical reporters. This breakthrough allows studying glycan changes in living cells and organisms during development and disease.

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Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

Area of Science:

Biochemistry
Molecular Biology
Medical Imaging

Background:

Molecular imaging allows in vivo visualization of molecules with minimal environmental disruption.
Glycans are important biomolecules but challenging to image in vivo using traditional methods like lectins or antibodies.
Existing glycan detection methods are not suitable for live imaging applications.

Purpose of the Study:

To introduce and validate a novel strategy for in vivo glycan imaging.
To overcome limitations of conventional glycan detection techniques for live imaging.
To enable the study of glycan dynamics in biological systems.

Main Methods:

Employing metabolic labeling of glycans with chemical reporters.
Utilizing subsequent ligation of fluorescent probes to labeled glycans.
Applying the technique in living cells and live organisms (e.g., zebrafish).

Main Results:

Successfully visualized glycans in vivo using the developed metabolic labeling approach.
Demonstrated the feasibility of imaging glycans in living cells.
Showcased the application of this technique in live organisms, such as zebrafish.

Conclusions:

Metabolic labeling with chemical reporters provides a new method for in vivo glycan imaging.
This technique allows for the visualization of glycans in living systems.
Offers a powerful tool for investigating glycome alterations in development and disease.