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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,...

Glycosaminoglycans

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...

Glycocalyx and its Functions

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.

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...

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...

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Related Experiment Video

Updated: Dec 31, 2025

Author Spotlight: MAPP Protocol – Advancing Glycan Analysis

Author Spotlight: MAPP Protocol – Advancing Glycan Analysis

Published on: September 29, 2023

Glycan Array Technology.

Juana Elizabeth Reyes Martinez¹, Baptiste Thomas², Sabine Lahja Flitsch³

¹División de Ciencias Naturales y Exactas, Departamento de Biología, Universidad de Guanajuato, Guanajuato, Mexico.

Advances in Biochemical Engineering/Biotechnology

|January 8, 2020

Summary

This summary is machine-generated.

Glycan arrays are crucial for studying protein-carbohydrate interactions in glycomics. Advances in probe synthesis and linker chemistry have significantly expanded their applications.

Keywords:

Antibodies Carbohydrate-binding proteins Glycan arrays Glycoenzymes Lectins Linkers

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Area of Science:

Glycomics
Carbohydrate Chemistry
Biotechnology

Background:

Glycan arrays are vital tools for high-throughput analysis of protein-carbohydrate interactions.
They are adapted from nucleic acid and protein microarray technologies.
Carbohydrate-specific challenges in probe availability, linker chemistry, and data analysis exist.

Purpose of the Study:

To review the challenges and advancements in glycan array technology.
To highlight the expanding applications of glycan arrays in glycomics.
To provide examples of recent applications.

Main Methods:

Review of existing literature and technologies in glycan array development.
Discussion of chemical and enzymatic synthesis methods for glycan probes.
Examination of linker attachment chemistries and analytical techniques.

Main Results:

Increased availability of diverse glycan probes through synthesis.
Development of robust linker chemistries for improved array performance.
Significant expansion of glycan array applications over the last decade.

Conclusions:

Glycan arrays are indispensable for glycomics research.
Overcoming technical challenges has led to broader applications.
Future developments promise further advancements in understanding biological systems.