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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

7.7K
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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Proteoglycans01:05

Proteoglycans

4.1K
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,...
4.1K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.1K
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...
3.1K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

6.4K
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.
6.4K
Glycosaminoglycans01:23

Glycosaminoglycans

5.4K
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...
5.4K
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

4.2K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
4.2K

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Updated: Oct 12, 2025

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

Published on: January 18, 2020

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IgG N-glycans.

Si Liu1, Xin Liu1

  • 1Key Laboratory for Biomedical Photonics of MOE, Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.

Advances in Clinical Chemistry
|November 23, 2021
PubMed
Summary
This summary is machine-generated.

Immunoglobulin G (IgG) glycosylation significantly impacts immune responses and disease. Understanding IgG N-glycans offers potential for developing novel biomarkers and therapeutic strategies for various conditions.

Keywords:
Analytical methodsBiological functionsGlycan repertoireIgG glycosylationRecent development

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Area of Science:

  • Biochemistry
  • Immunology
  • Glycobiology

Background:

  • Glycosylation is a crucial post-translational modification affecting protein function.
  • Immunoglobulin G (IgG), the most abundant serum glycoprotein, is vital for immune response.
  • Aberrant IgG glycosylation is linked to various disease states, highlighting its clinical relevance.

Purpose of the Study:

  • To review the repertoire and function of IgG glycans.
  • To discuss strategies for profiling the IgG N-glycome.
  • To explore the implications of IgG glycosylation in disease and therapeutics.

Main Methods:

  • Mass spectrometry (MS)-based techniques are primary tools for IgG N-glycome profiling.
  • Analysis includes categorizing glycans (high-mannose, complex, hybrid) and identifying modifications (fucosylation, sialylation, etc.).

Main Results:

  • IgG glycosylation influences antibody half-life, antigen binding, Fc structure, and effector functions.
  • Specific IgG N-glycans can modulate inflammatory responses.
  • IgG N-glycans show promise as biomarkers for disease diagnosis and prognosis.

Conclusions:

  • IgG glycosylation is a critical regulator of immune function and disease pathogenesis.
  • Targeted glycoengineering of IgG holds potential for developing new therapeutics.
  • Understanding IgG glycan profiles may lead to improved vaccine development.