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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

6.8K
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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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.8K
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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Proteoglycans01:05

Proteoglycans

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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,...
3.9K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

3.7K
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.
3.7K
Glycosaminoglycans01:23

Glycosaminoglycans

4.7K
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...
4.7K
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

3.8K
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...
3.8K

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Related Experiment Video

Updated: Jun 7, 2025

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

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IgG Glycosylation: Biomarker, Functional Modulator, and Structural Component.

Barbara Radovani1,2, Falk Nimmerjahn2,3

  • 1Faculty of Biotechnology and Drug Development, University of Rijeka, Rijeka, Croatia.

Journal of Immunology (Baltimore, Md. : 1950)
|November 18, 2024
PubMed
Summary
This summary is machine-generated.

Immunoglobulin G (IgG) glycosylation is vital for adaptive immunity, influencing structure and function. Understanding IgG glycoforms is key for therapeutic development and optimizing immune responses.

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Glycan Node Analysis: A Bottom-up Approach to Glycomics

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Area of Science:

  • Immunology
  • Glycobiology
  • Biochemistry

Background:

  • Immunoglobulin G (IgG) antibodies are central to adaptive immunity.
  • Glycosylation of IgG is essential for maintaining its structural integrity and modulating effector functions.

Purpose of the Study:

  • To review the cell biological, therapeutic, and disease-related aspects of IgG glycosylation.
  • To explore the impact of IgG glycosylation on disease modulation and therapeutic outcomes.
  • To discuss the potential for developing vaccines that induce Ag-specific IgG with optimal glycoforms.

Main Methods:

  • Review of existing literature on IgG glycosylation.
  • Analysis of glycan structures in different IgG regions (Fab and Fc).
  • Examination of the functional consequences of IgG glycosylation.

Main Results:

  • IgG glycosylation patterns vary across distinct regions (Fab vs. Fc).
  • Glycosylation significantly impacts IgG's role in disease modulation.
  • Specific glycoforms of IgG influence therapeutic efficacy and immune responses.

Conclusions:

  • Studying IgG glycosylation is crucial for understanding its dynamic and functional impacts.
  • Insights into IgG glycosylation can advance future research and clinical applications.
  • Targeting IgG glycosylation offers potential for novel therapeutic strategies and vaccine design.