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Related Concept Videos

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,...
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Protein Glycosylation01:25

Protein Glycosylation

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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.
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Oligosaccharide Assembly01:24

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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.
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Inflammatory Response01:28

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An inflammatory response is a localized, nonspecific immune reaction that occurs when a tissue is injured. It is characterized by redness, swelling, heat, and pain, which are commonly called the cardinal signs and symptoms of inflammation. Inflammation can sometimes result in a loss of function.
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Glycosaminoglycans01:23

Glycosaminoglycans

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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.
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Updated: Dec 29, 2025

Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Glycosylation changes in inflammatory diseases.

Sophie Groux-Degroote1, Sumeyye Cavdarli1, Kenji Uchimura1

  • 1University Lille, CNRS, UMR 8576 - UGSF - Unite de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France.

Advances in Protein Chemistry and Structural Biology
|January 31, 2020
PubMed
Summary
This summary is machine-generated.

Glycosylation changes in cell surface glycans are linked to inflammatory diseases. This review explores alterations in O-linked glycans, glycosaminoglycans, and glycosphingolipids in cystic fibrosis and neurodegenerative diseases.

Keywords:
Cystic fibrosisGangliosidesGlycosaminoglycansGlycosylationMucinsNeurodegenerative disorders

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Cell surface glycoconjugates are crucial for biological functions like cell signaling and immune responses.
  • Aberrant glycosylation patterns are associated with various inflammatory conditions and diseases.
  • Pro-inflammatory cytokines can alter cell surface glycosylation, influencing disease development.

Purpose of the Study:

  • To review current knowledge on glycosylation changes in mucin-type O-linked glycans, glycosaminoglycans, and glycosphingolipids.
  • To focus on the role of these changes in cystic fibrosis and neurodegenerative diseases.
  • To examine the impact of altered glycosylation on cell interactions and disease progression.

Main Methods:

  • Literature review of scientific articles and research papers.
  • Synthesis of information on glycosylation pathways and their regulation.
  • Analysis of studies focusing on specific diseases like cystic fibrosis and neurodegenerative disorders.

Main Results:

  • Glycosylation alterations are observed in mucin-type O-linked glycans, glycosaminoglycans, and glycosphingolipids.
  • These changes are implicated in the pathogenesis of cystic fibrosis and neurodegenerative diseases.
  • Altered glycosylation affects cell-cell interactions and immune cell functions in inflammatory settings.

Conclusions:

  • Glycosylation plays a significant role in the development and progression of inflammatory and neurodegenerative diseases.
  • Understanding these glycosylation changes offers potential therapeutic targets.
  • Further research into specific glycan alterations is warranted for disease management.