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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.
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...
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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,...
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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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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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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...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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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Protein-protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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The glycosaminoglycan interactome 2.0.

Sylvain D Vallet1, Coline Berthollier1, Sylvie Ricard-Blum1

  • 1Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, UMR 5246, Université de Lyon, Université Lyon 1, CNRS, Villeurbanne, France.

American Journal of Physiology. Cell Physiology
|May 11, 2022
PubMed
Summary

This study expands the glycosaminoglycan (GAG) interactome with 3,464 unique GAG-binding proteins, revealing insights into extracellular matrix organization and cell signaling. The expanded dataset differentiates protein interactions based on GAG composition.

Keywords:
extracellular matrixglycosaminoglycansinteraction networks

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Area of Science:

  • Biochemistry and Molecular Biology
  • Extracellular Matrix Research
  • Proteomics

Background:

  • Glycosaminoglycans (GAGs) are crucial polysaccharides involved in extracellular matrix organization, cell signaling, and adhesion.
  • Proteoglycans, formed by GAGs attached to core proteins, mediate diverse biological functions.
  • Understanding GAG-protein interactions is key to deciphering cellular processes.

Purpose of the Study:

  • To expand the GAG interactome dataset and identify novel GAG-binding proteins.
  • To analyze the specificity and functions of GAG-binding proteins.
  • To investigate differences in protein binding to various GAG types, including iduronic acid-containing and iduronic acid-lacking GAGs.

Main Methods:

  • Affinity chromatography was used to capture GAG-binding proteins from cell lysates and biological fluids.
  • Mass spectrometry was employed for the identification of captured proteins.
  • A comprehensive review of GAG-protein interactions and associated biological pathways was conducted.

Main Results:

  • An expanded dataset of 4,290 interactions involving 3,464 unique GAG-binding proteins was generated, significantly increasing the known GAG interactome.
  • The study details the interaction repertoire of natural GAGs and synthetic sulfated hyaluronan.
  • Differences in protein binding preferences for iduronic acid-containing GAGs (dermatan sulfate, heparin/heparan sulfate) versus those lacking iduronic acid (chondroitin sulfate, hyaluronan, keratan sulfate) were investigated.

Conclusions:

  • The expanded GAG interactome provides a valuable resource for studying GAG-protein interactions and their roles in biological processes.
  • The findings enhance our understanding of how GAG structure influences protein binding specificity.
  • This research offers new avenues for exploring the functional implications of GAG-protein networks in health and disease.