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Related Concept Videos

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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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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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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Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
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Mast cell glycosaminoglycans.

B Mulloy1, R Lever2, C P Page3

  • 1Sackler Institute of Pulmonary Pharmacology, Institute for Pharmaceutical Science, King's College London, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NN, UK. barbara.mulloy@kcl.ac.uk.

Glycoconjugate Journal
|December 1, 2016
PubMed
Summary

Mast cells store proteins in granules, with serglycin proteoglycans carrying glycosaminoglycan (GAG) chains like heparin. Research questions the significance of variations in heparin structures within mast cell populations.

Keywords:
ChondroitinDermatanGlycosaminoglycanHeparinMast cellSerglycin

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Investigating Mast Cell Secretory Granules; from Biosynthesis to Exocytosis
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Mast cells contain granules with diverse proteins released during degranulation.
  • Serglycin proteoglycans, carrying glycosaminoglycan (GAG) side chains (heparin, chondroitin, dermatan sulphate), are crucial for tight granule protein packing.
  • While chondroitin and dermatan sulphate structures are known, mast cell heparin/heparan sulphate chain composition remains poorly understood.

Purpose of the Study:

  • To investigate the structural composition of heparin/heparan sulphate chains in mast cell granules.
  • To compare the variability of heparin structures across different mast cell populations.
  • To determine if variations in heparin structures are as significant as variations in the chondroitin/heparin mix.

Main Methods:

  • Analysis of mast cell heparin from various species and tissues.
  • Characterization of glycosaminoglycan (GAG) side chain composition.
  • Comparative structural analysis of heparin/heparan sulphate chains.

Main Results:

  • Mast cell granules contain a complex mixture of proteoglycans, primarily serglycin.
  • The glycosaminoglycan (GAG) side chains on serglycin include heparin, chondroitin sulphate, and dermatan sulphate.
  • Significant variations exist in the composition and structure of heparin/heparan sulphate chains among different mast cell types.

Conclusions:

  • The structural diversity of heparin/heparan sulphate chains in mast cells is substantial.
  • Understanding these variations is critical, especially given the medical applications of heparin.
  • Further research is needed to fully elucidate the functional implications of heparin heterogeneity in mast cells.