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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.
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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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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Using sugar remodeling to study chondroitin sulfate function.

Hiroshi Kitagawa1

  • 1Department of Biochemistry, Kobe Pharmaceutical University.

Biological & Pharmaceutical Bulletin
|November 5, 2014
PubMed
Summary
This summary is machine-generated.

Chondroitin sulfate (CS) chains, a type of glycosaminoglycan, exhibit diverse functions regulated by structural modifications like sulfation. Sugar remodeling offers a promising approach to study CS chain function and its biological roles.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Chondroitin sulfate (CS) chains are glycosaminoglycans (GAGs) found on cell surfaces and in extracellular matrices, attached to proteoglycan proteins.
  • CS proteoglycans regulate crucial biological processes such as cell adhesion, proliferation, morphogenesis, and neurite outgrowth.
  • The functional diversity of CS proteoglycans arises from structural variations in CS chains, particularly through enzymatic modifications like sulfation.

Purpose of the Study:

  • To review recent findings on chondroitin sulfate (CS) function derived from studies utilizing "sugar remodeling."
  • To highlight the significance of structural variability in CS chains for determining CS proteoglycan function.
  • To emphasize sugar remodeling as a valuable method for investigating CS chain roles.

Main Methods:

  • The review focuses on studies involving "sugar remodeling," which is the experimental or therapeutic alteration of CS chains.
  • This involves perturbing specific CS biosynthetic enzymes in cells or living organisms.
  • Analysis of how these alterations impact CS chain structure and subsequent biological functions.

Main Results:

  • Structural variability of CS chains, including sulfation patterns and chain length, is finely tuned by the CS biosynthetic machinery.
  • These modifications specify the structure and function of CS proteoglycans.
  • Studies involving sugar remodeling have provided new insights into the specific functions of CS chains.

Conclusions:

  • Chondroitin sulfate (CS) chain structure, particularly its sulfation status and length, is critical for its biological functions.
  • Sugar remodeling is an effective strategy for dissecting the roles of CS chains in various biological events.
  • Further research using sugar remodeling promises to deepen our understanding of CS proteoglycan biology.