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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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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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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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Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
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Imaging Glycosaminoglycan Modification Patterns In Vivo.

Hannes E Bülow1,2

  • 1Department of Genetics, Albert Einstein College of Medicine, Bronx, NY, USA. hannes.buelow@einsteinmed.org.

Methods in Molecular Biology (Clifton, N.J.)
|October 9, 2021
PubMed
Summary

Researchers developed a transgenic method to visualize glycosaminoglycan (GAG) domains in live organisms. This technique allows direct observation of heparan sulfate (HS) and chondroitin sulfate (CS) domains, advancing GAG research.

Keywords:
CaenorhabditisChondroitin sulfateDermatan sulfateGlycosaminoglycansHeparan sulfateLive imagingNon-genetically encoded moleculesSingle chain variable fragment (scFv) antibody

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Developmental Biology

Background:

  • Glycosaminoglycans (GAGs), including heparan sulfates (HS) and chondroitin sulfates (CS), are complex polysaccharides crucial for protein binding and interactions.
  • GAG chains exhibit non-uniform modifications, creating distinct domains essential for biological functions.
  • Current methods struggle to visualize these GAG domains in vivo due to their non-genetic encoding.

Purpose of the Study:

  • To develop a novel transgenic approach for direct visualization of HS and CS domains in live organisms.
  • To overcome limitations of conventional methods in studying GAG domain localization and dynamics.
  • To enable genetic analysis of GAG domain biosynthesis and function.

Main Methods:

  • Utilized transgenic expression of fluorescently tagged single chain variable fragment (scFv) antibodies specific to HS and CS.
  • Applied the technique in live Caenorhabditis elegans for in vivo visualization.
  • Enabled concomitant co-labeling of multiple GAG domains.

Main Results:

  • Successfully visualized HS and CS domains in live C. elegans with high cellular specificity.
  • Demonstrated evolutionary conservation of GAG domain visualization.
  • Established a method for studying GAG dynamics and potential for genetic analysis.

Conclusions:

  • Transgenic scFv antibody expression provides an unprecedented tool for visualizing GAG domains in vivo.
  • This approach facilitates the study of GAG biology, dynamics, and biosynthesis.
  • Opens new avenues for genetic dissection of GAG function and interactions.