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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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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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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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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Perspectives in glycomics and lectin engineering.

Jan Tkac1, Tomas Bertok, Jozef Nahalka

  • 1Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dubravska Cesta 9, 845 38, Bratislava, Slovakia.

Methods in Molecular Biology (Clifton, N.J.)
|August 14, 2014
PubMed
Summary
This summary is machine-generated.

This chapter surveys advanced lectin-based glycoprotein analysis methods, including nanomaterials and novel aptamers for sensitive, label-free detection. It introduces a glycocodon concept for improved glycan-lectin interaction understanding and targeted lectin design.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Glycobiology

Background:

  • Glycoproteins play crucial roles in biological processes.
  • Accurate glycoprotein analysis is essential for understanding health and disease.
  • Lectin-based methods offer promising avenues for glycan analysis.

Purpose of the Study:

  • To provide a survey of recent advancements in lectin-based glycoprotein analysis.
  • To highlight novel techniques for sensitive and label-free glycoprofiling.
  • To introduce emerging concepts for future glycan analysis and lectin design.

Main Methods:

  • Integration of nanomaterials (nanoparticles, nanowires, nanotubes, nanochannels) for enhanced detection.
  • Utilization of novel transducing platforms for label-free glycoprotein detection.
  • Application of recombinant lectins with specific tags for oriented immobilization.
  • Development of modified lectins, peptide lectin aptamers, and DNA aptamers.

Main Results:

  • Nanomaterial integration and novel platforms enable highly sensitive, label-free glycoprofiling.
  • Recombinant lectins facilitate controlled immobilization for improved assay performance.
  • Novel aptamers and modified lectins offer new possibilities for glycan recognition.
  • The proposed glycocodon concept enhances understanding of glycan-lectin interactions.

Conclusions:

  • Recent advancements in lectin-based analysis, particularly using nanomaterials and aptamers, significantly improve glycoprotein detection sensitivity and specificity.
  • Novel approaches like the glycocodon concept are crucial for future robust glycan analysis and the rational design of lectins and aptamers.
  • These innovations pave the way for deeper insights into glycan functions and disease mechanisms.