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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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.
Glycosylation occurs in...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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.
Multiple sugar molecules that may or may...
Proteoglycans01:05

Proteoglycans

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,...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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.
Components of...

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Lectin-based structural glycomics: a practical approach to complex glycans.

Jun Hirabayashi1, Atsushi Kuno, Hiroaki Tateno

  • 1Lectin Application and Analysis Team, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki, Japan. jun-hirabayashi@aist.go.jp

Electrophoresis
|May 6, 2011
PubMed
Summary
This summary is machine-generated.

Glycans, complex carbohydrates, present unique heterogeneity. Lectin microarrays offer a high-throughput method for direct analysis of glycoconjugates like glycoproteins and cells, advancing glycomics research.

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Area of Science:

  • Glycoscience
  • Biochemistry
  • Analytical Chemistry

Background:

  • Glycans, found in glycoproteins, glycolipids, and glycosaminoglycans, exhibit significant heterogeneity due to their biosynthesis.
  • Conventional glycan analysis requires liberation and labeling, limiting throughput for omics studies.
  • Lectins, carbohydrate-binding proteins, offer direct analysis but traditional methods lack high throughput.

Purpose of the Study:

  • To introduce the concept, strategy, and technical advancements of lectin microarrays.
  • To highlight the motivation behind exploring glycomics.
  • To present lectin microarray as a novel, high-throughput technique for glycan analysis.

Main Methods:

  • Utilizing lectin microarrays for direct detection of glycoconjugates.
  • Employing carbohydrate-binding proteins (lectins) for analysis.
  • Developing a high-throughput platform for glycan profiling.

Main Results:

  • Lectin microarrays enable direct analysis of glycoconjugates (glycoproteins, cells) without prior glycan liberation.
  • The method provides a straightforward and informative approach to differential profiling.
  • This technique addresses the throughput limitations of conventional glycan analysis methods.

Conclusions:

  • Lectin microarrays represent a significant advancement in glycomics, offering high throughput and direct analysis.
  • The technique facilitates differential profiling across various research fields.
  • This innovation supports the growing demands of omics studies in understanding complex biological systems.