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Related Concept Videos

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.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
Multiple sugar molecules that may or may...
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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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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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Related Experiment Video

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Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Glycan Node Analysis: A Bottom-up Approach to Glycomics.

Sahba Zaare1, Jesús S Aguilar1, Yueming Hu1

  • 1Department of Chemistry & Biochemistry, The Biodesign Institute - Center for Personalized Diagnostics, Arizona State University.

Journal of Visualized Experiments : Jove
|June 11, 2016
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Summary

This study introduces a refined gas chromatography-mass spectrometry method to detect and quantify glycan structures in biofluids, aiding cancer research by identifying deregulated glycosyltransferases.

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Area of Science:

  • Glycomics
  • Mass Spectrometry
  • Biochemistry

Background:

  • Glycans play crucial roles in cellular functions.
  • Cancer and other diseases alter glycan structures.
  • Detecting specific glycans in biofluids is challenging.

Purpose of the Study:

  • To develop an improved GC-MS method for glycan analysis.
  • To enhance the detection and quantification of glycan nodes.
  • To identify deregulated glycosyltransferases in pathological conditions.

Main Methods:

  • Refined sample preparation including permethylation and extraction.
  • Gas chromatography-mass spectrometry (GC-MS) for detecting monosaccharides.
  • A novel normalization method using extracted ion chromatogram (XIC) areas.

Main Results:

  • Improved reproducibility and yield in glycan analysis.
  • Quantification of individual glycan nodes and identification of changes in glycome.
  • Demonstrated potential for detecting deregulated glycosyltransferases.

Conclusions:

  • The enhanced GC-MS method offers a complementary approach to traditional glycomics.
  • This method facilitates the analysis of clinical biofluids for disease biomarker discovery.
  • Further optimization could improve detection limits for broader clinical application.