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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...
Membrane Carbohydrates01:30

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
Membrane Carbohydrates01:30

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Decoding sugar functions by identifying target glycoproteins.

Naoyuki Taniguchi1, Eiji Miyoshi, Jianguo Gu

  • 1Department of Disease Glycomics, Institute for Microbial Diseases, Osaka University, 2-1 Suita, Osaka 565-0871, Japan. tani52@wd5.so-net.ne.jp <tani52@wd5.so-net.ne.jp>

Current Opinion in Structural Biology
|September 15, 2006
PubMed
Summary

Glycosyltransferase genes are key to understanding sugar chains in glycobiology. Defects in alpha1-6 fucosylation in mice led to lung damage, highlighting the role of specific sugar structures in disease.

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Area of Science:

  • Glycobiology
  • Molecular Biology
  • Biochemistry

Background:

  • Glycosyltransferase genes are crucial for synthesizing glycoconjugates, which are vital for cellular functions.
  • Understanding sugar chain biosynthesis is essential for decoding their roles in biological processes and diseases.

Purpose of the Study:

  • To explore the functional significance of specific glycosyltransferase genes in glycoconjugate biosynthesis.
  • To investigate the impact of altered N-glycan structures on glycoprotein function and cellular recognition, particularly in cancer.
  • To elucidate the role of alpha1-6 fucosylation in lung health and disease.

Main Methods:

  • Gene identification and characterization of glycosyltransferase functions.
  • Analysis of branched N-glycan structures and their impact on glycoproteins.
  • Utilizing a mouse model with a specific defect in alpha1-6 fucosylation to study lung pathology.
  • Investigating signaling pathways, including transforming growth factor-beta receptor signaling.

Main Results:

  • Specific glycosyltransferases enable the biosynthesis of branched N-glycan structures, functionally modifying glycoproteins.
  • A mouse model with alpha1-6 fucosylation deficiency exhibited emphysema-like lung changes and alveolar degradation.
  • Dysregulation of transforming growth factor-beta receptor signaling was implicated in the observed lung pathology.

Conclusions:

  • Glycosyltransferase genes are pivotal in glycoconjugate biosynthesis and have significant implications for cellular function and disease.
  • Altered fucosylation patterns, specifically alpha1-6 fucosylation, can lead to severe lung conditions.
  • Functional glycomics and target protein identification offer promising avenues for understanding disease mechanisms in the post-genomic era.