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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...

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Investigating cell surface galectin-mediated cross-linking on glycoengineered cells.

Brian Belardi1, Geoff P O'Donoghue, Adam W Smith

  • 1Department of Chemistry, and Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, California 94720, USA.

Journal of the American Chemical Society
|May 1, 2012
PubMed
Summary

Researchers provide direct evidence for galectin-1 cross-linking cell surface glycans. This study introduces a novel method to visualize galectin-mediated cellular aggregation, advancing understanding of galectin functions.

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Published on: December 26, 2011

Area of Science:

  • Biochemistry
  • Cell Biology
  • Polymer Chemistry

Background:

  • Galectins are glycan-binding proteins involved in cellular processes.
  • The galectin lattice hypothesis suggests galectins oligomerize cell surface molecules.
  • Direct evidence for galectin-mediated cross-linking on live cells is currently lacking.

Purpose of the Study:

  • To develop a method for probing galectin-induced multimerization of glycoconjugates on live cell surfaces.
  • To provide direct evidence for galectin-1-mediated cross-linking of cell surface glycans.
  • To investigate the role of glycan structure in galectin-ligand interactions.

Main Methods:

  • Synthesis of well-defined glycopolymers (GPs) using RAFT polymerization.
  • Functionalization of GPs with galectin-binding glycans, a lipid anchor, and a fluorophore.
  • Insertion of GPs into live cell membranes and measurement of fluorescence lifetime and diffusion time.

Main Results:

  • Observed direct evidence of galectin-1-mediated extended cross-linking of engineered glycoconjugates.
  • Demonstrated that galectin-1-induced cross-linking is dependent on glycan structure.
  • Validated a novel platform for studying galectin-ligand interactions in a live cell context.

Conclusions:

  • The developed platform enables direct visualization of galectin-mediated cellular aggregation.
  • This research provides critical support for the galectin lattice hypothesis.
  • The findings offer new insights into galectin ligand specificity and cellular functions.