Related Experiment Video

Updated: May 27, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

N-Glycosylation pattern of recombinant human CD82 (KAI1), a tumor-associated membrane protein

Hong Wang1, Wei Zhang, Jian Zhao

  • 1Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China.

Journal of Proteomics
|November 30, 2011
PubMed

Insights

This study characterizes the N-linked glycosylation of CD82 (KAI1), revealing three sites and unique glycan structures. These findings may influence CD82

Area of Science:

  • Glycomics
  • Proteomics
  • Cancer Biology

Background:

  • CD82 (KAI1) is a membrane glycoprotein known to suppress tumor cell migration, invasion, and metastasis.
  • Glycosylation of CD82 is implicated in cell adhesion and motility, but its N-glycosylation pattern remains undescribed.

Purpose of the Study:

  • To comprehensively characterize the N-linked glycosylation pattern of recombinant human CD82.
  • To identify and describe the specific N-glycans and glycosylation sites on CD82.

Main Methods:

  • Integrative proteomic and glycomic analyses.
  • Enzymatic (glycosidase, protease) and chemical (permethylation) digestions.
  • Mass spectrometry (MS), site-directed mutagenesis, and lectin blotting.

Main Results:

  • Three N-glycosylation sites were identified on CD82.
  • A novel putative glycosylation site at Asn(157) was discovered.
  • A heterogeneous N-linked glycan profile was detailed, featuring bisecting N-acetylglucosamine, (α-2,6) N-acetylneuraminic acid, and core fucose epitopes.

Conclusions:

  • The N-glycosylation pattern of CD82 is highly complex and heterogeneous.
  • Identified glycan epitopes are associated with cell adhesion and cancer metastasis.
  • Understanding CD82 glycosylation may offer insights into its anti-cancer properties.

More Related Videos

Analysis of SCAP N-glycosylation and Trafficking in Human Cells11:27

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

Related Concept Videos

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,...
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...