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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
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The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
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Oligosaccharide Assembly01:24

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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.
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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.
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Related Experiment Video

Updated: May 3, 2026

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies
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Core fucosylation and IgG function in NAIT.

Richard H Aster1

  • 1BLOODCENTER OF WISCONSIN;

Blood
|January 25, 2014
PubMed
Summary

Maternal antibodies targeting human platelet antigen 1a (HPA 1a) in neonatal alloimmune thrombocytopenia (NAIT) lack core fucose. These fucosylated antibodies more effectively promote the destruction of antibody-coated platelets.

Area of Science:

  • Immunology
  • Hematology
  • Glycobiology

Background:

  • Neonatal alloimmune thrombocytopenia (NAIT) is an immune condition where maternal antibodies target fetal platelets.
  • Human platelet-specific antigen 1a (HPA 1a) is a common target for these pathogenic antibodies.

Purpose of the Study:

  • To investigate the role of oligosaccharide structures, specifically core fucose, in HPA 1a-specific antibodies.
  • To determine how antibody fucosylation impacts the clearance of antibody-coated platelets in NAIT.

Main Methods:

  • Analysis of oligosaccharide content in maternal HPA 1a-specific antibodies.
  • Functional assays measuring phagocytosis of antibody-coated platelets by immune cells.

Main Results:

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  • Maternal HPA 1a-specific antibodies associated with NAIT showed a deficiency in core fucose residues.
  • Antibodies lacking core fucose were more potent in promoting phagocytosis of antibody-coated platelets compared to fucosylated antibodies.

    • Conclusions:

    • The absence of core fucose in HPA 1a-specific antibodies enhances their ability to trigger platelet destruction.
    • Targeting antibody fucosylation may offer a novel therapeutic strategy for managing NAIT.