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Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
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Published on: January 18, 2020

Immunological studies on glycated human IgG.

Saman Ahmad1, Moinuddin, Asif Ali

  • 1Department of Biochemistry, J.N. Medical College, Faculty of Medicine, Aligarh Muslim University, Aligarh, India.

Life Sciences
|May 29, 2012
PubMed
Summary

Advanced glycation end product (AGE) modified IgG (AGE-IgG) is highly immunogenic, generating neo-epitopes. These findings suggest AGE-modified IgG may contribute to autoantibodies in rheumatoid arthritis (RA).

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Area of Science:

  • Immunology
  • Biochemistry
  • Rheumatology

Background:

  • Advanced glycation end products (AGEs) are formed on proteins, including IgG, through non-enzymatic glycation.
  • AGE modification of IgG can alter its structure and potentially its immunogenicity.
  • Understanding the immunogenicity of AGE-modified IgG is crucial for investigating autoimmune diseases like rheumatoid arthritis (RA).

Purpose of the Study:

  • To investigate the immunogenicity of in vitro glycated human IgG (AGE-IgG) in experimental animals.
  • To characterize the binding properties of antibodies generated against AGE-IgG.
  • To explore the potential role of AGE-modified IgG in the pathogenesis of rheumatoid arthritis.

Main Methods:

  • Human IgG was glycated in vitro with glucose, and N(ε)-(carboxymethyl)lysine (CML) formation was confirmed.
  • Polyclonal antibodies were raised in rabbits against native and AGE-IgG.
  • Antibody specificity and cross-reactivity were assessed using competitive inhibition assays, band shift assays, and ELISA.

Main Results:

  • AGE-IgG demonstrated the formation of CML, confirming glycation.
  • AGE-IgG was highly immunogenic, inducing antibodies with specific binding to AGE-IgG over native IgG.
  • Cross-reactivity studies revealed diverse antigen-binding characteristics, with glycated proteins and amino acids acting as inhibitors.

Conclusions:

  • Antibodies against AGE-IgG exhibit antigen-binding properties similar to autoantibodies found in rheumatoid arthritis (RA).
  • Unique neo-epitopes generated on AGE-modified IgG, particularly under oxidative stress, may trigger autoantibody production in RA patients.
  • This study highlights a potential mechanism linking AGE modification of IgG to the autoimmune processes in RA.