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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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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,...
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Glycosaminoglycans01:23

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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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When T cells with CD4 markers are activated, they give rise to two types of effector cells: helper T cells and regulatory T cells. Meanwhile, T cells with CD8 markers differentiate into effector cytotoxic T cells. The differentiation of CD4 T cells into helper T cell subsets, such as Th1, Th2, and Th17 cells, is dependent on the antigen type, antigen-presenting cell, and regulatory cytokines.
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The Rhesus (Rh) antigen is crucial in determining blood groups and ensuring compatibility during blood transfusions.
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Immunoglobulin G Subclass-Specific Glycosylation Changes in Rheumatoid Arthritis.

Dániel Szabó1,2, Balázs Gyebrovszki3, Eszter Szarka3

  • 1MS Proteomics Research Group, HUN-REN Research Centre for Natural Sciences, 1117 Budapest, Hungary.

International Journal of Molecular Sciences
|October 16, 2025
PubMed
Summary
This summary is machine-generated.

This study reveals that N-glycosylation of anti-citrullinated protein antibodies (ACPAs) in rheumatoid arthritis (RA) correlates with disease severity. Isoform-specific analysis is crucial for understanding these complex changes in IgG glycosylation.

Keywords:
anti-citrullinated protein antibodiesarthritisglycosylationimmunoglobulin G isoformsrheumatoid

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Area of Science:

  • Immunology
  • Glycobiology
  • Rheumatology

Background:

  • Rheumatoid arthritis (RA) is a common inflammatory polyarthritis.
  • Anti-citrullinated protein antibodies (ACPAs) are key diagnostic markers for RA, present in 60-80% of patients.
  • Fc N-glycosylation of IgG autoantibodies significantly impacts their effector functions.

Purpose of the Study:

  • To compare Fc N-glycosylation of ACPA IgG versus non-ACPA IgG within the same RA patients and healthy controls.
  • To investigate IgG isoform-specific glycosylation patterns in RA.
  • To correlate glycosylation features with clinical inflammatory markers and disease activity scores.

Main Methods:

  • Isolation of ACPA and normal serum IgG from patients and controls.
  • Trypsin digestion of IgG and peptide mixture separation using reversed-phase nanoLC.
  • Analysis of glycoform abundance using a Bruker Maxis II Q-TOF mass spectrometer.

Main Results:

  • Significant negative correlation found between galactosylation/sialylation of ACPA IgG and inflammatory markers (CRP, ESR) and rheumatoid factor (RF).
  • Non-ACPA IgG showed a significant negative correlation between glycosylation and disease activity score (DAS).
  • Isoform-specific analysis revealed that IgG1 explains changes in bisecting GlcNAc, while fucosylation invariance results from opposing changes in two isoforms.

Conclusions:

  • Fc N-glycosylation patterns of IgG, particularly in an isoform-specific manner, are altered in RA patients.
  • Glycosylation of ACPA IgG and non-ACPA IgG shows distinct correlations with disease markers.
  • Isoform-specific analysis is essential for a comprehensive understanding of IgG glycosylation in RA pathogenesis and as potential biomarkers.