Related Experiment Video
Updated: May 18, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
[The alterations of proteins glycosylation in rheumatic diseases]
Anna Chludzińska1, Lech Chrostek, Bogdan Cylwik
1Department of Biochemical Diagnostics, Medical University in Bialystok, Poland.
Abstract:
The alterations in glycosylation of serum glycoproteins were reported in several pathological conditions including rheumatic diseases. The many studies demonstrated the occurrence of some differentially glycosylated plasma immunoglobulins, especially IgG in rheumatoid arthritis. The most characteristic features are the decrease in galactose content, the presence of N-acetylglucosamine and the increase in fucose content. The structure of oligosaccharides attached to the antibody Fc region affect the pharmacokinetics and antibody effector functions of antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity. The changes in immunoglobulin glycosylation was suggested to be important in the etiology of rheumatoid athritis and correlated with the disease severity. In addition to impaired glycosylation of imunoglubulins, in rheumatic diseases exist the disturbances in glycosylation of both acute-phase and non acute-phase response, such as alpha-1 acid glycoprotein, haptoglobin and alpha-2 macroglobulin. The alterations in glycosylation of these glycoproteins were also correlated with the disease activity.
Related Concept Videos
Proteoglycans
Protein Glycosylation
Glycosylation occurs in...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Rheumatic Heart Disease I: Introduction
Rheumatic Heart Disease II: Clinical Manifestations and Diagnostic Studies