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Pol. Merkur. Lek (Pol. Med. J.), 2012, XXXIII/194: 112-116 Maximize

Pol. Merkur. Lek (Pol. Med. J.), 2012, XXXIII/194: 112-116

Title: The alterations of proteins glycosylation in rheumatic diseases

Authors: Chludzińska A., Chrostek L., Cylwik B.

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The alterations of proteins glycosylation in rheumatic diseases


Chludzińska A., Chrostek L., Cylwik B.

Department of Biochemical Diagnostics, Medical University in Bialystok, Poland

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 α-1 acid glycoprotein, haptoglobin and α-2 macroglobulin. The alterations in glycosylation of these glycoproteins were also correlated with the disease activity.

Key words: glycosylation, rheumatic diseases

Pol. Merk. Lek., 2012, XXXIII, 194, 112