engleski

Glycosylation changes in rheumatoid diseases

More than a half of all known proteins contain covalently attached oligosaccharides that represent a significant part of their molecular structure. It is estimated that over 500 specific enzymes (glycosidases and glycosyltransferases) are involved in the synthesis of carbohydrate structures on glycoconjugates, and the whole process is very complex and energetically expensive for the cell. Due to very high structural variability and the lack of adequate methods to analyze it, carbohydrate parts of glycoconjugates were ignored by most of the scientific community until only few years ago. However, thanks to the development of novel methods, in the last years there is an exponential increase in the knowledge about the physiological roles of carbohydrate structures. As well as many other diseases, rheumatoid arthritis is associated with specific changes in protein glycosylation. Majority of studies focused on galactosylation of IgG, but recently we demonstrated that the most prominent glycosylation change in both rheumatoid arthritis and juvenile rheumatoid arthritis is the increase in fucosylation. Using a novel method based on recently developed BioprobeŽ technology we were able to show that juvenile rheumatoid arthritis is also associated with changes in the activity of serum lectins. Although the functional significance of these changes are still not known, they could prove to be a valuable diagnostic marker for rheumatoid diseases.

Glycobiology; Glycoproteins; Lectins; Rheumatoid Arthritis

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