engleski

Glycosylation changes in stress and disease

It is only to be expected that glycosylation, as a complex and multistep posttranslational process undergoes changes under disturbed living conditions, regardless whether there is a stressor acting upon the organism or the organism is fighting a disease. In our studies we have witnessed the both: Changes in glycosylation patterns of serum proteins have been identified in subjects exposed to severe stress experience and stressin as the most interesting glycoprotein has been studied into more details. One of its main characteristics was the unusually high sialylation, probably as a consequence of increased activity of liver sialyltransferases that we were able to demonstrate in animal models of stress. Interaction with lectin receptors is one of the main modes of glycoconjugate action, and indeed, we have found several changes in lectins on animal models of stress. Stress induced expression of a novel lectin CBP33, and in the same time it decreased expression of galectin-3. Several diseases that have strong elements of stress in their etiology are also associated with changes in glycosylation. We have studied glycosylation of IgG in rheumatoid diseases and found that in addition to changes in galactoosylation, both rheumatoid arthritis and juvenile arthritis are associated with significant increase in IgG fucosylation. Interestingly, there is a strong line of evidence suggesting that this increase derives primarily from O-linked fucose. The underlying mechanisms of the observed changes are still mostly unknown and it is a great challenge to study defense mechanisms at the level of glycosylation.

stress; glycobiology; glycoproteins; lectins; rheumatoid arthritis

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