Abstract
Inflammatory diseases are accompanied by numerous changes at the site of inflammation as well as many systemic physiological and biochemical changes. In the past two decades more and more attention is being paid to changes in glycosylation and in this review we describe some of the changes found on main serum proteins (α1-acid glycoprotein, immunoglobulin G, immunoglobulin A, transferrin, haptoglobin, α2-macroglobulin, C-reactive protein, and others). Molecular background and physiological importance of most of these changes are yet to be discovered, but it is evident that glycosylation plays an important role in the inflammatory response. Maybe the greatest value of these changes currently lays in their potential diagnostic and prognostic usage, either in combination with current diagnostic markers or on their own. However, determining glycan structures is still technically too complex for most clinical laboratories and further efforts have to be made to develop simple analytical tools to study changes in glycosylation.
Highlights
Inflammation is a complex biological response of an organism to harmful stimuli, such as pathogens, damaged cells, or irritants
Similar changes have been observed in juvenile rheumatoid arthritis [51,52], lectin study [53] reported no difference between galactosylation of juvenile rheumatoid arthritis patients and the control group until patients were divided in a group of those having acute phase of disease and those in remission
Development of an enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody directed against abnormally glycosylated serum alpha2-macroglobulin which was capable of recognizing changes of glycosylation in systemic lupus erythematosus patients contributed further to this findings and may be useful in differential diagnosis [90]
Summary
Inflammation is a complex biological response of an organism to harmful stimuli, such as pathogens, damaged cells, or irritants. In acute inflammation the increase in biantennary structures was found to reach the maximum value in the early phase of inflammation (2nd day after surgical trauma), after which it decreased to control levels [21,27, 28] Kinetics of this change in acute inflammation differs from the variation in the content of fucosylated glycans [21]. Work on the prognostic value of α1-acid glycoprotein glycosylation in septic shock [30], indicated that a modest elevation in biantennary glycans in combination with a strong increase in sialyl-Lewis X was associated with higher mortality than a high transient increase in biantennary glycans with gradually increasing sialyl-Lewis X expression This clearly demonstrates that the manner of changes in glycan structures can be associated with disease severity
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