Glycan signatures in rheumatic diseases and their associated functional implications NatRevRheumatol LUMC_Leiden rheumaticdisease disease glycan Glycobiology Glycosylation
By Dr. Liji Thomas, MDNov 28 2022Reviewed by Danielle Ellis, B.Sc. The addition of sugars to a protein structure may affect the stability of the protein, interactions of receptors with ligands, and signaling pathway activity. This modification, called glycosylation, is linked to inflammation and disease progression.
Both O- and N-glycosylation have been identified and occur through distinct pathways. The final signature is affected by the availability of sugars, enzymes, and transporters required for glycosylation and the extent to which the right molecular regions are open to such reactions.
Active RA shows a distinct pattern of glycan residues on both the Fc and Fab domains of IgG autoantibodies, while patients in remission show another specific profile. The absence or removal of galactosyl residues on the Fc domain is associated with active, progressive, or relapsing disease and could be a useful biomarker for rheumatic diseases.
Mechanisms of action Future research should explore the mechanisms of inflammation associated with the presence of IgG Fc sugars comprising fucosyl but not galactosyl residues. Some possibilities include steric hindrance by fucosyl residues on the Fc domain that prevents the activation of the corresponding Fcγ receptor, FcγRIIIa, reducing binding affinity and cytotoxicity by up to 20-fold.
In RA, synovial fibroblasts show a poor concentration of surface sialyl residues in response to the altered cytokine pattern. This inhibits their binding to galectin-3, causing the release of a different pattern of cytokines characteristic of a pro-inflammatory switch.
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