Abnormalities in the glycosylation of IgG and its clinical utility.
It is approximately ten years since the first detailed analysis of the variation in oligosaccharide structures attached to human serum IgG was published [1]. This study also showed that the percentage incidence of agalactosyl structures on the bi-antennary oligosaccharide complex linked to the Fc region, was increased in patients with rheumatoid arthritis. An earlier study [2], published in abstract from only, had also suggested that this was the case but was never followed up. In this review the considerable amount of work that has explored the clinical relevance of abnormalities in the glycosylation of IgG is analysed critically.
Isenberg
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Bloomsbury Rheumatology Unit/Division of Rheumatology, Department of Medicine, University College London, United Kingdom.
D001172:Arthritis, Rheumatoid / Q000276:immunology; D005260:Female; D005690:Galactose / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000097:blood / Q000737:chemistry; D007074:Immunoglobulin G / Q000097:blood* / Q000737:chemistry; D009844:Oligosaccharides / Q000097:blood* / Q000737:chemistry; D011247:Pregnancy; D013585:Synovitis / Q000276:immunology
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D009844:Oligosaccharides; D005690:Galactose