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Titlebook: Glycoimmunology; Azita Alavi,John S. Axford Book 1995 The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer

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Lectin-Carbohydrate Interactions in Disease,nd CD8. T-lymphocytes in a number of diseases including systemic lupus erythematosus, rheumatoid arthritis (RA), Behcet’s disease and IgA nephropathy. We have demonstrated that calcium independent binding to this receptor is mediated by the O-linked disaccharide Galβ3GalNAc which is associated with
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Glycosylation of Antibody Molecules,ype” effector functions. Thus, whilst residual binding activity of aglycosylated IgGs for human FCγRI, mouse FCγRII and Clq have been demonstrated biological activities mediated through human FCγRII and FCγRIII and the C1 component of complement are ablated.
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The Effects of Altered Glycosylation of IgG on Rheumatoid Factor-Binding and Immune Complex Formatitis. This involved a decrease in the amount of galactose on the Fc biantennary oligosaccharides resulting in chain termination with N-acetylglucosamine. We have shown similar changes in two animal models of arthritis (i) where DBA/1 mice were immunised with type II collagen [2] and (ii) in the spont
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An Introduction to Glycosylation and Rheumatic Disease, labelled and oligosaccharides (Oxford Glycosystems) and the other is based on high pH anion exchange, coupled with electrochemical detection (Dionex Carbohydrate System), which allows determination of the monosaccharide composition as well as mapping of the oligosaccharide moieties.
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Abnormalities in the Glycosylation of IgG and its Clinical Utility,ed [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 form only, had also suggested that this was the
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,β1,4-Galactosyltransferase Variations in Rheumatoid Arthritis,the interrelationship between reduced galactosylation of the oligosaccharides of IgG, auto-sensitization to which is thought to be of central importance in the pathogenesis of rheumatoid arthritis (RA), and the enzyme β 1,4-Galactosyltransferase (GTase) that catalyses the addition of galactose to th
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Unbelebte äußere Krankheitsursacheno acid sequon of Asn-Xxx-Ser/Thr for N-glycosylation, the amino acids Ser/Thr for O-glycosylation and the C terminal amino acid in the GPI anchor of membrane bound glycoproteins. Typically a glycoprotein has greater than three glycan sites, each site containing between 10 and 30 structures. The pres
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