title: Beta 1,4-galactosyltransferase variations in rheumatoid arthritis.
abstract: Evidence indicating an important link between glycosylation changes and autoimmune rheumatic disease is presented. Attention is especially focused on 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 beta 1,4-Galactosyltransferase (GTase) that catalyses the addition of galactose to the oligosaccharide chains on this molecule. Data are presented to indicate that GTase undergoes a variety of normal and disease associated changes. These variations are believed to contribute to the pathological processes in rheumatoid disease, and a hypothesis is suggested, whereby disease is associated with the dysregulation of an integrated glycosylation network, comprising IgG galactosylation, lymphocytic GTase and anti-GTase antibodies, that is a component of the normal immune system.
authors.affiliation: Division of Immunology, St George's Hospital Medical School, London, United Kingdom.
authors.forename: A
authors.initials: A
authors.lastname: Alavi
authors.forename: J
authors.initials: J
authors.lastname: Axford
mesh_terms: D001172:Arthritis, Rheumatoid / Q000201:enzymology* / Q000276:immunology; D005690:Galactose / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism; D009237:N-Acetyllactosamine Synthase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*
chemical_list: D007074:Immunoglobulin G; D007527:Isoenzymes; D009237:N-Acetyllactosamine Synthase; D005690:Galactose