title: [Glycosylation-dependent effector function of IgG antibodies].
abstract: The Fc fragments of pathogenic IgG autoantibodies in patients with rheumatoid arthritis are low-galactosylated and low-sialylated. In contrast, high-galactosylated and high-sialylated antigen-specific IgG antibodies are sufficient to inhibit a pro-inflammatory immune response in an antigen-specific manner and might be a promising therapeutic tool to re-establish tolerance against defined self-antigens in autoimmune patients.
authors.affiliation: Labor für Toleranz und Autoimmunität, Institut für Systemische Entzündungsforschung, Universität zu Lübeck, Ratzeburger Allee 160, 23538, Lübeck, Deutschland. Marc.Ehlers@uk-sh.de
authors.forename: M
authors.initials: M
authors.lastname: Ehlers
mesh_terms: D000818:Animals; D001172:Arthritis, Rheumatoid / Q000276:immunology*; D001323:Autoantibodies / Q000276:immunology*; D017127:Glycation End Products, Advanced / Q000276:immunology*; D006801:Humans; D007113:Immunity, Innate / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D018448:Models, Immunological; D006023:Glycoproteins
chemical_list: D001323:Autoantibodies; D017127:Glycation End Products, Advanced; D007074:Immunoglobulin G; C046179:glycosylated IgG; D006023:Glycoproteins