Naslov
Fucosylation of IgG heavy chains in autoimmune diseases

Autori
Dumić, Jerka ; Gornik, Ivan ; Lauc, Gordan ; Flögel, Mirna

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
28th Meeting of the Federation of European Biochemical Societies : Book of Abstracts / - Istanbul, 2002

Skup
28th Meeting of the Federation of European Biochemical Societies

Mjesto i datum
Istanbul, Turska, 20.10.2002. - 25.10.2002

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
immunoglomulin G; O-fucosylation

Sažetak
Over a half of all today known proteins are glycosylated. Although precise function of all glycans is still unknown it is well established that they determine structural features of glycoproteins, influence their folding, assembling, targeting and secretion, affect their half-life and functional characteristics. Changes of protein glycosylation have been found in many pathological conditions, but in many cases it is still unclear whether these changes are just a consequence or a cause of disease. Changes of N-glycan attached to highly conserved glycosylation site on heavy chain of immunoglobulin G (HC-IgG), are directly related to the pathogenesis of some autoimmune diseases. Our aim was to determine possible fucosylation changes of HC-IgG in multiple sclerosis (MM), juvenile rheumatoid arthritis (JRA) and rheumatoid arthritis (RA). IgG was purified from sera of 21 MM patients (14 matching controls), sera from 20 JRA patients (13 matching controls) and sera from 29 RA patients (17 matching controls), using ammonium sulfate precipitation and anion-exchange chromatography. Heavy chains were separated from light chains by SDS-PAGE followed by Western blotting, and their fucosylation was analyzed using fucose-specific Ulex europaeus I lectin. We have found that fucose was approximately 230% and 40% increased in patients with JRA and RA, respectively, while in patients with MM was reduced 30% (all p < 0.001). Although functional meaning of these changes is still unknown, elevation of 230% suggested alternative way of fucose linkage ; using HPLC-MS and HPAEC we showed, for the first time, O-linked fucose on the HC-IgG

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA