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Fucosylation of IgG heavy chains in autoimmune diseases (CROSBI ID 504251)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija

Dumić, Jerka ; Gornik, Ivan ; Lauc, Gordan ; Flögel, Mirna Fucosylation of IgG heavy chains in autoimmune diseases // FEBS Forum for Young Scientists : Book of Abstracts / Makarow, Maja ; Ozben, Tomris ; Saris, Nina (ur.). Istanbul: Federation of European Biochemical Societies (FEBS), 2002. str. 30-x

Podaci o odgovornosti

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

engleski

Fucosylation of IgG heavy chains in autoimmune diseases

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

immunoglomulin G; O-fucosylation

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Podaci o prilogu

30-x.

2002.

objavljeno

Podaci o matičnoj publikaciji

FEBS Forum for Young Scientists : Book of Abstracts

Makarow, Maja ; Ozben, Tomris ; Saris, Nina

Istanbul: Federation of European Biochemical Societies (FEBS)

Podaci o skupu

FEBS Forum for Young scientists

predavanje

18.10.2002-20.10.2002

Istanbul, Turska

Povezanost rada

Biologija