Pregled bibliografske jedinice broj: 1015613
Fc-linked immunoglobulin G N-glycosylation in Fcy receptor knock-out mice
Fc-linked immunoglobulin G N-glycosylation in Fcy receptor knock-out mice // EMBO Workshop: Antibodies and Complement: Effector Functions, Therapies and Technologies
Girona, Španjolska, 2018. xx, 1 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 1015613 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Fc-linked immunoglobulin G N-glycosylation in Fcy receptor knock-out mice
Autori
Zaytseva, Olga O. ; Seeling, Michaela ; Krištić, Jasminka ; Lauc, Gordan ; Pezer, Marija ; Nimmerjahn, Falk
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Skup
EMBO Workshop: Antibodies and Complement: Effector Functions, Therapies and Technologies
Mjesto i datum
Girona, Španjolska, 28.06.2018. - 01.07.2018
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
Fcγ receptor ; IgG N-glycan profile ; immunoglobulin G ; N-glycosylation
Sažetak
Immunoglobulin G (IgG) is involved in a number of both protective and pathogenic immune response pathways. By binding to receptors specific for its Fc region – Fcγ receptors (FcγRs) – expressed on the surface of various immune cells, IgG is involved in the regulation of both, the innate and adaptive arms of the immune response. In mice, as well as in humans, each IgG molecule contains a single biantennary N-glycan covalently attached to the conserved N-glycosylation site on each of its heavy chains. Multiple in vitro studies have confirmed that the composition of IgG N-glycans affects its binding to the FcγRs. Polyclonal IgG glycosylation is known to vary markedly in different physiological and pathological states. However, little is known about the mechanisms that regulate the composition of IgG glycome. In this study we investigated whether a feedback regulation of IgG glycosylation depending on the available repertoire of FcRs exists in vivo. To this purpose, we analyzed serum IgG glycosylation in mice deficient for a single FcγR (FcγRI-/-, FcγRIIB-/-, FcγRIII-/-, FcγRIV-/-), all activating FcγRs (FcRγ-/-) or all FcγRs (FcRγ-/-FcγRIIB-/-) on C57Bl/6 background. We also analyzed IgG N-glycan profiles of FcγRIIB-/-, FcRγ-/- and FcRγ-/- FcγRIIB-/- on Balb/c background. IgG isolated from serum was digested with trypsin and the resulting Fc-glycopeptides were analysed with liquid chromatography - electrospray ionization - mass spectrometry.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Temeljne medicinske znanosti
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
GENOS d.o.o.
