Pregled bibliografske jedinice broj: 1072493
Alpha-1-acid glycoprotein glycosylation in individuals at increased risk of type 2 diabetes
Alpha-1-acid glycoprotein glycosylation in individuals at increased risk of type 2 diabetes // 12th International Symposium on Glycosyltransferases (GlycoT 2020)
online, 2020. 6, 1 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 1072493 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Alpha-1-acid glycoprotein glycosylation in
individuals at increased risk of type 2 diabetes
Autori
Keser, Toma ; Tijardović, Marko ; Gornik, Ivan ; Lukić, Edita ; Lauc, Gordan ; Gornik, Olga ; Novokmet, Mislav
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Skup
12th International Symposium on Glycosyltransferases (GlycoT 2020)
Mjesto i datum
Online, 21.06.2020. - 23.06.2020
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
alpha-1-acid glycoprotein ; glycosylation ; high-throughput ; biomarker ; type 2 diabetes
Sažetak
Glycosylation, the addition of oligosaccharide chains is one of the most abundant co- and post- translational modifications. Changes in human plasma N-glycome are associated with many diseases and represent promising diagnostic and prognostic biomarkers. Recently, we showed that the increased branching of plasma N-glycan structures is associated with higher risk of developing type 2 diabetes. There we measured the whole plasma protein N-glycome, which is comprised of different glycans originating from many different glycoproteins. The most likely candidate for the origin of those glycan changes is alpha-1-acid glycoprotein (AGP), since it is the source of the most branched glycan structures present in the whole plasma protein N-glycome. Using a high- throughput and site-specific AGP N-glycosylation LC- MS analysis method, we analyzed N-linked glycans on a glycopeptide level from plasma of 59 patients who developed hyperglycemia during ICU hospitalization due to an acute illness (a known predictor of type 2 diabetes) and compared them with glycans from 49 similar ICU patients who remained normoglycemic. Samples were taken after the cessation of inflammatory process was confirmed (based on blood count and CRP). Individuals at higher risk of diabetes presented increased N-glycan branching on AGP’s second glycosylation site and lower sialylation of N-glycans on AGP’s third and AGP1’s fourth glycosylation site. Although this must be confirmed on a larger prospective cohort, it indicates that site-specific AGP N-glycan profile could aid in development of stratification methods which could reliably distinguish individuals who are at high risk of type 2 diabetes.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Farmacija, Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
Medicinski fakultet, Zagreb,
Klinički bolnički centar Zagreb,
GENOS d.o.o.
Profili:
Olga Gornik Kljaić
(autor)
Ivan Gornik
(autor)
Gordan Lauc
(autor)
Mislav Novokmet
(autor)
Toma Keser
(autor)