Naslov
Altered N–glycosylation of immunoglobulin G and total plasma proteins in patients with atrial fibrillation

Autori
Radovani, Barbara ; Szavits Nossan, Janko ; Lauc, Gordan ; Gudelj, Ivan

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

Izvornik
Program and Abstracts for the 2021 Annual Meeting of the Society for Glycobiology / Colley, Karen - : Oxford University Press, 2021, 1670-1776

Skup
Society for Glycobiology (SFG) 2021 Annual Meeting “Glycobiology at the Forefront of Human Health and Disease”

Mjesto i datum
San Diego (CA), Sjedinjene Američke Države, 07.11.2021. - 10.11.2021

Vrsta sudjelovanja
Poster

Vrsta recenzije
Podatak o recenziji nije dostupan

Ključne riječi
Atrial fibrillation, immunoglobulin G, glycosylation

Sažetak
Atrial fibrillation (AF) is the most common persistent cardiac arrhythmia, affecting more than 1% of the population. It is characterized by rapid and disorganized atrial activation leading to impaired atrial function, with myocardial fibrosis being one of the main factors influencing the pathophysiological changes of the heart. Consequently, AF is a risk factor for embolic stroke and worsening heart failure and has been associated with increased morbidity and mortality [1]. Significant alterations in N-glycosylation are known to occur in some cardiovascular diseases (CVD), of which alterations in N-glycome of immunoglobulin G (IgG) are an independent risk factor for atherosclerotic CVD [2-3]. Given the importance of glycosylation in CVD and the fact that no studies of glycosylation have been performed to date in AF, a preliminary analysis of IgG and total plasma protein N-glycans was performed. The aim of this analysis was to gain insight into the status of IgG and total plasma protein N-glycans in AF, the possible existence of a causal relationship between the abundance of certain N-glycan structures and the degree of fibrosis, and AF recurrence after pulmonary vein isolation. IgG and total protein plasma N-glycans were analyzed by ultra-high performance liquid chromatography with hydrophilic interactions (HILIC-UPLC). The results obtained indicate that altered N-glycosylation occurs in patients with AF, especially in IgG N-glycans, highlighting the importance of immunoglobulin glycosylation and the possible interaction between the immune response and pathophysiological changes in AF.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Interdisciplinarne prirodne znanosti

POVEZANOST RADA