IgG N-Glycosylation Is Altered in Coronary Artery Disease

Coronary artery disease (CAD) is the most common cardiovascular disease (CVD), and previous studies have shown a significant association between N-glycosylation, a highly regulated posttranslational modification, and the development of atherosclerotic plaques. Our aim was to determine whether the N-...

Full description

Bibliographic Details
Main Authors: Barbara Radovani, Frano Vučković, Aldo P. Maggioni, Ele Ferrannini, Gordan Lauc, Ivan Gudelj
Format: Article
Language:English
Published: MDPI AG 2023-02-01
Series:Biomolecules
Subjects:
Online Access:https://www.mdpi.com/2218-273X/13/2/375
_version_ 1797622067655344128
author Barbara Radovani
Frano Vučković
Aldo P. Maggioni
Ele Ferrannini
Gordan Lauc
Ivan Gudelj
author_facet Barbara Radovani
Frano Vučković
Aldo P. Maggioni
Ele Ferrannini
Gordan Lauc
Ivan Gudelj
author_sort Barbara Radovani
collection DOAJ
description Coronary artery disease (CAD) is the most common cardiovascular disease (CVD), and previous studies have shown a significant association between N-glycosylation, a highly regulated posttranslational modification, and the development of atherosclerotic plaques. Our aim was to determine whether the N-glycome of immunoglobulin G (IgG) is associated with CAD, as N-glycans are known to alter the effector functions of IgG, which may enhance the inflammatory response in CAD. Therefore, in this study, we isolated IgG from subjects with coronary atherosclerosis (CAD+) and from subjects with clean coronaries (CAD−). The purified IgGs were denatured and enzymatically deglycosylated, and the released and fluorescently labelled N-glycans were analysed by ultra-high performance liquid chromatography based on hydrophilic interactions with fluorescence detection (HILIC-UHPLC-FLR). Sex-stratified analysis of 316 CAD− and 156 CAD+ cases revealed differences in IgG N-glycome composition. The most notable differences were observed in women, where the presence of sialylated N-glycan structures was negatively associated with CAD. The obtained chromatograms provide insight into the IgG N-glycome composition in CAD as well as the biomarker potential of IgG N-glycans in CAD.
first_indexed 2024-03-11T09:05:58Z
format Article
id doaj.art-6c4ed80f61e9481bb5b184d4a3ef8efe
institution Directory Open Access Journal
issn 2218-273X
language English
last_indexed 2024-03-11T09:05:58Z
publishDate 2023-02-01
publisher MDPI AG
record_format Article
series Biomolecules
spelling doaj.art-6c4ed80f61e9481bb5b184d4a3ef8efe2023-11-16T19:24:19ZengMDPI AGBiomolecules2218-273X2023-02-0113237510.3390/biom13020375IgG N-Glycosylation Is Altered in Coronary Artery DiseaseBarbara Radovani0Frano Vučković1Aldo P. Maggioni2Ele Ferrannini3Gordan Lauc4Ivan Gudelj5Department of Biotechnology, University of Rijeka, 51000 Rijeka, CroatiaGenos Glycoscience Research Laboratory, 10000 Zagreb, CroatiaHeart Care Foundation ANMCO Research Center, 50100 Florence, ItalyCNR Institute of Clinical Physiology, 56100 Pisa, ItalyGenos Glycoscience Research Laboratory, 10000 Zagreb, CroatiaDepartment of Biotechnology, University of Rijeka, 51000 Rijeka, CroatiaCoronary artery disease (CAD) is the most common cardiovascular disease (CVD), and previous studies have shown a significant association between N-glycosylation, a highly regulated posttranslational modification, and the development of atherosclerotic plaques. Our aim was to determine whether the N-glycome of immunoglobulin G (IgG) is associated with CAD, as N-glycans are known to alter the effector functions of IgG, which may enhance the inflammatory response in CAD. Therefore, in this study, we isolated IgG from subjects with coronary atherosclerosis (CAD+) and from subjects with clean coronaries (CAD−). The purified IgGs were denatured and enzymatically deglycosylated, and the released and fluorescently labelled N-glycans were analysed by ultra-high performance liquid chromatography based on hydrophilic interactions with fluorescence detection (HILIC-UHPLC-FLR). Sex-stratified analysis of 316 CAD− and 156 CAD+ cases revealed differences in IgG N-glycome composition. The most notable differences were observed in women, where the presence of sialylated N-glycan structures was negatively associated with CAD. The obtained chromatograms provide insight into the IgG N-glycome composition in CAD as well as the biomarker potential of IgG N-glycans in CAD.https://www.mdpi.com/2218-273X/13/2/375immunoglobulin GN-glycansglycosylationinflammationcoronary artery diseasecardiovascular disease
spellingShingle Barbara Radovani
Frano Vučković
Aldo P. Maggioni
Ele Ferrannini
Gordan Lauc
Ivan Gudelj
IgG N-Glycosylation Is Altered in Coronary Artery Disease
Biomolecules
immunoglobulin G
N-glycans
glycosylation
inflammation
coronary artery disease
cardiovascular disease
title IgG N-Glycosylation Is Altered in Coronary Artery Disease
title_full IgG N-Glycosylation Is Altered in Coronary Artery Disease
title_fullStr IgG N-Glycosylation Is Altered in Coronary Artery Disease
title_full_unstemmed IgG N-Glycosylation Is Altered in Coronary Artery Disease
title_short IgG N-Glycosylation Is Altered in Coronary Artery Disease
title_sort igg n glycosylation is altered in coronary artery disease
topic immunoglobulin G
N-glycans
glycosylation
inflammation
coronary artery disease
cardiovascular disease
url https://www.mdpi.com/2218-273X/13/2/375
work_keys_str_mv AT barbararadovani iggnglycosylationisalteredincoronaryarterydisease
AT franovuckovic iggnglycosylationisalteredincoronaryarterydisease
AT aldopmaggioni iggnglycosylationisalteredincoronaryarterydisease
AT eleferrannini iggnglycosylationisalteredincoronaryarterydisease
AT gordanlauc iggnglycosylationisalteredincoronaryarterydisease
AT ivangudelj iggnglycosylationisalteredincoronaryarterydisease