IgG N-Glycosylation Is Altered in Coronary Artery Disease

• Published in: Biomolecules (Basel, Switzerland) Vol. 13; no. 2; p. 375
• Main Authors: Radovani, Barbara, Vučković, Frano, Maggioni, Aldo P., Ferrannini, Ele, Lauc, Gordan, Gudelj, Ivan
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.02.2023; MDPI
• Subjects: Angina pectoris; Arteriosclerosis; Atherosclerosis; Biomarkers; Cardiovascular disease; Cardiovascular diseases; Chemical properties; Chromatography; Chromatography, High Pressure Liquid; Complications and side effects; Coronary Artery Disease; Coronary heart disease; Coronary vessels; Development and progression; Disease prevention; Female; Glycosylation; Health aspects; Heart diseases; High-performance liquid chromatography; Humans; Immunoglobulin G; Immunoglobulin G - chemistry; Inflammation; Lipoproteins; N-glycans; Plasma; Polysaccharides; Polysaccharides - chemistry; Proteins; Solvents; Vein & artery diseases; Croatia; United States > US; coronary artery disease; cardiovascular disease; glycosylation; immunoglobulin G; N-glycans; inflammation
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom13020375

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.