A Case-control Study in an Orcadian Population Investigating the Relationship between Human Plasma N-glycans and Metabolic Syndrome

Glycosylation refers to the enzymatic post-translational modification in which the addition of complex oligosaccharide molecules (glycans) enriches protein complexity and functional diversity. Glycans have a broad spectrum of biological roles, including their influence on protein folding, cell signaling and immune function. Alongside the genome and proteome,the human glycome is subject to immense variation. This variation arises as the reactions that link individual sugar units together are influenced heavily by several factors, both genetic and environmental, including cell metabolism, genomic enzyme expression and nutrient availability. N-glycosylation, in which the glycan is linked with nitrogen of asparagine or arginine side-chains, is the most common type of glycosidic bond. N-glycan profiles have been found to remain highly stable over periods of time, with even up to one year between measurements. This suggests that alterations to human N-glycan profiles may be due to pathophysiological mechanisms or complex environmental exposures.

Recent advances in high throughput analytical technology, including High Performance Liquid Chromatography (HPLC), have fueled a growing interest in the role of glycans in health and disease. Glycans have alreadybeen implicated in the pathology of numerous inflammatory disorders, including inflammatory bowel disease, various cancers and rheumatoid arthritis.