Protuglikanska protutijela i glikozilacija imunoglobulina g u raku debeloga crijeva

Glycosylation changes are often described in different physiological processes and pathological conditions and as a lifestyle effect. Alterations in cancer cells metabolism result in the production of altered glycan structures, which are being recognized by the immune system that result in generation of novel anti-glycan antibodies. Presence and screening of antibodies was performed using glycan arrays. Immunoglobulin G (IgG) glycosylation was performed using plasma purification and glycan chromatography. Results show significant differences between healthy individuals and those with cancer. Antibody binding to 24/48 glycans give positive results with great statistical significance between studied sample groups. IgG glycosylation analysis shows that 10/23 glycan chromatographic peaks are changed in colorectal cancer and that galactosylation is one of the main indicators of appearance and progression of the disease. Understanding of IgG glycosylation changes and protein-glycan interactions, and the fact they are effective in numerous diseases are important for understanding biology of cancer cells.