Biological importance of glycosylation.
Glycosylation is the primary cause of microheterogeneity in proteins (glycoforms). These reflect complexity at both molecular and cellular levels. Protein sugar prints are conserved and not random under normal physiological conditions. There are many potential functions of glycosylation. For instance, physical properties include: folding, trafficking, packing, stabilisation, protease protection, quaternary structure and organization of water structure. Properties relating to recognition and biological triggering are characterized by: weak interactions, multiple presentation and precise geometry. Many of the properties may only operate in a specific biological context. Changes in sugar prints may both reflect and results in physiological changes, e.g. cancer and rheumatoid arthritis. It is necessary, in many systems, to evaluate glycosylation. This requires accurate monitoring of sugar prints of using automated and predictive technology. Glycosylation often affords a sensitive means of monitoring pharmaceutical products for Quality Control.
Dwek
R A
RA
The Glycobiology Institute, University of Oxford, United Kingdom.
D000818:Animals; D001172:Arthritis, Rheumatoid / Q000276:immunology / Q000378:metabolism; D002240:Carbohydrate Sequence; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry; D010958:Plasminogen / Q000737:chemistry / Q000378:metabolism; D010959:Tissue Plasminogen Activator / Q000737:chemistry / Q000378:metabolism
D006023:Glycoproteins; D007074:Immunoglobulin G; D009844:Oligosaccharides; D010958:Plasminogen; D010959:Tissue Plasminogen Activator