engleski

Glycan structures – a source of new diagnostic information

Although glycosylation is the most abundant posttranslational modification and importance of glycoconjugates for many biological processes including fertilization, immune defence, viral replications, microbial infection, cell growth, adhesion and inflammation is well documented, using of glycans as a source of diagnostic information was until recently quite poor. There were two main reasons for such situation: enormous individual glycan variability (microheterogeneity) and lack of routinely applicable methods for glycan analysis. Still, over the years analysis of glycans was indispensable step for diagnosis of hereditary disorders caused by defect glycan metabolism, such as Tay-Sachs disease, Gaucher disease, muscle-eye-brain disease, Fukuyama-type Congenital Muscular Dystrophy (FCMD) and Congenital Disorders of Glycosylation (CDG). But in the last few years emerging pool of evidences that many acquired diseases (e.g. cancer, diabetes, allergies, autoimmune, cardiovascular, neurological and gastric disorders) are followed by specific changes of glycosylation that can be cause or consequence of a disease, initiated tremendous enhancement of analytical tools and approaches for glycan analysis (MALDI-MS, HPAEC, FACE). Individuals demonstrate variability in their glycan profiles and this manifests in physiological diversity. This is why, individualization of therapy in near future will require identifying glycan’ s biomarkers unique to a specific patient population – “ glycomics profiles” that can be use to determine how well an individual will respond to different drugs in terms of efficacy and toxicity (pharmacoglycomics). The most promising tool in that field is GlycoChip&reg ; technology – microarray of complex carbohydrates, allowing accurate and efficient analysis of protein-glycan interactions. But not only glycans but also their specific physiological receptors – lectins are affected in many diseases. A new analytical tool – Glycoprobes&reg ; synthesized in our lab allows measuring of lectin activity in complex biological sample providing in that way much accurate and valuable data than lectin quantity. In the naxt few years analysis of specific changes of glycosylation and lectin activity will become indispensable step for diagnosis, prognosis and treatment of many diseases.

glycosylation; glycoproteins; lectins; diseases; diagnosis

nije evidentirano