Thursday, May 4 | 16:00 – 16:20 | Auditorium
The majority of proteins that evolved after appearance of multicellular life are glycosylated and glycans significantly affect structure and function of these proteins. However, due to structural complexity of glycans and the absence of a direct genetic template, the analysis of protein glycosylation is much more complicated than the analysis of DNA or proteins. Consequently, the knowledge about the importance of individual variation in glycans for both normal physiological processes and diseases is still limited. By generating glycomic data for over 150,000 individuals from some of the best characterized clinical and epidemiological cohorts we enabled glycomics to meet other ‘omics. Changes in glycosylation have been observed in numerous diseases, often even before other symptoms of a disease appeared, indicating that they may reflect early steps in the molecular pathophysiology of many complex diseases. Glycans are not only biomarkers, but also functional effectors that modulate protein function and initial data from intervention studies and animal models suggest that reversing changes in glycosylation may decrease the disease risk.