earticle

영어

Glycosylation is highly sensitive to the biochemical environment and has been implicated in development and disease. Global glycan profiling of human serum based on mass spectrometry has already led to promising markers for several types of cancer and disease. However, there is no compatible tool to verify the accuracy of sample preparation. Current research and analysis of glycome, different expression methods were exist even same glycan composition. There is no standard reference. Because of these reasons, we have developed glycan map using mass spectrometry. In this study, we profiled a large of set of human sera (n=200) by MALDI-TOF and found 80 common glycan compositions. Glycan map was established based on the glycan correlation and structure connectivity. We observed 18 detected glycans regardless of individual health and environment effect. These glycans should be detected on profiling. Therefore, representative glycans can be applied to quality control reference of glycan profiling. A new glycome map was proposed to provide all possible glycan compositions and structure in human serum. By projecting serum glycans onto a glycome map, total serum N-glycan modifications can be easily characterized with high speed and high accuracy. This represents a new platform for the discovery of biomarkers resulting from variations in N-glycan biosynthesis during disease progression.