Structures of glycoproteins are characterized by their complexity and diversity. To clarify their functions, synthetic approaches are considered to be promising. Development of synthetic methodologies for efficient and facile preparation of oligosaccharides is a focal issue in carbohydrate chemistry. In light of their structural diversity, practical strategy to facilitate the synthesis of oligosaccharide is expected to be highly valuable. Glycoprotein glycans are known to play numerous biological roles, both intra- and intra-cellularly, through their interaction with various proteins such as lectins, glycosidases, and glycosyltransferases. However, their precise analysis has been hindered by structural heterogeneity of glycoproteins. Under these circumstances, our effort has been directed to synthesis of glycoprotein glycans and related probes for analysis of their intracellular functions.<br/>In glycoprotein folding events in the ER, incorporation and detachment of glucose to high-mannose-type glycans on immaturely folded glycoproteins serve as key signals. To understand them, our efforts have been directs to analyze enzymes and chaperones in the ER, such as Calnexin/Calreticulin, UGGT (UDP-Glc: glycoprotein glucosyltransferase), glucosidase II, Sep15, and ERp29. Extensive use of structurally defined substrates including high-mannose-type glycan derivatives and glycoproteins, which are obtained by chemical or chemoenzymatic synthesis, will be featured.

Analysis of glucose mediated glycoprotein folding events in the endoplasmic reticulum

255th National Meeting (2018)

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