Influence of aglycone structures on N-glycan processing reactions in the endoplasmic reticulum
| Autor: | Kiichiro Totani, Kenta Yamaya, Yukishige Ito, Makoto Hirano |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Boron Compounds Male Glycosylation Protein Conformation Mannose Cell Fractionation Endoplasmic Reticulum Biochemistry Analytical Chemistry Acetylglucosamine 03 medical and health sciences chemistry.chemical_compound Mice N-glycan processing Mannosidases Animals Secretion Fluorescent Dyes Glycoproteins chemistry.chemical_classification 030102 biochemistry & molecular biology Endoplasmic reticulum Organic Chemistry General Medicine Oligosaccharide Mice Inbred C57BL 030104 developmental biology Aglycone Glucose chemistry Carbohydrate Sequence Liver Glucosyltransferases Hepatocytes Glycoprotein Calreticulin Linker Hydrophobic and Hydrophilic Interactions Glucosidases |
| Zdroj: | Carbohydrate research. 439 |
| ISSN: | 1873-426X |
| Popis: | Glycoprotein N-linked oligosaccharides in the endoplasmic reticulum function as tags to regulate glycoprotein folding, sorting, secretion and degradation. Since the N-glycan structure of a glycoprotein should reflect the folding state, N-glycan processing may be affected by the aglycone state. In this study, we examined the influence of aglycone structures on N-glycan processing using synthetic substrates. We prepared (Glc1)Man9GlcNAc2 linked to hydrophobic BODIPY-dye with a systematic series of different linker lengths. With these compounds, glucose transfer, glucose trimming and mannose trimming reactions of an endoplasmic reticulum fraction were examined. The results showed that substrates with shorter linkers between the N-glycan and hydrophobic patch had higher activities for both the glucose transfer and the mannose trimming reactions. In contrast, the glucose trimming reaction showed lower activity when substrates had shorter linkers. Thus, the reactivity for N-linked oligosaccharide processing of glycoproteins in the endoplasmic reticulum might be tunable by the aglycone structure, e.g., protein portion of glycoproteins. |
| Databáze: | OpenAIRE |
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