Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle

Deglucosylation and reglucosylation of glycoproteins by glucosidase II and uridine diphosphate‐glucose: glycoprotein glucosyltransferase 1 (UGGT1), respectively, are important steps in glycoprotein quality control. Misfolded glycoprotein accumulation is associated with endoplasmic reticulum stress a...

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Bibliographic Details
Published in:FEBS letters 2020-06, Vol.594 (11), p.1759-1769
Main Authors: Kuribara, Taiki, Imagawa, Ayami, Hirano, Makoto, Ito, Yukishige, Totani, Kiichiro
Format: Article
Language:English
Subjects:
alpha-Glucosidases - genetics
alpha-Glucosidases - metabolism
Animals
diabetes
Diabetes Mellitus, Type 2
Disease Models, Animal
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
glycoenzyme
glycoprotein quality control
Glycoproteins - chemistry
Glycoproteins - metabolism
Glycosylation
Liver - enzymology
Male
Metabolic Syndrome - enzymology
Metabolic Syndrome - metabolism
Obesity
Protein Folding
Rats
Rats, Zucker
trans‐omics
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Summary:Deglucosylation and reglucosylation of glycoproteins by glucosidase II and uridine diphosphate‐glucose: glycoprotein glucosyltransferase 1 (UGGT1), respectively, are important steps in glycoprotein quality control. Misfolded glycoprotein accumulation is associated with endoplasmic reticulum stress and can lead to protein misfolding diseases such as metabolic syndrome. Here, we analyzed the expression and activities of glucosidase II and UGGT1 in rat models of obesity and obese type 2 diabetes, and phenotypes associated with moderate and severe metabolic syndrome, respectively. In obesity, the mRNA and protein levels of glucosidase II and UGGT1 are decreased and their activities are reduced. In obese type 2 diabetes, the mRNA and protein levels of these enzymes are increased, and glucosidase II activity is slightly recovered, although UGGT1 activity is reduced. Our findings suggest that metabolic syndrome affects deglucosylation/reglucosylation enzymes according to disease severity.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13780