Chemical Synthesis of Intentionally Misfolded Homogeneous Glycoprotein: A Unique Approach for the Study of Glycoprotein Quality Control

Biosynthesis of glycoproteins in the endoplasmic reticulum employs a quality control system, which discriminates and excludes misfolded malfunctional glycoproteins from a correctly folded one. As chemical tools to study the glycoprotein quality control system, we systematically synthesized misfolded...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2012-05, Vol.134 (17), p.7238-7241
Main Authors: Izumi, Masayuki, Makimura, Yutaka, Dedola, Simone, Seko, Akira, Kanamori, Akiko, Sakono, Masafumi, Ito, Yukishige, Kajihara, Yasuhiro
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Endoplasmic Reticulum - enzymology
Glucosyltransferases - metabolism
Glycopeptides - chemical synthesis
Glycopeptides - chemistry
Glycopeptides - metabolism
Glycoproteins - chemical synthesis
Glycoproteins - chemistry
Glycoproteins - metabolism
Humans
Mannose - chemistry
Models, Molecular
Molecular Sequence Data
Oligosaccharides - chemistry
Oxidation-Reduction
Protein Folding
Substrate Specificity
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Summary:Biosynthesis of glycoproteins in the endoplasmic reticulum employs a quality control system, which discriminates and excludes misfolded malfunctional glycoproteins from a correctly folded one. As chemical tools to study the glycoprotein quality control system, we systematically synthesized misfolded homogeneous glycoproteins bearing a high-mannose type oligosaccharide via oxidative misfolding of a chemically synthesized homogeneous glycopeptide. The endoplasmic reticulum folding sensor enzyme, UDP-glucose:glycoprotein glucosyltransferase (UGGT), recognizes a specific folding intermediate, which exhibits a molten globule-like hydrophobic nature.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja3013177