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Structural approaches to the study of oligosaccharides in glycoprotein quality control.

Current opinion in structural biology (2005-09-13)
Yukishige Ito, Shinya Hagihara, Ichiro Matsuo, Kiichiro Totani
ABSTRACT

High-mannose-type oligosaccharides have been shown to play important roles in protein quality control. Several intracellular proteins, such as lectins, chaperones and glycan-processing enzymes, are involved in this process. These include calnexin/calreticulin, UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (such as VIP36 and ERGIC-53), mannosidase-like proteins (e.g. EDEM and Htm1p) and ubiquitin ligase (Fbs). They are thought to recognize high-mannose-type glycans with subtly different structures, although the precise specificities are yet to be clarified. In order to gain a clear understanding of these protein-carbohydrate interactions, comprehensive synthesis of high-mannose-type glycans was conducted. In addition, two approaches to the synthesis of artificial glycoproteins with homogeneous oligosaccharides were investigated. Furthermore, a novel substrate of UGGT was discovered.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
D-(+)-Mannose, powder, BioReagent, suitable for cell culture
Sigma-Aldrich
D-(+)-Mannose, BioUltra, ≥99.5% (sum of enantiomers, HPLC)
Millipore
D-(+)-Mannose, suitable for microbiology, ≥99%
Millipore
D-(+)-Mannose, ≥99.0% (sum of enantiomers, HPLC), suitable for microbiology
Sigma-Aldrich
D-(+)-Mannose, wood, ≥99%