Glycoprotein maturation and the UPR.
- Hülsmeier AJ Institute of Physiology, University of Zürich, Winterthurerstrasse, Zürich, Switzerland.
- Welti M
- Hennet T
- 2011-02-19
Published in:
- Methods in enzymology. - 2011
Animals
Chromatography, High Pressure Liquid
Dolichol Phosphates
Dolichols
Glycoproteins
Glycosylation
Humans
Oligosaccharides
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Unfolded Protein Response
English
Glycosylation is a complex form of protein modification occurring in the secretory pathway. The addition of N- and O-glycans affects intracellular processes like the folding and trafficking of most glycoproteins. To better understand the impact of glycosylation in protein folding and maturation, parameters like glycosylation site occupancy and oligosaccharide structure must be measured quantitatively. In this chapter, we describe current methods enabling the determination of N-glycosylation by assessment of cellular dolichol phosphate levels, dolichol-linked oligosaccharides, and the occupancy of N-glycosylation sites. We also provide detailed methods for the analysis of O-glycosylation, whose role in intracellular protein maturation is often overlooked.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1016/B978-0-12-385928-0.00010-9
- PMID 21329800
- Persistent URL
- https://sonar.ch/global/documents/236036
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