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Processing and Re-Processing of Asparagine-linked Oligosaccharides
Hughes, R. C.
Hughes, R. C.
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Issue Date
1991
Submitted date
2024-02-20
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Abstract
The assembly of asparagine-linked oligosaccharides in glycoprotein biosynthesis is cell specific, polypeptide specific and glycosylation site specific. Recombinant glycoproteins produced in nonhomologous cells are likely to be glycosylated abnormally and the consequences on proteinstability, conformation and biological activity need to be considered. Although the major pathways of assembly of asparagine-linked oligosaccharides are identified, their regulation during biosynthesis is not understood. The early events in oligosaccharide processing catalyzed by glucosidases I and II and specific mannosidases are particularly complex. Experiments using various inhibitors of processing glucosidases and mannosidases as well as structural analysis of processing intermediates, show that different processing pathways. are selected for assembly of glycans substituted at specific sites in glycoproteins. New mannosidases are being described that participate in these diverse pathways. A novel mannosidase of rat liver is concentrated in endosomes as well as the cis Golgi compartment and may play an additional role in remodelling of glycoproteins that occurs during internalisation and recycling of cell surface glycoproteins.
Citation
Protein glycosylation, 3 - 11
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Type
Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 15
ISSN
0930-4320
EISSN
ISBN
3527283676
1560811846
1560811846
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Attribution-NonCommercial-ShareAlike 4.0 International