Dumermuth, E. and Beuret, N. and Spiess, M. and Crottet, P.. (2002) Ubiquitous 9-O-acetylation of sialoglycoproteins restricted to the Golgi complex. Journal of biological chemistry, Vol. 277 , no. 21. pp. 18687-18693.
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Official URL: http://edoc.unibas.ch/dok/A5258052
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Abstract
9-O-Acetylation of sialic acid is known as a cell type-specific modification of secretory and plasma membrane glycoconjugates of higher vertebrates with important functions in modulating cell-cell recognition. Using a recombinant probe derived from influenza C virus hemagglutinin, we discovered 9-O-acetylated protein in the Golgi complex of various cell lines, most of which did not display 9-O-acetylated sialic acid on the cell surface. All cell lines expressed a sulfated glycoprotein of 50 kDa (sgp50) carrying 9-O-acetylated sialic acids, which was used as a model substrate. Like gp40, the major receptor for influenza C virus of Madin-Darby canine kidney I cells, sgp50 is 9-O-acetylated on O-linked glycans. However, gp40 was not 9-O-acetylated when expressed in Madin-Darby canine kidney II or COS-7 cells. The results demonstrate the existence of two 9-O-acetylation machineries for O-glycosylated proteins with distinct substrate specificities. The widespread occurrence of 9-O-acetylated protein in the Golgi furthermore suggests an additional intracellular role for this modification.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Biochemistry (Spiess) |
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UniBasel Contributors: | Spiess, Martin |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | American Society of Biological Chemists |
ISSN: | 0021-9258 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Last Modified: | 22 Mar 2012 14:20 |
Deposited On: | 22 Mar 2012 13:19 |
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