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Analysis of Cell Surface N-glycosylation of the Human Embryonic Kidney 293T Cell Line.
- Source :
-
Journal of Carbohydrate Chemistry . May-Aug2011, Vol. 30 Issue 4-6, p218-232. 15p. - Publication Year :
- 2011
-
Abstract
- Protein glycosylation is a prominent posttranslational modification and is involved in many biological functions. Human cell lines used for the expression of recombinant glycoproteins present variations in their cell surface N-glycosylation due to their cell type–specific origin. We therefore investigated the presence of specific glycosyltransferases by RT-PCR and the cell surface N-glycan structures of HEK293T cells by MALDI-TOF-MS and MALDI-TOF/TOF-MS analyses. Expression of N-acetylglucosaminyltransferase-III and fucosyltransferase-VIII were coincident with the presence of bisecting N-acetylglucosamine and high amounts of core-fucosylated N-glycans. Furthermore, a high overall amount of sialylated N-glycans and the expression of α2,3- and α2,8-specific, but not α2,6-specific, sialyltransferases were found. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 07328303
- Volume :
- 30
- Issue :
- 4-6
- Database :
- Academic Search Index
- Journal :
- Journal of Carbohydrate Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 67129568
- Full Text :
- https://doi.org/10.1080/07328303.2011.600489