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.
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