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dc.contributor.authorAlam, Shahidul
dc.contributor.authorAnugraham, Merrina
dc.contributor.authorHuang, Yen-Lin
dc.contributor.authorKohler, Reto
dc.contributor.authorHettich, Timm
dc.contributor.authorWinkelbach, Katharina
dc.contributor.authorGrether, Yasmin
dc.contributor.authorNunez Lopez, Monica
dc.contributor.authorKhasbiullina, Nailia
dc.contributor.authorBovin, Nicolai V.
dc.contributor.authorSchlotterbeck, Götz
dc.contributor.authorJacob, Francis
dc.date.accessioned2018-01-23T08:33:35Z
dc.date.available2018-01-23T08:33:35Z
dc.date.issued2017-03-30
dc.identifier.doi10.1038/srep45367
dc.identifier.urihttp://hdl.handle.net/11654/25891
dc.description.abstractThe (neo-) lacto series glycosphingolipids (nsGSLs) comprise of glycan epitopes that are present as blood group antigens, act as primary receptors for human pathogens and are also increasingly associated with malignant diseases. Beta-1, 3-N-acetyl-glucosaminyl-transferase 5 (B3GNT5) is suggested as the key glycosyltransferase for the biosynthesis of nsGSLs. In this study, we investigated the impact of CRISPR-Cas9 -mediated gene disruption of B3GNT5 (∆B3GNT5) on the expression of glycosphingolipids and N-glycoproteins by utilizing immunostaining and glycomics-based PGC-UHPLC-ESI-QTOF-MS/MS profiling. ∆B3GNT5 cells lost nsGSL expression coinciding with reduction of α2-6 sialylation on N-glycoproteins. In contrast, disruption of B4GALNT1, a glycosyltransferase for ganglio series GSLs did not affect α2-6 sialylation on N-glycoproteins. We further profiled all known α2-6 sialyltransferase-encoding genes and showed that the loss of α2-6 sialylation is due to silencing of ST6GAL1 expression in ∆B3GNT5 cells. These results demonstrate that nsGSLs are part of a complex network affecting N-glycosylation in ovarian cancer cells.
dc.description.urihttps://www.nature.com/articles/srep45367
dc.language.isoen_US
dc.relation.ispartofScientific Reports
dc.accessRightsAnonymous
dc.subjectlacto series
dc.subjectglycolipid
dc.subjectbiosynthesis
dc.titleAltered (neo-) lacto series glycolipid biosynthesis impairs α2-6 sialylation on N-glycoproteins in ovarian cancer cells
dc.type01 - Zeitschriftenartikel, Journalartikel oder Magazin
dc.volume7
dc.audienceScience
fhnw.publicationStatePublished
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publication
fhnw.InventedHereYes
fhnw.PublishedSwitzerlandNo
fhnw.paginationArticle number: 45367
fhnw.IsStudentsWorkno
fhnw.publicationOnlineJa


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