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Altered (neo-) lacto series glycolipid biosynthesis impairs α2-6 sialylation on N-glycoproteins in ovarian cancer cells.

  • Alam S Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Anugraham M Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Huang YL Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Kohler RS Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Hettich T School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Muttenz, 4132, Switzerland.
  • Winkelbach K Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Grether Y Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • López MN Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
  • Khasbiullina N Shemyakin- Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russian Federation.
  • Bovin NV Shemyakin- Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russian Federation.
  • Schlotterbeck G School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Muttenz, 4132, Switzerland.
  • Jacob F Ovarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
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  • 2017-03-31
Published in:
  • Scientific reports. - 2017
CRISPR-Cas Systems
Cell Line, Tumor
Female
Gene Knockout Techniques
Glycomics
Glycoproteins
Glycosphingolipids
HeLa Cells
Humans
N-Acetylgalactosaminyltransferases
Ovarian Neoplasms
English The (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.
Language
  • English
Open access status
gold
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https://sonar.ch/global/documents/160059
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