Evidence map›Paper›PMID 28358117›Full record

ArticleScientific reports2017

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

Shahidul Alam, Merrina Anugraham, Yen-Lin Huang, Reto S Kohler, Timm Hettich, Katharina Winkelbach, Yasmin Grether, Mónica Núñez López, Nailia Khasbiullina, Nicolai V Bovin and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 27 citations in OpenAlex.

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  9. Site-specificiScience · 2021
    Article
  10. The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Shahidul AlamOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Merrina AnugrahamOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Yen-Lin HuangOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Reto S KohlerOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Timm HettichSchool of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Muttenz, 4132, Switzerland.
Katharina WinkelbachOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Yasmin GretherOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Mónica Núñez LópezOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
Nailia KhasbiullinaShemyakin- Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russian Federation.
Nicolai V BovinShemyakin- Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russian Federation.
Götz SchlotterbeckSchool of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Muttenz, 4132, Switzerland.
Francis JacobOvarian Cancer Research, Department of Biomedicine, University Hospital Basel, University of Basel, Basel, 4031, Switzerland.
University of Basel · CHUniversity Hospital of Basel · CHFHNW University of Applied Sciences and Arts · CHInstitute of Bioorganic Chemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Cell Line, TumorCRISPR-Cas SystemsFemaleGene Knockout TechniquesGlycomicsGlycoproteinsGlycosphingolipidsHeLa CellsHumansN-AcetylgalactosaminyltransferasesOvarian NeoplasmsB4galnt1 protein, humanGlycoproteinsGlycosphingolipidsN-Acetylgalactosaminyltransferases

Identifiers

PMID28358117
PMCPMC5371825
OpenAlexW2602271431

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.