Evidence map›Paper›PMID 26161413›Full record

ArticleBioMed research international2015

Glycosyltransferases as Markers for Early Tumorigenesis.

Ulrich Andergassen, Friederike Liesche, Alexandra C Kölbl, Matthias Ilmer, Stefan Hutter, Klaus Friese, Udo Jeschke

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

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  15. Oncogenic Epstein-Barr virus recruits Nm23-H1 to regulate chromatin modifiers.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  16. The Journal of biological chemistry · 2018
    Article
  17. Review
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  19. Article
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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

7 authors at 2 institutions in 2 countries.

Ulrich AndergassenKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Friederike LiescheKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Alexandra C KölblKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Matthias IlmerDepartment of Translational Molecular Pathology, University of Texas MD Anderson Cancer Center, 7435 Fannin Street, Houston, TX 77054, USA.
Stefan HutterKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Klaus FrieseKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Udo JeschkeKlinik und Poliklinik für Frauenheilkunde und Geburtshilfe, Ludwig-Maximilians-Universitaet Muenchen, Campus Innenstadt, Maistraße 11, 80337 Munich, Germany.
Klinik für Frauenheilkunde · DEThe University of Texas MD Anderson Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlycosylation is the most frequent posttranslational modification of proteins and lipids influencing inter- and intracellular communication and cell adhesion. Altered glycosylation patterns are characteristically observed in tumour cells. Normal and altered carbohydrate chains are transferred to their acceptor structures via glycosyltransferases. Here, we present the correlation between the presence of three different glycosyltransferases and tumour characteristics.

methods235 breast cancer tissue samples were stained immunohistochemically for the glycosyltransferases N-acetylgalactosaminyltransferase 6 (GALNT6), β-1,6-N-acetylglucosaminyltransferase 2 (GCNT2), and ST6 (α-N-acetyl-neuraminyl-2,3-β-galactosyl-1,3)-N-acetylgalactosamine α-2,6-sialyltransferase 1 (ST6GALNac1). Staining was evaluated by light microscopy and was correlated to different tumour characteristics by statistical analysis.

resultsWe found a statistically significant correlation for the presence of glycosyltransferases and tumour size and grading. Specifically smaller tumours with low grading revealed the highest incidences of glycosyltransferases. Additionally, Her4-expression but not pHer4-expression is correlated with the presence of glycosyltransferases. All other investigated parameters could not uncover any statistically significant reciprocity.

conclusionHere we show, that glycosyltransferases can identify small tumours with well-differentiated cells; hence, glycosylation patterns could be used as a marker for early tumourigenesis. This assumption is supported by the fact that Her4 is also correlated to glycosylation, whereas the activated form of Her4 does not show such a connection with glycosylation.

Indexed as

Biomarkers, TumorBreast NeoplasmsCarcinogenesisFemaleGlycosyltransferasesHumansImmunohistochemistryKaplan-Meier EstimateBiomarkers, TumorGlycosyltransferases

Identifiers

PMID26161413
PMCPMC4486746
OpenAlexW1573555338

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.