Evidence map›Paper›PMID 26908442›Full record

ArticleOncotarget2016

Carcinoma-associated fucosylated antigens are markers of the epithelial state and can contribute to cell adhesion through CLEC17A (Prolectin).

Adrien Breiman, María Dolores López Robles, Sophie de Carné Trécesson, Klara Echasserieau, Karine Bernardeau, Kurt Drickamer, Anne Imberty, Sophie Barillé-Nion, Frédéric Altare, Jacques Le Pendu

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Regulation of the Lewis Blood Group Antigen Expression: A Literature Review Supplemented with Computational Analysis.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
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

10 authors at 5 institutions in 2 countries.

Adrien BreimanInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
María Dolores López RoblesInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Sophie de Carné TrécessonInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Klara EchasserieauInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Karine BernardeauInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Kurt DrickamerDepartment of Life Sciences, Imperial College London, London SW7, UK.
Anne ImbertyCERMAV-UPR 5301, CNRS, Université Grenoble Alpes, 38041 Grenoble, France.
Sophie Barillé-NionInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Frédéric AltareInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Jacques Le PenduInserm U892, CNRS UMR6299, University of Nantes, 44007 Nantes, France.
Centre National de la Recherche Scientifique · FRNantes Université · FRInserm · FRImperial College London · GBLaboratoire de Thermique et Energie de Nantes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Terminal fucosylated motifs of glycoproteins and glycolipid chains are often altered in cancer cells. We investigated the link between fucosylation changes and critical steps in cancer progression: epithelial-to-mesenchymal transition (EMT) and lymph node metastasis.Using mammary cell lines, we demonstrate that during EMT, expression of some fucosylated antigens (e.g.: Lewis Y) is decreased as a result of repression of the fucosyltransferase genes FUT1 and FUT3. Moreover, we identify the fucose-binding bacterial lectin BC2L-C-Nt as a specific probe for the epithelial state.Prolectin (CLEC17A), a human lectin found on lymph node B cells, shares ligand specificities with BC2L-C-Nt. It binds preferentially to epithelial rather than to mesenchymal cells, and microfluidic experiments showed that prolectin behaves as a cell adhesion molecule for epithelial cells. Comparison of paired primary tumors/lymph node metastases revealed an increase of prolectin staining in metastasis and high FUT1 and FUT3 mRNA expression was associated with poor prognosis. Our data suggest that tumor cells invading the lymph nodes and expressing fucosylated motifs associated with the epithelial state could use prolectin as a colonization factor.

Indexed as

Cell AdhesionApoptosisBiomarkers, TumorBreast NeoplasmsCell ProliferationEpithelial-Mesenchymal TransitionFemaleFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferaseHumansLectins, C-TypeLymphatic MetastasisTumor Cells, Cultured3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferaseBiomarkers, TumorCLEC17A protein, humanFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferaseLectins, C-Typeepithelial to mesenchymal transitionfucoselectinslymph node metastasis

Identifiers

PMID26908442
PMCPMC4924698
OpenAlexW2288614375

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.