Evidence map›Paper›PMID 17646933›Full record

ArticleMolecular and cellular biochemistry2007

Cadherins are regulated by Ep-CAM via phosphaditylinositol-3 kinase.

Manon J Winter, Vincenzo Cirulli, Inge H Briaire-de Bruijn, Sergey V Litvinov

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. MMTV/LTR Promoter-Driven Transgenic Expression of EpCAM Leads to the Development of Large Pancreatic Islets.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015
    Article
  9. Cell adhesion and urothelial bladder cancer: the role of cadherin switching and related phenomena.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 3 institutions in 4 countries.

Manon J WinterDepartment of Pathology, Leiden University Medical Center, P.O. Box 9600, 2300 RC, Leiden, The Netherlands. winterm1@wyeth.com
Vincenzo Cirulli
Inge H Briaire-de Bruijn
Sergey V Litvinov
Leiden University Medical Center · NLPowerCell (Sweden) · SEUniversidad Católica Santo Domingo · DO

Funding

PANCREATIC BETA CELL DEVELOPMENT--HUMAN DCC+ STEM CELLSR01DK055183 · NIDDK · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI CIRULLI, VINCENZINO · 1998 to 2002
$841k
Role of Connexins in Beta-Cell Development and FunctionR01DK063443 · NIDDK · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI CIRULLI, VINCENZINO · 2002 to 2003
$630k
NIDDK NIH HHS DK55183NIDDK NIH HHS DK63443
6 · The paper itself

Abstract

The cross-signaling between (cell) adhesion molecules is nowadays a well-accepted phenomenon and includes orchestrated cellular changes and changes in the microenvironment. For example, Ep-CAM is an epithelial adhesion molecule that prevails in active proliferating tissue and is suppressed in a more differentiated state of the cell. E-cadherin adhesion complexes are typical for the advanced and terminal differentiated cell status. During normal proliferation, E-cadherin is not suppressed. We have demonstrated the effect of overexpression of Ep-CAM on E-cadherin, which probably affects the connection of cadherins and F-actin. Phosphatidylinositol 3-kinase (Pi3K) participates in various regulating mechanisms, for example in signaling to nuclei, vesicle transport, and cytoskeletal rearrangements. The effect of Ep-CAM on E-cadherin mediated junctions as well as the involvement of Pi3K in regulating adherens junctions, led us to investigate the potential interaction between Pi3K and Ep-CAM. Introduction of Ep-CAM in the epithelial cells caused abrogation of N-cadherin mediated cell-cell adhesion, which could be inhibited by Pi3K inhibitor LY294002. Moreover, the Pi3K subunit p85 was precipitated with Ep-CAM from cell lysates, and this complex showed kinase activity. The Pi3K activity shuttled from N-cadherin to Ep-CAM. From our results, we conclude that Ep-CAM cross signaling with N-cadherin involves Pi3K, resulting in the abrogation of the cadherin adhesion complexes in epithelial cells.

Indexed as

Antigens, NeoplasmCadherinsCell AdhesionCell Adhesion MoleculesCell LineChromonesEpithelial Cell Adhesion MoleculeHumansMorpholinesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein BindingSignal Transduction2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneAntigens, NeoplasmCadherinsCell Adhesion MoleculesChromonesEPCAM protein, humanEpithelial Cell Adhesion MoleculeMorpholinesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase Inhibitors

Identifiers

PMID17646933
OpenAlexW2012052254

What OpenQuestion holds

Textmetadata
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.