Evidence map›Paper›PMID 23409978›Full record

ArticleBioscience reports2013

EpCAM proteolysis: new fragments with distinct functions?

Ulrike Schnell, Jeroen Kuipers, Ben N G Giepmans

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 82 citations in OpenAlex.

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  6. EpCAM tumor specificity and proteoform patterns in urothelial cancer.Journal of cancer research and clinical oncology · 2023
    Article
  7. Article
  8. Breaking free: endocytosis and endosomal escape of extracellular vesicles.Extracellular vesicles and circulating nucleic acids · 2023
    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

3 authors at 2 institutions in 1 country.

Ulrike SchnellDepartment of Cell Biology, University Medical Center Groningen, University of Groningen, P.O. Box 196, 9700 AD, Groningen, The Netherlands.
Jeroen KuipersDepartment of Cell Biology, University Medical Center Groningen, University of Groningen, P.O. Box 196, 9700 AD, Groningen, The Netherlands.
Ben N G GiepmansDepartment of Cell Biology, University Medical Center Groningen, University of Groningen, P.O. Box 196, 9700 AD, Groningen, The Netherlands.
University Medical Center Groningen · NLUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EpCAM [epithelial cell adhesion molecule; CD326 (cluster of differentiation 326)] is highly expressed on epithelium-derived tumours and can play a role in cell proliferation. Recently, RIP (regulated intramembrane proteolysis) has been implicated as the trigger for EpCAM-mediated proliferative signalling. However, RIP does not explain all EpCAM-derived protein fragments. To shed light on how proteolytic cleavage is involved in EpCAM signalling, we characterized the protein biochemically using antibodies binding to three different EpCAM domains. Using a newly generated anti-EpCAM antibody, we find that EpCAM can be cleaved at multiple positions within its ectodomain in addition to described peptides, revealing that EpCAM is processed via distinct proteolytic pathways. Here, we report on four new peptides, but also discuss the previously described cleavage products to provide a comprehensive picture of EpCAM cleavage at multiple positions. The complex regulation of EpCAM might not only result in the absence of full-length EpCAM, but the newly formed EpCAM-derived proteins may have their own signalling properties.

Indexed as

ProteolysisSignal TransductionAntibodies, Anti-IdiotypicAntigens, NeoplasmCell Adhesion MoleculesCell CommunicationCell ProliferationEpithelial Cell Adhesion MoleculeHCT116 CellsHEK293 CellsHumansNeoplasmsProtein Structure, TertiaryAntibodies, Anti-IdiotypicAntigens, NeoplasmCell Adhesion MoleculesEPCAM protein, humanEpithelial Cell Adhesion Molecule

Identifiers

PMID23409978
PMCPMC3601740
OpenAlexW2132846945

What OpenQuestion holds

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LicenceCC BY-NC
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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.