Evidence map›Paper›PMID 31455004›Full record

SynthesisInternational journal of molecular sciences2019

L1 Cell Adhesion Molecule in Cancer, a Systematic Review on Domain-Specific Functions.

Miriam van der Maten, Casper Reijnen, Johanna M A Pijnenborg, Mirjam M Zegers

Open access · goldAbstract readSystematic Review
In one paragraph

Synthesis in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

37 citing papers in PubMed, 61 citations in OpenAlex.

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  15. Blood-derived APLP1Science advances · 2025
    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

4 authors at 1 institution in 1 country.

Miriam van der MatenDepartment of Obstetrics and Gynaecology, Radboud university medical center, 6525 GA Nijmegen, The Netherlands.
Casper ReijnenDepartment of Obstetrics and Gynaecology, Radboud university medical center, 6525 GA Nijmegen, The Netherlands.
Johanna M A PijnenborgDepartment of Obstetrics and Gynaecology, Radboud university medical center, 6525 GA Nijmegen, The Netherlands. hanny.ma.pijnenborg@radboudumc.nl.
Mirjam M ZegersDepartment of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboud university medical center, 6525 GA Nijmegen, The Netherlands. Mirjam.zegers@radboudumc.nl.
Radboud University Nijmegen · NL

Funding

KWF Kankerbestrijding 10616/2016-2
6 · The paper itself

Abstract

L1 cell adhesion molecule (L1CAM) is a glycoprotein involved in cancer development and is associated with metastases and poor prognosis. Cellular processing of L1CAM results in expression of either full-length or cleaved forms of the protein. The different forms of L1CAM may localize at the plasma membrane as a transmembrane protein, or in the intra- or extracellular environment as cleaved or exosomal forms. Here, we systematically analyze available literature that directly relates to L1CAM domains and associated signaling pathways in cancer. Specifically, we chart its domain-specific functions in relation to cancer progression, and outline pre-clinical assays used to assess L1CAM. It is found that full-length L1CAM has both intracellular and extracellular targets, including interactions with integrins, and linkage with ezrin. Cellular processing leading to proteolytic cleavage and/or exosome formation results in extracellular soluble forms of L1CAM that may act through similar mechanisms as compared to full-length L1CAM, such as integrin-dependent signals, but also through distinct mechanisms. We provide an algorithm to guide a step-wise analysis on L1CAM in clinical samples, to promote interpretation of domain-specific expression. This systematic review infers that L1CAM has an important role in cancer progression that can be attributed to domain-specific forms. Most studies focus on the full-length plasma membrane L1CAM, yet knowledge on the domain-specific forms is a prerequisite for selective targeting treatment.

Indexed as

Protein Interaction Domains and MotifsAnimalsBiomarkersCarrier ProteinsCell AdhesionCell Transformation, NeoplasticHumansNeoplasmsNeural Cell Adhesion Molecule L1Protein BindingSignal TransductionBiomarkersCarrier ProteinsNeural Cell Adhesion Molecule L1biomarkercell adhesionL1CAMoncogenic signalingsystematic reviewtumor biology

Identifiers

PMID31455004
PMCPMC6747497
OpenAlexW2970591810

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.