Evidence map›Paper›PMID 31650345›Full record

ArticleBreast cancer research and treatment2020

Functional inhibition of F11 receptor (F11R/junctional adhesion molecule-A/JAM-A) activity by a F11R-derived peptide in breast cancer and its microenvironment.

Radoslaw Bednarek, Anna Selmi, Dagmara Wojkowska, Kamil Karolczak, Marcin Popielarski, Marta Stasiak, Moro O Salifu, Anna Babinska, Maria Swiatkowska

Open access · hybridAbstract read
In one paragraph

Article in Breast cancer research and treatment, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

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  17. The Roles of Junctional Adhesion Molecules (JAMs) in Cell Migration.Frontiers in cell and developmental biology · 2022
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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

9 authors at 2 institutions in 2 countries.

Radoslaw BednarekDepartment of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland. radoslaw.bednarek@umed.lodz.pl.ORCID http://orcid.org/0000-0003-4505-9498
Anna SelmiDepartment of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland.
Dagmara WojkowskaDepartment of Haemostasis and Haemostatic Disorders, Medical University of Lodz, Lodz, Poland.
Kamil KarolczakDepartment of Haemostasis and Haemostatic Disorders, Medical University of Lodz, Lodz, Poland.
Marcin PopielarskiDepartment of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland.
Marta StasiakDepartment of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland.
Moro O SalifuDepartment of Medicine, State University of New York, Downstate Medical Center, Brooklyn, NY, USA.
Anna BabinskaDepartment of Medicine, State University of New York, Downstate Medical Center, Brooklyn, NY, USA.
Maria SwiatkowskaDepartment of Cytobiology and Proteomics, Medical University of Lodz, Lodz, Poland.
Medical University of Lodz · PLState University of New York · US

Funding

Narodowe Centrum Badań i Rozwoju STRATEGMED1/233226/11/NCBR/2015Uniwersytet Medyczny w Lodzi 503/6-171-01/502-64-091
6 · The paper itself

Abstract

purposeTo examine the involvement of the F11R/JAM-A protein in breast cancer metastasis, we utilized the F11R/JAM-A antagonistic peptide 4D (P4D) in experiments of transendothelial migration (TEM) of breast cancer cells.

methodsExperiments were conducted in the mouse 4T1 breast cancer model utilizing the human mammary epithelial cell and endothelial cell lines. The levels of soluble F11R/JAM-A (sJAM-A) in the murine plasmas were measured by ELISA. Levels of F11R/JAM-A mRNA and protein in cell lines were assessed by qRT-PCR and Western blot, respectively. Cell surface expression of F11R/JAM-A was demonstrated by flow cytometry. Functional tests included the TEM of breast cancer cells and adhesion of breast cancer cells to the endothelium. The endothelial permeability was studied by fluorescent tracer assay and by the Real-Time Cell Analysis (RTCA).

resultsThe tumor inducers Tβ4 and TGF-β1 reduced the levels of sJAM-A in murine plasma, and reduced the F11R/JAM-A protein levels in the human microvascular endothelial cell line HMEC-1. The adhesion and TEM measured between breast cancer cells and inflamed or Tβ4-treated endothelium were inhibited by P4D. The presence of P4D did not destabilize the pre-existing tight junctions in the endothelial monolayer. The barrier-protecting effect of P4D was stronger than that of forskolin, when a booster dose of P4D was applied to the inflamed endothelium.

conclusionsF11R/JAM-A protein can be considered as a novel target in the treatment of breast cancer metastasis. In vivo and clinical studies are needed to further investigate the effectiveness of F11R/JAM-A-derived peptide as a possible anti-metastatic drug.

Indexed as

AnimalsBreast NeoplasmsCell Adhesion MoleculesCell Line, TumorCytokinesEndothelial CellsFemaleGene ExpressionHumansMicePeptide FragmentsProtective AgentsReceptors, Cell SurfaceTransforming Growth Factor betaTumor MicroenvironmentCell Adhesion MoleculesCytokinesF11R protein, humanPeptide FragmentsProtective AgentsReceptors, Cell SurfaceTransforming Growth Factor betaBreast cancerEndotheliumF11RJAM-AMetastasisPlatelet F11 receptor

Identifiers

PMID31650345
PMCPMC6987052
OpenAlexW2981741694

What OpenQuestion holds

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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.