Evidence map›Paper›PMID 26598555›Full record

ArticleJournal of cell science2016

VE-cadherin facilitates BMP-induced endothelial cell permeability and signaling.

Andreas Benn, Clara Bredow, Isabel Casanova, Slobodan Vukičević, Petra Knaus

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 81 citations in OpenAlex.

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  20. The BMP Pathway in Blood Vessel and Lymphatic Vessel Biology.International journal of molecular sciences · 2021
    Review
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

5 authors at 3 institutions in 2 countries.

Andreas BennInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany DFG Graduate School 1093 Berlin School of Integrative Oncology, Berlin 13353, Germany DFG Graduate School 203 Berlin-Brandenburg School for Regenerative Therapies, Berlin 13353, Germany.
Clara BredowInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.
Isabel CasanovaInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.
Slobodan VukičevićCenter for Translational and Clinical Research, University of Zagreb, Zagreb 10000, Croatia.
Petra KnausInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany DFG Graduate School 1093 Berlin School of Integrative Oncology, Berlin 13353, Germany DFG Graduate School 203 Berlin-Brandenburg School for Regenerative Therapies, Berlin 13353, Germany knaus@chemie.fu-berlin.de.
Freie Universität Berlin · DEGerman Society for Thoracic and Cardiovascular Surgery · DEUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several vascular disorders, such as aberrant angiogenesis, atherosclerosis and pulmonary hypertension, have been linked to dysfunctional BMP signaling. Vascular hyperpermeability via distortion of endothelial cell adherens junctions is a common feature of these diseases, but the role of BMPs in this process has not been investigated. BMP signaling is initiated by binding of ligand to, and activation of, BMP type I (BMPRI) and type II (BMPRII) receptors. Internalization of VE-cadherin as well as c-Src kinase-dependent phosphorylation have been implicated in the loosening of cell-cell contacts, thereby modulating vascular permeability. Here we demonstrate that BMP6 induces hyperpermeabilization of human endothelial cells by inducing internalization and c-Src-dependent phosphorylation of VE-cadherin. Furthermore, we show BMP-dependent physical interaction of VE-cadherin with the BMP receptor ALK2 (BMPRI) and BMPRII, resulting in stabilization of the BMP receptor complex and, thereby, the support of BMP6-Smad signaling. Our results provide first insights into the molecular mechanism of BMP-induced vascular permeability, a hallmark of various vascular diseases, and provide the basis for further investigations of BMPs as regulators of vascular integrity, both under physiological and pathophysiological conditions.

Indexed as

Adherens JunctionsAntigens, CDBone Morphogenetic Protein 6Bone Morphogenetic Protein ReceptorsCadherin 5CadherinsCapillary PermeabilityCell Membrane PermeabilityEndocytosisHumansHuman Umbilical Vein Endothelial CellsModels, BiologicalPhosphorylationPhosphotyrosineProtein BindingProto-Oncogene Proteins pp60(c-src)Antigens, CDBone Morphogenetic Protein 6Bone Morphogenetic Protein ReceptorsCadherin 5CadherinsPhosphotyrosineProto-Oncogene Proteins pp60(c-src)ACVR1ALK2BMPBMPR2Cadherin 5Endothelial cellsPermeabilitySrcVE-cadherin

Identifiers

PMID26598555
PMCPMC4732303
OpenAlexW2177201093

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.