Evidence map›Paper›PMID 28593951›Full record

ArticleNature communications2017

Preventing tissue fibrosis by local biomaterials interfacing of specific cryptic extracellular matrix information.

Christine-Maria Horejs, Jean-Philippe St-Pierre, Juha R M Ojala, Joseph A M Steele, Patricia Barros da Silva, Angela Rynne-Vidal, Stephanie A Maynard, Catherine S Hansel, Clara Rodríguez-Fernández, Manuel M Mazo and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-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

17 citing papers in PubMed, 51 citations in OpenAlex.

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  7. Intersection of stem cell biology and engineering towards next generationFrontiers in bioengineering and biotechnology · 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

16 authors at 3 institutions in 4 countries.

Christine-Maria HorejsDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Jean-Philippe St-PierreDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Juha R M OjalaDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, Stockholm 17177, Sweden.
Joseph A M SteeleDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Patricia Barros da SilvaDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, Stockholm 17177, Sweden.
Angela Rynne-VidalCentro de Biología Molecular Severo Ochoa, CSIC, Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain.
Stephanie A MaynardDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Catherine S HanselDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Clara Rodríguez-FernándezDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Manuel M MazoDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Amanda Y F YouDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Alex J WangDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Thomas von ErlachDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.ORCID 0000-0002-8979-6652
Karl TryggvasonDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, Stockholm 17177, Sweden.
Manuel López-CabreraCentro de Biología Molecular Severo Ochoa, CSIC, Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain.
Molly M StevensDepartment of Materials, Imperial College London, Exhibition Road, London SW7 2AZ, UK.ORCID 0000-0002-7335-266X
Imperial College London · GBKarolinska Institutet · SECentro de Biología Molecular Severo Ochoa · ES

Funding

European Research Council 616417Medical Research Council MR/K026666/1Medical Research Council MR/K026682/1Medical Research Council MR/L012677/1Wellcome Trust 098411
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) contribute to the breakdown of tissue structures such as the basement membrane, promoting tissue fibrosis. Here we developed an electrospun membrane biofunctionalized with a fragment of the laminin β1-chain to modulate the expression of MMP2 in this context. We demonstrate that interfacing of the β1-fragment with the mesothelium of the peritoneal membrane via a biomaterial abrogates the release of active MMP2 in response to transforming growth factor β1 and rescues tissue integrity ex vivo and in vivo in a mouse model of peritoneal fibrosis. Importantly, our data demonstrate that the membrane inhibits MMP2 expression. Changes in the expression of epithelial-to-mesenchymal transition (EMT)-related molecules further point towards a contribution of the modulation of EMT. Biomaterial-based presentation of regulatory basement membrane signals directly addresses limitations of current therapeutic approaches by enabling a localized and specific method to counteract MMP2 release applicable to a broad range of therapeutic targets.

Indexed as

AnimalsBiocompatible MaterialsDisease Models, AnimalEpithelial CellsEpithelial-Mesenchymal TransitionEpitheliumExtracellular MatrixGene Expression ProfilingHEK293 CellsHumansIntegrin alpha3beta1LamininMammary Glands, HumanMatrix Metalloproteinase 2Membranes, ArtificialMiceBiocompatible MaterialsIntegrin alpha3beta1LamininMatrix Metalloproteinase 2Membranes, Artificial

Identifiers

PMID28593951
PMCPMC5472175
OpenAlexW2622616651

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.