Evidence map›Paper›PMID 30739912›Full record

ArticleBritish journal of cancer2019

Tumour cell blebbing and extracellular vesicle shedding: key role of matrikines and ribosomal protein SA.

Bertrand Brassart, Jordan Da Silva, Mélissa Donet, Emeline Seurat, Frédéric Hague, Christine Terryn, Fréderic Velard, Jean Michel, Halima Ouadid-Ahidouch, Jean-Claude Monboisse and 4 more

Open access · hybridAbstract read
In one paragraph

Article in British journal of cancer, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

28 citing papers in PubMed, 37 citations in OpenAlex.

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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

14 authors at 5 institutions in 2 countries.

Bertrand BrassartUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France. bertrand.brassart@univ-reims.fr.
Jordan Da SilvaUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Mélissa DonetUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Emeline SeuratUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Frédéric HagueUniversité de Picardie Jules Verne, SFR CAP-Santé (FED 4231), Laboratoire de Physiologie Cellulaire et Moléculaire, EA 4667, Amiens, France.
Christine TerrynPlate-forme Imagerie Cellulaire et Tissulaire, Université de Reims Champagne-Ardenne, Reims, France.
Fréderic VelardBiomatériaux & inflammation en site osseux, EA 4691, SFR CAP-Santé (FED 4231), Université de Reims-Champagne-Ardenne, Reims, France.
Jean MichelLaboratoire de Recherche en Nanosciences, EA 4682, SFR CAP-Santé (FED 4231), Université de Reims-Champagne-Ardenne, Reims, France.
Halima Ouadid-AhidouchUniversité de Picardie Jules Verne, SFR CAP-Santé (FED 4231), Laboratoire de Physiologie Cellulaire et Moléculaire, EA 4667, Amiens, France.
Jean-Claude MonboisseUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Aleksander HinekPhysiology & Experimental Medicine Program, Hospital for Sick Children, Toronto, ON, Canada.
François-Xavier MaquartUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Laurent RamontUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Sylvie Brassart-PascoUniversité de Reims Champagne Ardenne, SFR CAP-Santé (FED 4231), Laboratoire de Biochimie Médicale et Biologie Moléculaire, Reims, France.
Centre National de la Recherche Scientifique · FRUniversité de Reims Champagne-Ardenne · FRCentre Hospitalier Universitaire Amiens-Picardie · FRLaboratoire de Recherche en NanosciencesUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCarcinogenesis occurs in elastin-rich tissues and leads to local inflammation and elastolytic proteinase release. This contributes to bioactive matrix fragment (Matrikine) accumulation like elastin degradation products (EDP) stimulating tumour cell invasive and metastatic properties. We previously demonstrate that EDPs exert protumoural activities through Hsp90 secretion to stabilised extracellular proteinases.

methodsEDP influence on cancer cell blebbing and extracellular vesicle shedding were examined with a videomicroscope coupled with confocal Yokogawa spinning disk, by transmission electron microscopy, scanning electron microscopy and confocal microscopy. The ribosomal protein SA (RPSA) elastin receptor was identified after affinity chromatography by western blotting and cell immunolocalisation. mRNA expression was studied using real-time PCR. SiRNA were used to confirm the essential role of RPSA.

resultsWe demonstrate that extracellular matrix degradation products like EDPs induce tumour amoeboid phenotype with cell membrane blebbing and shedding of extracellular vesicle containing Hsp90 and proteinases in the extracellular space. EDPs influence intracellular calcium influx and cytoskeleton reorganisation. Among matrikines, VGVAPG and AGVPGLGVG peptides reproduced EDP effects through RPSA binding.

conclusionsOur data suggests that matrikines induce cancer cell blebbing and extracellular vesicle release through RPSA binding, favouring dissemination, cell-to-cell communication and growth of cancer cells in metastatic sites.

Indexed as

AmidesCalciumCell CommunicationCell Line, TumorElastinExtracellular Matrix ProteinsExtracellular VesiclesHeterocyclic Compounds, 4 or More RingsHSP90 Heat-Shock ProteinsHumansNeoplasmsPeptide FragmentsPyridinesReceptors, Lamininrho-Associated KinasesRibosomal ProteinsAmidesblebbistatinCalciumElastinExtracellular Matrix ProteinsHeterocyclic Compounds, 4 or More RingsHSP90 Heat-Shock ProteinsPeptide FragmentsPyridinesReceptors, Lamininrho-Associated KinasesRibosomal ProteinsROCK1 protein, humanRPSA protein, humanY 27632

Identifiers

PMID30739912
PMCPMC6461924
OpenAlexW2913774914

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.