Evidence map›Paper›PMID 24874477›Full record

ArticleBritish journal of cancer2014

Elastin peptides regulate HT-1080 fibrosarcoma cell migration and invasion through an Hsp90-dependent mechanism.

M Donet, S Brassart-Pasco, S Salesse, F-X Maquart, B Brassart

Open access · hybridAbstract read
In one paragraph

Article in British journal of cancer, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

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  11. TRPM7/RPSA Complex Regulates Pancreatic Cancer Cell Migration.Frontiers in cell and developmental biology · 2020
    Article
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  20. MMP generated matrikines.Matrix biology : journal of the International Society for Matrix Biology
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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

5 authors at 1 institution in 1 country.

M Donet1] Laboratoire de Biochimie Médicale et Biologie Moléculaire, UMR CNRS/URCA 7369 MEDyC, UFR Médecine, Université de Reims Champagne Ardenne, 51 Rue Cognacq Jay, 51095 Reims, France [2] CNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire - MEDyC, 51 Rue Cognacq Jay, 51095 Reims, France.
S Brassart-Pasco1] Laboratoire de Biochimie Médicale et Biologie Moléculaire, UMR CNRS/URCA 7369 MEDyC, UFR Médecine, Université de Reims Champagne Ardenne, 51 Rue Cognacq Jay, 51095 Reims, France [2] CNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire - MEDyC, 51 Rue Cognacq Jay, 51095 Reims, France.
S Salesse1] Laboratoire de Biochimie Médicale et Biologie Moléculaire, UMR CNRS/URCA 7369 MEDyC, UFR Médecine, Université de Reims Champagne Ardenne, 51 Rue Cognacq Jay, 51095 Reims, France [2] CNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire - MEDyC, 51 Rue Cognacq Jay, 51095 Reims, France.
F-X Maquart1] Laboratoire de Biochimie Médicale et Biologie Moléculaire, UMR CNRS/URCA 7369 MEDyC, UFR Médecine, Université de Reims Champagne Ardenne, 51 Rue Cognacq Jay, 51095 Reims, France [2] CNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire - MEDyC, 51 Rue Cognacq Jay, 51095 Reims, France [3] CHU de Reims, Laboratoire Central de Biochimie, 51092 Reims, France.
B Brassart1] Laboratoire de Biochimie Médicale et Biologie Moléculaire, UMR CNRS/URCA 7369 MEDyC, UFR Médecine, Université de Reims Champagne Ardenne, 51 Rue Cognacq Jay, 51095 Reims, France [2] CNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire - MEDyC, 51 Rue Cognacq Jay, 51095 Reims, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe elastin-derived peptides (EDPs) exert protumoural activities by potentiating the secretion of matrix metalloproteinases (MMP) and the plasminogen-plasmin activating system. In the present paper, we studied heat-shock protein 90 (Hsp90) involvement in this mechanism.

methodsHT-1080 fibrosarcoma cell migration and invasion were studied in artificial wound assay and modified Boyden chamber assay, respectively. Heat-shock protein 90 was studied by western blot and immunofluorescence. Matrix metalloproteinase-2 and urokinase plasminogen activator (uPA) were studied by gelatin ± plasminogen zymography and immunofluorescence. Heat-shock protein 90 partners were studied by immunoprecipitation. Messenger RNA expression was studied using real-time PCR. Small interfering RNAs were used to confirm the essential role of Hsp90.

resultsWe showed that kappa-elastin and VGVAPG elastin hexapeptide stimulated Hsp90, pro-MMP-2 and uPA secretion within 6 h, whereas AGVPGLGVG and GRKRK peptides had no effect. No increase of mRNA level was observed. Heat-shock protein 90-specific inhibitors inhibit EDP-stimulated HT-1080 cell-invasive capacity and restrained EDP-stimulated pro-MMP-2 and uPA secretions. The inhibitory effect was reproduced by using Hsp90-blocking antibody or Hsp90 knockdown by siRNA. Heat-shock protein 90 interacted with and stabilised uPA and pro-MMP-2 in conditioned culture media of HT-1080 fibrosarcoma cells.

conclusionsTaken together, our results demonstrate that EDPs exert protumoural activities through an Hsp90-dependent mechanism involving pro-MMP-2 and uPA.

Indexed as

Cell Line, TumorCell MovementElastinFibrosarcomaHSP90 Heat-Shock ProteinsHumansMatrix Metalloproteinase 2Neoplasm InvasivenessPeptide FragmentsTransfectionUrokinase-Type Plasminogen ActivatorCol-1 peptide, humanElastinHSP90 Heat-Shock ProteinsMatrix Metalloproteinase 2Peptide FragmentsUrokinase-Type Plasminogen Activator

Identifiers

PMID24874477
PMCPMC4090727
OpenAlexW2079238342

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.