Evidence map›Paper›PMID 32286475›Full record

ArticleScientific reports2020

Analysis of the inhibiting activity of reversion-inducing cysteine-rich protein with Kazal motifs (RECK) on matrix metalloproteinases.

Soraia R Mendes, Laura Del Amo-Maestro, Laura Marino-Puertas, Iñaki de Diego, Theodoros Goulas, F Xavier Gomis-Rüth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Matrix Metalloproteinases in Inflammatory Dermatoses.International journal of molecular sciences · 2025
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. TwoGenes · 2021
    Article
  11. Review
  12. Article
  13. Article
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

6 authors at 1 institution in 1 country.

Soraia R MendesProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain.
Laura Del Amo-MaestroProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain.
Laura Marino-PuertasProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain.
Iñaki de DiegoProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain.
Theodoros GoulasProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain.
F Xavier Gomis-RüthProteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Higher Scientific Research Council (CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac, 15-21, 08028, Barcelona, Catalonia, Spain. xgrcri@ibmb.csic.es.
Institut de Biologia Molecular de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) occur in 23 human paralogues with key functions in physiology, and their activity is controlled by protein inhibitors. Reversion-inducing cysteine-rich protein with Kazal motifs (RECK), which is essential for embryogenesis and tumour suppression, has been reported to inhibit MMPs. Here, we developed eukaryotic and bacterial expression systems for different RECK variants and analysed their inhibitory capacity against representative MMPs in vitro. We could not detect any significant inhibition. Instead, we found that partially purified RECK from the conditioned medium of transfected Expi293F cells but not that of ExpiCHO-S or Drosophila Schneider cells contained a contaminant with proteolytic activity. The contaminant was removed through treatment with a small-molecule serine peptidase inhibitor and additional chromatographic purification. A tantamount contaminant was further detected in an equivalent expression system of the N-terminal fragment of the proteoglycan testican 3, but not in those of two other proteins. These results indicate that previous reports of inhibitory activity of recombinant RECK on MMPs, which were performed with partially purified samples, were probably masked by a coeluting contaminant present in the supernatant of HEK293-derived cells. Thus, RECK is probably not a direct inhibitor of MMP catalytic activity but may still regulate MMPs through other mechanisms.

Indexed as

AnimalsCHO CellsCricetulusDrosophila melanogasterEnzyme AssaysGPI-Linked ProteinsHEK293 CellsHumansMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesProteolysisRecombinant ProteinsTransfectionGPI-Linked ProteinsMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesRECK protein, humanRecombinant Proteins

Identifiers

PMID32286475
PMCPMC7156630
OpenAlexW3015566295

What OpenQuestion holds

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Registered trials

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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.