Evidence map›Paper›PMID 25081520›Full record

ArticleCancer medicine2014

Functional relationship between matrix metalloproteinase-11 and matrix metalloproteinase-14.

Emilie Buache, Robert Thai, Corinne Wendling, Fabien Alpy, Adeline Page, Marie-Pierre Chenard, Vincent Dive, Marc Ruff, Annick Dejaegere, Catherine Tomasetto and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cancer medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Selected Cytokines and Metalloproteinases in Inflammatory Bowel Disease.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Article
  10. Review
  11. The Expanding Role of MT1-MMP in Cancer Progression.Pharmaceuticals (Basel, Switzerland) · 2019
    Review
  12. Article
  13. Review
  14. Article
  15. HRenal failure · 2017
    Article
  16. Review
  17. Article
  18. 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

11 authors at 6 institutions in 1 country.

Emilie BuacheInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Department of Functional Genomics and Cancer, CNRS UMR 7104, INSERM U964, Université de Strasbourg, Illkirch, France.
Robert Thai
Corinne Wendling
Fabien Alpy
Adeline Page
Marie-Pierre Chenard
Vincent Dive
Marc Ruff
Annick Dejaegere
Catherine Tomasetto
Marie-Christine Rio
Centre National de la Recherche Scientifique · FRUniversité de Strasbourg · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRHôpital d'Hautepierre · FRInstitut de génétique et de biologie moléculaire et cellulaire · FRLa Ligue Contre le Cancer · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MMP-11 is a key factor in physiopathological tissue remodeling. As an active form is secreted, its activity must be tightly regulated to avoid detrimental effects. Although TIMP-1 and TIMP-2 reversibly inhibit MMP-11, another more drastic scenario, presumably via hydrolysis, could be hypothesized. In this context, we have investigated the possible implication of MMP-14, since it exhibits a spatiotemporal localization similar to MMP-11. Using native HFL1-produced MMP-11 and HT-1080-produced MMP-14 as well as recombinant proteins, we show that MMP-11 is a MMP-14 substrate. MMP-14 cleaves MMP-11 catalytic domain at the PGG(P1)-I(P1')LA and V/IQH(P1)-L(P1')YG scissile bonds, two new cleavage sites. Interestingly, a functional test showed a dramatical reduction in MMP-11 enzymatic activity when incubated with active MMP-14, whereas inactive point-mutated MMP-14 had no effect. This function is conserved between human and mouse. Thus, in addition to the canonical reversible TIMP-dependent inhibitory system, irreversible MMP proteolytic inactivation might occur by cleavage of the catalytic domain in a MMP-dependent manner. Since MMP-14 is produced by HT-1080 cancer cells, whereas MMP-11 is secreted by HFL1 stromal cells, our findings support the emerging importance of tumor-stroma interaction/cross-talk. Moreover, they highlight a Janus-faced MMP-14 function in the MMP cascade, favoring activation of several pro-MMPs, but limiting MMP-11 activity. Finally, both MMPs are active at the cell periphery. Since MMP-14 is present at the cell membrane, whereas MMP-11 is soluble into the cellular microenvironment, this MMP-14 function might represent one critical regulatory mechanism to control the extent of pericellular MMP-11 bioavailability and protect cells from excessive/inappropriate MMP-11 function.

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainCell Line, TumorEnzyme ActivationGene ExpressionHumansMatrix Metalloproteinase 11Matrix Metalloproteinase 14MiceModels, MolecularMolecular Sequence DataNeoplasmsProtein ConformationProteolysisRecombinant ProteinsMatrix Metalloproteinase 11Matrix Metalloproteinase 14Recombinant ProteinsCell microenvironmentepithelial-stromal cell interactionMMP inactivationtissue remodeling

Identifiers

PMID25081520
PMCPMC4302670
OpenAlexW1995047976

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.