Evidence map›Paper›PMID 23413031›Full record

ArticleThe Journal of biological chemistry2013

Targeting a single function of the multifunctional matrix metalloprotease MT1-MMP: impact on lymphangiogenesis.

Signe Ingvarsen, Astrid Porse, Charlotte Erpicum, Ludovic Maertens, Henrik J Jürgensen, Daniel H Madsen, Maria C Melander, Henrik Gårdsvoll, Gunilla Høyer-Hansen, Agnès Noel and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Matrix Metalloproteinase 14 in Corneal Neovascularization.International journal of molecular sciences · 2026
    Review
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  11. A DNA aptamer recognizing MMP14 forOncology letters · 2019
    Article
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  19. The role of lymphangiogenesis and angiogenesis in tumor metastasis.Cellular oncology (Dordrecht, Netherlands) · 2016
    Review
  20. 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

13 authors at 4 institutions in 3 countries.

Signe IngvarsenFinsen Laboratory, Rigshospitalet/BRIC, DK-2200 Copenhagen N, Denmark.
Astrid Porse
Charlotte Erpicum
Ludovic Maertens
Henrik J Jürgensen
Daniel H Madsen
Maria C Melander
Henrik Gårdsvoll
Gunilla Høyer-Hansen
Agnès Noel
Kenn Holmbeck
Lars H Engelholm
Niels Behrendt
Rigshospitalet · DKUniversity of Liège · BENational Institutes of Health · USUniversity of Copenhagen · DK

Funding

Matrix Metalloproteinases: Remodeling of the Extracellular MatrixZIADE000676 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI ROBEY, PAMELA G · 2009 to 2017
$9.7M
Intramural NIH HHS
6 · The paper itself

Abstract

The group of matrix metalloproteases (MMPs) is responsible for multiple processes of extracellular matrix remodeling in the healthy body but also for matrix and tissue destruction during cancer invasion and metastasis. The understanding of the contributions from each individual MMP, both in healthy and pathological events, has been complicated by the lack of specific inhibitors and the fact that some of the potent MMPs are multifunctional enzymes. These factors have also hampered the setup of therapeutic strategies targeting MMP activity. A tempting target is the membrane-associated MT1-MMP, which has well-documented importance in matrix degradation but which takes part in more than one pathway in this regard. In this report, we describe the selective targeting of a single function of this enzyme by means of a specific monoclonal antibody against MT1-MMP, raised in an MT1-MMP knock-out mouse. The antibody blocks the enzyme ability to activate proMMP-2 without interfering with the collagenolytic function or the general proteolytic activity of MT1-MMP. Using this antibody, we have shown that the MT1-MMP-catalyzed activation of proMMP-2 is involved in the outgrowth of cultured lymphatic endothelial cells in a collagen matrix in vitro, as well as in lymphatic vessel sprouting assayed ex vivo. This is the first example of the complete inactivation of a single function of a multifunctional MMP and the use of this strategy to pursue its role.

Indexed as

AnimalsAntibodies, Monoclonal, Murine-DerivedCHO CellsCricetinaeEnzyme ActivationEnzyme PrecursorsExtracellular MatrixGelatinasesHumansLymphangiogenesisMatrix Metalloproteinase 14MiceMice, KnockoutNeoplasm MetastasisNeoplasm ProteinsNeoplasmsAntibodies, Monoclonal, Murine-DerivedEnzyme PrecursorsGelatinasesMatrix Metalloproteinase 14MMP14 protein, humanMmp14 protein, mouseNeoplasm Proteinsprogelatinase

Identifiers

PMID23413031
PMCPMC3624404
OpenAlexW2033691351

What OpenQuestion holds

Textmetadata
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.