Evidence map›Paper›PMID 18022611›Full record

ArticleDevelopmental biology2008

Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis.

Joanne Shi, Mi-Young Son, Susan Yamada, Ludmila Szabova, Stacie Kahan, Kaliopi Chrysovergis, Lauren Wolf, Andrew Surmak, Kenn Holmbeck

Registry-linked trialOpen access · greenAbstract read
In one paragraph

Article in Developmental biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04463290 (Association of Single Nucleotide Polymorphisms), which is not on this map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.7field-weighted citation impact, top 5% 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.

NCT04463290 unknown statusnot on this mapstarted 2020, after this paper: background citation

Association of Single Nucleotide Polymorphisms (SNPs) in Metalloproteinases (MMPs) Genes With the Risk of Primary Knee Osteoarthritis in Greek Population.

TypeobservationalSponsorAristotle University Of ThessalonikiRan2020 to 2022Enrolled200ConditionsMetalloproteinase SNPs -1575 G/A MMP-2, 836 A/G MMP-9 and -77 A/G MMP-13 and Risk for Developing Knee Osteoarthritis in Greek PopulationArmsNo intervention, Patients selection based on clinical symptoms and radiological imaging
3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
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  4. Article
  5. Vanadium Modulates Proteolytic Activities and MMP-14-Like Levels duringInternational journal of molecular sciences · 2022
    Article
  6. Review
  7. Review
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  11. Review
  12. Article
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  14. Article
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  17. Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  18. Article
  19. Article
  20. Riding the metalloproteinase roller coaster.The Journal of biological chemistry · 2017
    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

9 authors at 1 institution in 1 country.

Joanne ShiMatrix Metalloproteinase Unit, Craniofacial and Skeletal Diseases Branch, National Institute of Dental and Craniofacial Research, NIH, Bldg. 30, Room 125, 30 Convent Drive, MSC 4380, Bethesda, MD 20892-4380, USA.
Mi-Young Son
Susan Yamada
Ludmila Szabova
Stacie Kahan
Kaliopi Chrysovergis
Lauren Wolf
Andrew Surmak
Kenn Holmbeck
National Institute of Dental and Craniofacial Research · US

Funding

Matrix Metalloproteinases: Remodelling of the ExtracelluZ01DE000676 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI ROBEY, PAMELA G · 1996 to 2008
$2.3M
Intramural NIH HHS Z01 DE000676Intramural NIH HHS Z99 DE999999
6 · The paper itself

Abstract

Peri-cellular remodeling of mesenchymal extracellular matrices is considered a prerequisite for cell proliferation, motility and development. Here we demonstrate that membrane-type 3 MMP, MT3-MMP, is expressed in mesenchymal tissues of the skeleton and in peri-skeletal soft connective tissue. Consistent with this localization, MT3-MMP-deficient mice display growth inhibition tied to a decreased viability of mesenchymal cells in skeletal tissues. We document that MT3-MMP works as a major collagenolytic enzyme, enabling cartilage and bone cells to cleave high-density fibrillar collagen and modulate their resident matrix to make it permissive for proliferation and migration. Collectively, these data uncover a novel extracellular matrix remodeling mechanism required for proper function of mesenchymal cells. The physiological significance of MT3-MMP is highlighted in mice double deficient for MT1-MMP and MT3-MMP. Double deficiency transcends the combined effects of the individual single deficiencies and leads to severe embryonic defects in palatogenesis and bone formation incompatible with life. These defects are directly tied to loss of indispensable collagenolytic activities required in collagen-rich mesenchymal tissues for extracellular matrix remodeling and cell proliferation during embryogenesis.

Indexed as

Cell ProliferationOsteogenesisAnimalsCollagenExtracellular MatrixMatrix Metalloproteinase 14Matrix Metalloproteinase 16MesodermMetallothionein 3MiceMice, KnockoutPalateSkullCollagenMatrix Metalloproteinase 14Matrix Metalloproteinase 16Metallothionein 3Mt3 protein, mouse

Identifiers

PMID18022611
PMCPMC2262846
OpenAlexW2012083187

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.