Evidence map›Paper›PMID 17055228›Full record

ArticleMechanisms of development2007

Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development.

Takashi Hasebe, Rebecca Hartman, Liezhen Fu, Tosikazu Amano, Yun-Bo Shi

Erratum issuedAbstract read
In one paragraph

Article in Mechanisms of development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
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  5. Article
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  8. Remodelling the extracellular matrix in development and disease.Nature reviews. Molecular cell biology · 2014
    Review
  9. Article
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  11. Article
  12. Article
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  14. Article
  15. Article
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  18. Article
  19. Matrix metalloproteinases and the regulation of tissue remodelling.Nature reviews. Molecular cell biology · 2007
    Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors.

Takashi HasebeSection on Molecular Morphogenesis, Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bldg. 18T, Rm. 106, Bethesda, MD 20892, USA.
Rebecca Hartman
Liezhen Fu
Tosikazu Amano
Yun-Bo Shi

Funding

Molecular mechanism of thyroid hormone receptor function during metamorphosisZ01HD001901 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SHI, YUN-BO · 1995 to 2008
$2.1M
Regulation and function of matrix metalloproteinases during frog metamorphosisZ01HD008859 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SHI, YUN-BO · 2008 to 2008
$506k
Intramural NIH HHSNICHD NIH HHS Z01 HD001901-10
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are a large family of extracellular or membrane-bound proteases. Their ability to cleave extracellular matrix (ECM) proteins has implicated a role in ECM remodeling to affect cell fate and behavior during development and in pathogenesis. We have shown previously that membrane-type 1 (MT1)-MMP [corrected] is coexpressed temporally and spatially with the MMP gelatinase A (GelA) in all cell types of the intestine and tail where GelA is expressed during Xenopus laevis metamorphosis, suggesting a cooperative role of these MMPs in development. Here, we show that Xenopus GelA and MT1-MMP interact with each other in vivo and that overexpression of MT1-MMP and GelA together in Xenopus embryos leads to the activation of pro-GelA. We further show that both MMPs are expressed during Xenopus embryogenesis, although MT1-MMP gene is expressed earlier than the GelA gene. To investigate whether the embryonic MMPs play a role in development, we have studied whether precocious expression of these MMPs alters development. Our results show that overexpression of both MMPs causes developmental abnormalities and embryonic death by a mechanism that requires the catalytic activity of the MMPs. More importantly, we show that coexpression of wild type MT1-MMP and GelA leads to a cooperative effect on embryonic development and that this cooperative effect is abolished when the catalytic activity of either MMP is eliminated through a point mutation in the catalytic domain. Thus, our studies support a cooperative role of these MMPs in embryonic development, likely through the activation of pro-GelA by MT1-MMP.

Indexed as

AnimalsAnimals, Genetically ModifiedBase SequenceCatalytic DomainDNAEnzyme ActivationExtracellular MatrixGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicMatrix Metalloproteinase 14Matrix Metalloproteinase 2Mutagenesis, Site-DirectedPoint MutationProtein Structure, TertiaryRecombinant ProteinsXenopus laevisDNAMatrix Metalloproteinase 14Matrix Metalloproteinase 2Recombinant Proteins

Identifiers

PMID17055228
PMCPMC1820633

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.