Evidence map›Paper›PMID 15371548›Full record

ArticleMolecular biology of the cell2004

Activities of the matrix metalloproteinase stromelysin-2 (MMP-10) in matrix degradation and keratinocyte organization in wounded skin.

Monika Krampert, Wilhelm Bloch, Takako Sasaki, Philippe Bugnon, Thomas Rülicke, Eckhard Wolf, Monique Aumailley, William C Parks, Sabine Werner

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.4field-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.

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

59 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Science advances · 2024
    Article
  7. Article
  8. Article
  9. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Matrix Metalloproteinases: How Much Can They Do?International journal of molecular sciences · 2020
    Article
  17. Review
  18. ΔViruses · 2019
    Article
  19. Wound Healing: A Cellular Perspective.Physiological reviews · 2019
    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

9 authors at 6 institutions in 3 countries.

Monika KrampertDepartment of Biology, Institute of Cell Biology, Eidgenössishe Technische Hochschule Zurich, 8093 Zurich, Switzerland.
Wilhelm Bloch
Takako Sasaki
Philippe Bugnon
Thomas Rülicke
Eckhard Wolf
Monique Aumailley
William C Parks
Sabine Werner
German Sport University Cologne · DELudwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DEUniversity of Cologne · DEUniversity of Washington · USUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The matrix metalloproteinase stromelysin-2 is expressed in keratinocytes of the epithelial tongue of skin wounds, suggesting a role in keratinocyte migration. Here, we show that stromelysin-2 enhances migration of cultured keratinocytes. To gain insight into the in vivo activities of stromelysin-2 in epithelial repair, we generated transgenic mice expressing a constitutively active stromelysin-2 mutant in keratinocytes. These animals had no alterations in skin architecture, and the healing rate of skin wounds was normal. Histologically, however, we found abnormalities in the organization of the wound epithelium. Keratinocytes at the migrating epidermal tip were scattered in most sections of mice with high expression level, and there was a reduced deposition of new matrix. In particular, the staining pattern of laminin-5 at the wound site was altered. This may be due to proteolytic processing of laminin-5 by stromelysin-2, because degradation of laminin-5 by this enzyme was observed in vitro. The inappropriate matrix contact of keratinocytes was accompanied by aberrant localization of beta1-integrins and phosphorylated focal adhesion kinase, as well as by increased apoptosis of wound keratinocytes. These results suggest that a tightly regulated expression level of stromelysin-2 is required for limited matrix degradation at the wound site, thereby controlling keratinocyte migration.

Indexed as

AnimalsApoptosisCell Adhesion MoleculesCell MovementCells, CulturedEpitheliumExtracellular MatrixFemaleFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene ExpressionHumansIntegrin beta1KalininKeratinocytesMaleCell Adhesion MoleculesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesIntegrin beta1KalininMatrix Metalloproteinase 10MetalloendopeptidasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktPTK2 protein, humanPtk2 protein, mouse

Identifiers

PMID15371548
PMCPMC532007
OpenAlexW2141880708

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.