Evidence map›Paper›PMID 20308072›Full record

ArticleThe Journal of biological chemistry2010

Biochemical characterization of the cellular glycosylphosphatidylinositol-linked membrane type-6 matrix metalloproteinase.

Ilian A Radichev, Albert G Remacle, Sergey A Shiryaev, Angela N Purves, Sherida L Johnson, Maurizio Pellecchia, Alex Y Strongin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Peripheral membrane associations of matrix metalloproteinases.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  7. Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  8. Article
  9. Article
  10. Biochemical and Biological Attributes of Matrix Metalloproteinases.Progress in molecular biology and translational science · 2017
    Review
  11. Matrix metalloproteinases as reagents for cell isolation.Enzyme and microbial technology · 2016
    Article
  12. Article
  13. Article
  14. Interstitial collagen catabolism.The Journal of biological chemistry · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

7 authors at 1 institution in 1 country.

Ilian A RadichevSanford-Burnham Medical Research Institute, La Jolla, California 92037, USA.
Albert G Remacle
Sergey A Shiryaev
Angela N Purves
Sherida L Johnson
Maurizio Pellecchia
Alex Y Strongin
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

METALLOPROTEINASES IN TUMOR NEOVASCULARIZATIONR01CA083017 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2014
$3.8M
MT1-MMP pericellular proteolysis in malignancyR01CA077470 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2009
$3.1M
NCI NIH HHS CA77470NCI NIH HHS CA83017NCI NIH HHS R01 CA077470NCI NIH HHS R01 CA083017
6 · The paper itself

Abstract

Ubiquitously expressed membrane type-1 matrix metalloproteinase (MT1-MMP), an archetype member of the MMP family, binds tissue inhibitor of metalloproteinases-2 (TIMP-2), activates matrix metalloproteinase-2 (MMP-2), and stimulates cell migration in various cell types. In contrast with MT1-MMP, the structurally similar MT6-MMP associates with the lipid raft compartment of the plasma membrane using a GPI anchor. As a result, MT6-MMP is functionally distinct from MT1-MMP. MT6-MMP is insufficiently characterized as yet. In addition, a number of its biochemical features are both conflicting and controversial. To reassess the biochemical features of MT6-MMP, we have expressed the MT6-MMP construct tagged with a FLAG tag in breast carcinoma MCF-7 and fibrosarcoma HT1080 cells. We then used phosphatidylinositol-specific phospholipase C to release MT6-MMP from the cell surface and characterized the solubilized MT6-MMP fractions. We now are confident that cellular MT6-MMP partially exists in its complex with TIMP-2. Both TIMP-1 and TIMP-2 are capable of inhibiting the proteolytic activity of MT6-MMP. MT6-MMP does not stimulate cell migration. MT6-MMP, however, generates a significant level of gelatinolysis of the fluorescein isothiocyanate-labeled gelatin and exhibits an intrinsic, albeit low, ability to activate MMP-2. As a result, it is exceedingly difficult to record the activation of MMP-2 by cellular MT6-MMP. Because of its lipid raft localization, cellular MT6-MMP is inefficiently internalized. MT6-MMP is predominantly localized in the cell-to-cell junctions. Because MT6-MMP has been suggested to play a role in disease, including cancer and autoimmune multiple sclerosis, the identity of its physiologically relevant cleavage targets remains to be determined.

Indexed as

AnimalsCHO CellsCricetinaeCricetulusEnzyme ActivationGlycosylphosphatidylinositolsGPI-Linked ProteinsHumansIntercellular JunctionsMatrix Metalloproteinase 14Matrix Metalloproteinase 2Matrix Metalloproteinases, Membrane-AssociatedMembrane MicrodomainsMultiple SclerosisMultiprotein ComplexesNeoplasmsGlycosylphosphatidylinositolsGPI-Linked ProteinsMatrix Metalloproteinase 14Matrix Metalloproteinase 2matrix metalloproteinase 25Matrix Metalloproteinases, Membrane-AssociatedMultiprotein ComplexesTissue Inhibitor of Metalloproteinase-2Type C Phospholipases

Identifiers

PMID20308072
PMCPMC2871476
OpenAlexW2047973155

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.