Evidence map›Paper›PMID 18441011›Full record

ArticleThe Journal of biological chemistry2008

Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging.

Mingxing Ouyang, Shaoying Lu, Xiao-Yan Li, Jing Xu, Jihye Seong, Ben N G Giepmans, John Y-J Shyy, Stephen J Weiss, Yingxiao Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.6field-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

53 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Resource for FRET-Based Biosensor Optimization.Frontiers in cell and developmental biology · 2022
    Review
  7. Multiphoton intravital microscopy of rodents.Nature reviews. Methods primers · 2022
    Article
  8. Deficiency of IntegrinFrontiers in cell and developmental biology · 2022
    Article
  9. Intersection of stem cell biology and engineering towards next generationFrontiers in bioengineering and biotechnology · 2022
    Review
  10. Article
  11. Review
  12. Frontiers in physics · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 4 institutions in 3 countries.

Mingxing OuyangDepartment of Bioengineering and the Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana-Champaign, Illinois 61801, USA.
Shaoying Lu
Xiao-Yan Li
Jing Xu
Jihye Seong
Ben N G Giepmans
John Y-J Shyy
Stephen J Weiss
Yingxiao Wang
University of Illinois Urbana-Champaign · USUniversity of Michigan · USUniversity Medical Center Groningen · NLUniversity of California, Riverside · US

Funding

FUNCTION OF THE MEMBRANE TYPE MATRIX METALLOPROTEINASER01CA071699 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN J · 1997 to 2024
$7.3M
Flow Regulation of SREBP in AtherosclerosisR01HL077448 · NHLBI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI SHYY, JOHN Y-J Y-J · 2004 to 2007
$1.4M
NCI NIH HHS CA71699NHLBI NIH HHS HL77448
6 · The paper itself

Abstract

Membrane type 1 matrix metalloproteinase (MT1-MMP) plays a critical role in cancer cell biology by proteolytically remodeling the extracellular matrix. Utilizing fluorescence resonance energy transfer (FRET) imaging, we have developed a novel biosensor, with its sensing element anchoring at the extracellular surface of cell membrane, to visualize MT1-MMP activity dynamically in live cells with subcellular resolution. Epidermal growth factor (EGF) induced significant FRET changes in cancer cells expressing MT1-MMP, but not in MT1-MMP-deficient cells. EGF-induced FRET changes in MT1-MMP-deficient cells could be restored after reconstituting with wild-type MT1-MMP, but not MMP-2, MMP-9, or inactive MT1-MMP mutants. Deletion of the transmembrane domain in the biosensor or treatment with tissue inhibitor of metalloproteinase-2, a cell-impermeable MT1-MMP inhibitor, abolished the EGF-induced FRET response, indicating that MT1-MMP acts at the cell surface to generate FRET changes. In response to EGF, active MT1-MMP was directed to the leading edge of migrating cells along micropatterned fibronectin stripes, in tandem with the local accumulation of the EGF receptor, via a process dependent upon an intact cytoskeletal network. Hence, the MT1-MMP biosensor provides a powerful tool for characterizing the molecular processes underlying the spatiotemporal regulation of this critical class of enzymes.

Indexed as

Gene Expression Regulation, EnzymologicBiosensing TechniquesCell MembraneCell MovementEpidermal Growth FactorErbB ReceptorsFibronectinsFluorescence Resonance Energy TransferHeLa CellsHumansImage Processing, Computer-AssistedMatrix Metalloproteinase 14Models, BiologicalPlasmidsTissue Inhibitor of Metalloproteinase-2Epidermal Growth FactorErbB ReceptorsFibronectinsMatrix Metalloproteinase 14Tissue Inhibitor of Metalloproteinase-2

Identifiers

PMID18441011
PMCPMC2427332
OpenAlexW2059369244

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.