Evidence map›Paper›PMID 20937775›Full record

ArticleMolecular and cellular biology2010

The protein kinase C cascade regulates recruitment of matrix metalloprotease 9 to podosomes and its release and activation.

Helan Xiao, Xiao-Hui Bai, Andras Kapus, Wei-Yang Lu, Alan S Mak, Mingyao Liu

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  5. Article
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  7. Review
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Protein kinase C, focal adhesions and the regulation of cell migration.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2014
    Review
  15. Review
  16. Article
  17. Review
  18. p53 in cell invasion, podosomes, and invadopodia.Cell adhesion & migration · 2014
    Review
  19. Article
  20. Atypical protein kinase C in cell motility.Cellular and molecular life sciences : CMLS · 2013
    Review
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

6 authors at 4 institutions in 1 country.

Helan XiaoDivision of Cell and Molecular Biology, University Health Network Toronto General Research Institute, Toronto, Ontario, Canada.
Xiao-Hui Bai
Andras Kapus
Wei-Yang Lu
Alan S Mak
Mingyao Liu
University Health Network · CAQueen's University · CASt. Michael's Hospital · CAWestern University · CA

Funding

Canadian Institutes of Health Research MOP-13270Canadian Institutes of Health Research MOP-42546
6 · The paper itself

Abstract

Podosomes are transient cell surface structures essential for degradation of extracellular matrix during cell invasion. Protein kinase C (PKC) is involved in the regulation of podosome formation; however, the roles of individual PKC isoforms in podosome formation and proteolytic function are largely unknown. Recently, we reported that PDBu, a PKC activator, induced podosome formation in normal human bronchial epithelial cells. Here, we demonstrate that phorbol-12,13-dibutyrate (PDBu)-induced podosome formation is mainly mediated through redistribution of conventional PKCs, especially PKCα, from the cytosol to the podosomes. Interestingly, although blocking atypical PKCζ did not affect PDBu-induced podosome formation, it significantly reduced matrix degradation at podosomes. Inhibition of PKCζ reduced recruitment of matrix metalloprotease 9 (MMP-9) to podosomes and its release and activation. Downregulation of MMP-9 by small interfering RNA (siRNA) or neutralization antibody also significantly reduced matrix degradation. The regulatory effects of PKCζ on matrix degradation and recruitment of MMP-9 to podosomes were PKCζ kinase activity dependent. PDBu-induced recruitment of PKCζ and MMP-9 to podosomes was blocked by inhibition of novel PKC with rottlerin or PKCδ siRNA. Our data suggest that multiple PKC isozymes form a signaling cascade that controls podosome formation and dynamics and MMP-9 recruitment, release, and activation in a coordinated fashion.

Indexed as

Base SequenceBiological Transport, ActiveCells, CulturedCell Surface ExtensionsDNA PrimersEpithelial CellsExtracellular MatrixGene Knockdown TechniquesHumansIsoenzymesMatrix Metalloproteinase 14Matrix Metalloproteinase 9Matrix Metalloproteinase InhibitorsPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CDNA PrimersIsoenzymesMatrix Metalloproteinase 14Matrix Metalloproteinase 9Matrix Metalloproteinase InhibitorsMMP14 protein, humanPhorbol 12,13-DibutyrateProtein Kinase CProtein Kinase C zetaRNA, Small Interfering

Identifiers

PMID20937775
PMCPMC2976425
OpenAlexW2047054436

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.