Evidence map›Paper›PMID 24771611›Full record

ArticleJournal of cellular biochemistry2014

A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells.

Polly J Phillips-Mason, Sonya E L Craig, Susann M Brady-Kalnay

Abstract read
In one paragraph

Article in Journal of cellular biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Endothelial protease-activated receptor 4: impotent or important?Frontiers in cardiovascular medicine · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. PTPmu-targeted nanoparticles label invasive pediatric and adult glioblastoma.Nanomedicine : nanotechnology, biology, and medicine · 2020
    Article
  9. Article
  10. Review
  11. A PTPmu Biomarker is Associated with Increased Survival in Gliomas.International journal of molecular sciences · 2019
    Article
  12. Article
  13. Review
  14. 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

3 authors at 1 institution in 1 country.

Polly J Phillips-MasonDepartment of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio, 44106-4960.
Sonya E L Craig
Susann M Brady-Kalnay
Case Western Reserve University · US

Funding

Detecting invading glioma cells through in vivo molecular imaging of the cell surR01NS063971 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI BRADY-KALNAY, SUSANN M · 2009 to 2013
$1.9M
NINDS NIH HHS R01 NS063971NINDS NIH HHS R01-NS063971
6 · The paper itself

Abstract

Cleavage of the cell-cell adhesion molecule, PTPµ, occurs in human glioblastoma multiforme brain tumor tissue and glioma cell lines. PTPµ cleavage is linked to increased cell motility and growth factor independent survival of glioma cells in vitro. Previously, PTPµ was shown to be cleaved by furin in the endoplasmic reticulum to generate membrane associated E- (extracellular) and P- (phosphatase) subunits, and by ADAMs and the gamma secretase complex at the plasma membrane. We also identified the presence of additional extracellular and intracellular PTPµ fragments in brain tumors. We set out to biochemically analyze PTPµ cleavage in cancer cells. We determined that, in addition to the furin-processed form of PTPµ, a pool of 200 kDa full-length PTPµ exists at the plasma membrane that is cleaved directly by ADAM to generate a larger shed form of the PTPµ extracellular segment. Notably, in glioma cells, full-length PTPµ is also subject to calpain cleavage, which generates novel PTPµ fragments not found in other immortalized cells. We also observed glycosylation and phosphorylation differences in the cancer cells. Our data suggest that an additional serine protease also contributes to PTPµ shedding in glioma cells. We hypothesize that a "protease storm" occurs in cancer cells whereby multiple proteases converge to reduce the presence of cell-cell adhesion molecules at the plasma membrane and to generate protein fragments with unique biological functions. As a consequence, the "protease storm" could promote the migration and invasion of tumor cells.

Indexed as

ADAM ProteinsBrain NeoplasmsCalpainCell Adhesion MoleculesCell Line, TumorCell MovementFurinGlioblastomaGlycosylationHumansPhosphorylationReceptor-Like Protein Tyrosine Phosphatases, Class 2ADAM ProteinsCalpainCell Adhesion MoleculesFurinFURIN protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 2PROTEOLYSIS; SHEDDING; PTPmu; RECEPTOR PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE; ADAM; CALPAIN; FURIN; SERINE PROTEASE; GLIOMA

Identifiers

PMID24771611
PMCPMC4600327
OpenAlexW2140292255

What OpenQuestion holds

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LicenceTDM
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.