Evidence map›Paper›PMID 29165389›Full record

ReviewInternational journal of molecular sciences2017

Proteinase-Activated Receptor 2 May Drive Cancer Progression by Facilitating TGF-β Signaling.

Hendrik Ungefroren, David Witte, Bernhard H Rauch, Utz Settmacher, Hendrik Lehnert, Frank Gieseler, Roland Kaufmann

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. 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
1.6field-weighted citation impact, top 15% 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, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  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 3 institutions in 1 country.

Hendrik UngefrorenFirst Department of Medicine, University Hospital Schleswig-Holstein, D-23538 Lübeck, Germany. hendrik.ungefroren@uksh.de.
David WitteFirst Department of Medicine, University Hospital Schleswig-Holstein, D-23538 Lübeck, Germany. davidwittemail@gmail.com.
Bernhard H RauchDepartment of General Pharmacology, Institute of Pharmacology, University Medicine Greifswald, D-17487 Greifswald, Germany. Bernhard.Rauch@uni-greifswald.de.ORCID 0000-0002-6003-4662
Utz SettmacherDepartment of General, Visceral and Vascular Surgery, Jena University Hospital, D-07747 Jena, Germany. Utz.Settmacher@med.uni-jena.de.
Hendrik LehnertFirst Department of Medicine, University Hospital Schleswig-Holstein, D-23538 Lübeck, Germany. Hendrik.Lehnert@uni-luebeck.de.
Frank GieselerFirst Department of Medicine, University Hospital Schleswig-Holstein, D-23538 Lübeck, Germany. frank.gieseler@uksh.de.ORCID 0000-0001-6409-3822
Roland KaufmannDepartment of General, Visceral and Vascular Surgery, Jena University Hospital, D-07747 Jena, Germany. Roland.Kaufmann@med.uni-jena.de.
University Hospital Schleswig-Holstein · DEJena University Hospital · DEUniversitätsmedizin Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The G protein-coupled receptor proteinase-activated receptor 2 (PAR2) has been implicated in various aspects of cellular physiology including inflammation, obesity and cancer. In cancer, it usually acts as a driver of cancer progression in various tumor types by promoting invasion and metastasis in response to activation by serine proteinases. Recently, we discovered another mode through which PAR2 may enhance tumorigenesis: crosstalk with transforming growth factor-β (TGF-β) signaling to promote TGF-β1-induced cell migration/invasion and invasion-associated gene expression in ductal pancreatic adenocarcinoma (PDAC) cells. In this chapter, we review what is known about the cellular TGF-β responses and signaling pathways affected by PAR2 expression, the signaling activities of PAR2 required for promoting TGF-β signaling, and the potential molecular mechanism(s) that underlie(s) the TGF-β signaling-promoting effect. Since PAR2 is activated through various serine proteinases and biased agonists, it may couple TGF-β signaling to a diverse range of other physiological processes that may or may not predispose cells to cancer development such as local inflammation, systemic coagulation and pathogen infection.

Indexed as

Signal TransductionAnimalsCell Transformation, NeoplasticDisease ProgressionHumansNeoplasmsProtein BindingProtein Serine-Threonine KinasesReceptor, PAR-2Receptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ITransforming Growth Factor betaProtein Serine-Threonine KinasesReceptor, PAR-2Receptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ITGFBR1 protein, humanTransforming Growth Factor betaALK5pancreatic carcinomaPAR2serine proteinasessignalingTGF-β

Identifiers

PMID29165389
PMCPMC5713460
OpenAlexW2770605651

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.