Evidence map›Paper›PMID 18794797›Full record

ArticleOncogene2008

Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor.

J Wykosky, E Palma, D M Gibo, S Ringler, C P Turner, W Debinski

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

85 citing papers in PubMed, 137 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Targeting the EphA2 pathway: could it be the way for bone sarcomas?Cell communication and signaling : CCS · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. World journal of gastrointestinal oncology · 2022
    Review
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

J WykoskyDepartment of Neurosurgery, Brain Tumor Center of Excellence, Wake Forest University School of Medicine, Comprehensive Cancer Center, Winston-Salem, NC 27157, USA.
E Palma
D M Gibo
S Ringler
C P Turner
W Debinski
Wake Forest University · US

Funding

Training Program in Translational Radiation OncologyT32CA113267 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI BLACKSTOCK, ARTHUR W · 2005 to 2014
$2.6M
EphA2: Function and Targeting in Malignant GliomasF31NS055533 · NINDS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI WYKOSKY, JILL E · 2006 to 2008
$82k
NCI NIH HHS 5 T32 CA113267-04NCI NIH HHS T32 CA113267NINDS NIH HHS F31 NS055533PHS HHS 1 F31 NSO55533-01
6 · The paper itself

Abstract

The ephrinA1 ligand exerts antioncogenic effects in tumor cells through activation and downregulation of the EphA2 receptor and has been described as a membrane-anchored protein requiring clustering for function. However, while investigating the ephrinA1/EphA2 system in the pathobiology of glioblastoma multiforme (GBM), we uncovered that ephrinA1 is released from GBM and breast adenocarcinoma cells as a soluble, monomeric protein and is a functional form of the ligand in this state. Conditioned media containing a soluble monomer of ephrinA1 caused EphA2 internalization and downregulation, dramatic alteration of cell morphology and suppression of the Ras-MAPK pathway. Moreover, soluble monomeric ephrinA1 was functional in a physiological context, eliciting collapse of embryonic neuronal growth cones. We also found that ephrinA1 is cleaved from the plasma membrane of GBM cells, an event which involves the action of a metalloprotease. Thus, the ephrinA1 ligand can, indeed, function as a soluble monomer and may act in a paracrine manner on the EphA2 receptor without the need for juxtacrine interactions. These findings have important implications for further deciphering the function of these proteins in pathology and physiology, as well as for the design of ephrinA1-based EphA2-targeted antitumor therapeutics.

Indexed as

Biophysical PhenomenaCell Line, TumorEphrin-A1Gene Expression RegulationGlioblastomaHumansLigandsReceptor, EphA2SolubilityTransfectionEphrin-A1LigandsReceptor, EphA2

Identifiers

PMID18794797
PMCPMC3683835
OpenAlexW2079223115

What OpenQuestion holds

Textmetadata
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.