HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

Functional activation of EphA5 receptor does not promote cell proliferation in the aberrant EphA5 expressing human glioblastoma U-118 MG cell line.

Abstract
Eph receptors are a subfamily of receptor tyrosine kinases (RTKs), that are activated by ephrin ligands and appear to play important roles in axon guidance and cell migration during development of the nervous system. Over-expression or constitutive activation of Eph receptors has been linked with increased proliferation in various tumours. We have recently described lineage aberrant expression of EphA5 in primary human astrocytomas, glioblastomas and in the human glioblastoma U-118 MG cell line. A role for EphA5 expression in these tumours is not apparent, and we have investigated the cellular effects of EphA5 activation using the human glioblastoma U-118 MG cell line as a model. Immunofluorescent staining demonstrated cell surface expression of EphA5. Activation of the EphA5 receptor using an ephrin-A1 recombinant fusion protein resulted in tyrosine phosphorylation of EphA5 in a time-dependent manner. Exposure of U-118 MG glioblastoma cells to ephrin-A1 did not result in significant spontaneous or FCS-stimulated cell proliferation, though a marginal decrease was observed. This is in converse to the effects of Eph activation in other tumour cell lines, and is the first study to investigate EphA5 in glioblastoma cell lines.
AuthorsV Bruce, G Olivieri, O Eickelberg, G C Miescher
JournalBrain research (Brain Res) Vol. 821 Issue 1 Pg. 169-76 (Mar 06 1999) ISSN: 0006-8993 [Print] Netherlands
PMID10064801 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright 1999 Elsevier Science B.V.
Chemical References
  • Ephrin-A1
  • Membrane Proteins
  • Proteins
  • Recombinant Fusion Proteins
  • Receptor Protein-Tyrosine Kinases
  • Receptor, EphA5
Topics
  • Cell Division (physiology)
  • Ephrin-A1
  • Glioblastoma (pathology, physiopathology)
  • Humans
  • Immunohistochemistry
  • Membrane Proteins (physiology)
  • Phosphorylation
  • Proteins (pharmacology)
  • Receptor Protein-Tyrosine Kinases (physiology)
  • Receptor, EphA5
  • Recombinant Fusion Proteins (pharmacology)
  • Tumor Cells, Cultured

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: