Signalling pathways involved in the chemotactic activity of CXCL12 in cultured rat cerebellar neurons and CHP100 neuroepithelioma cells

J Neuroimmunol. 2003 Feb;135(1-2):38-46. doi: 10.1016/s0165-5728(02)00432-0.

Abstract

We compared the signal transduction pathways activated by stromal cell-derived factor-1 (CXCL12) chemokine in two different cell systems: primary cultures of rat cerebellar granule neurons (CGN) and human neuroepithelioma CHP100 cells. Both cell types express functional CXC chemokine receptor 4 (CXCR4), which is coupled both to extracellular signal-regulated kinase (ERK) and Akt phosphorylation pathways. The activation of ERK shows different dependency on the phosphatidylinositol 3-kinase (PI3-K) pathway and different sensitivity to pertussis toxin (PTX) treatment, indicative of coupling to different G proteins in the two cell systems considered. We demonstrate that the inhibition of either the ERK kinase or the PI3-K pathways blocks the CXCL12 induced-chemotaxis in CHP100 cells; while only PI3-K activity is stringently necessary for CGN migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Movement / drug effects
  • Cells, Cultured
  • Cerebellum / metabolism*
  • Chemokine CXCL12
  • Chemokines, CXC / pharmacology*
  • Chemotactic Factors / pharmacology*
  • Inositol 1,4,5-Trisphosphate / metabolism
  • Mitogen-Activated Protein Kinases / metabolism
  • Neuroectodermal Tumors, Primitive, Peripheral / metabolism*
  • Pertussis Toxin / pharmacology
  • Phosphatidylinositol 3-Kinases / physiology
  • Phosphorylation
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Rats
  • Rats, Wistar
  • Signal Transduction*

Substances

  • CXCL12 protein, human
  • Chemokine CXCL12
  • Chemokines, CXC
  • Chemotactic Factors
  • Proto-Oncogene Proteins
  • Inositol 1,4,5-Trisphosphate
  • Pertussis Toxin
  • Akt1 protein, rat
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Mitogen-Activated Protein Kinases