Extension of glial processes by activation of Ca2+-permeable AMPA receptor channels

Neuroreport. 2001 Mar 26;12(4):745-8. doi: 10.1097/00001756-200103260-00026.

Abstract

AMPA type-glutamate receptor channels (AMPARs) assembled without the GluR2 (GluR-B) subunit are characterized by high Ca2+ permeability, and are expressed abundantly in cerebellar Bergmann glial cells. Here we show that the morphology of cultured Bergmann glia-like fusiform cells derived from the rat cerebellum was changed by manipulating expression of Ca2+-permeable AMPARs using adenoviral vector-mediated gene transfer. Converting endogenous Ca2+-permeable AMPARs into Ca2+-impermeable channels by viral-mediated transfer of GluR2 gene induced retraction of glial processes. In contrast, overexpression of Ca2+-permeable AMPARs markedly elongated glial processes. The process extension was blocked by 2,3-Dihydroxy-6-nitro-7-sulfamoylbenzo(F)quinoxaline (NBQX), a specific antagonist of AMPAR. These results indicate that glutamate regulates the morphology of glial processes by activating Ca2+-permeable AMPARs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / genetics
  • Animals
  • Calcium / metabolism*
  • Cell Size / drug effects
  • Cell Size / physiology
  • Cells, Cultured
  • Cerebellum / cytology
  • Excitatory Amino Acid Antagonists / pharmacology
  • Gene Expression / physiology
  • Glutamic Acid / pharmacology
  • Neuroglia / cytology
  • Neuroglia / drug effects
  • Neuroglia / metabolism*
  • Quinoxalines / pharmacology
  • Rats
  • Rats, Wistar
  • Receptors, AMPA / antagonists & inhibitors
  • Receptors, AMPA / genetics
  • Receptors, AMPA / metabolism*

Substances

  • Excitatory Amino Acid Antagonists
  • Quinoxalines
  • Receptors, AMPA
  • 2,3-dioxo-6-nitro-7-sulfamoylbenzo(f)quinoxaline
  • Glutamic Acid
  • glutamate receptor ionotropic, AMPA 2
  • Calcium