Recombinant AMPA receptors with low Ca2+ permeability increase intracellular Ca2+ in HEK 293 cells

Neuroreport. 1997 May 27;8(8):1975-80. doi: 10.1097/00001756-199705260-00036.

Abstract

Although AMPA receptor subunit configuration controls the Ca2+ permeability of the ion channel, not much is known about Ca2+ signals generated by different AMPA receptor subtypes. We examined the Ca2+ signaling properties of recombinant AMPA receptors using patch clamp to determine ionic permeability properties and Ca2+ imaging to examine changes in intra-cellular Ca2+ level ([Ca2+]i). Activation of recombinant AMPA receptors robustly increased [Ca2+]i even in cells expressing heteromeric receptors containing edited GluRB, which harbored receptors with very low average Ca2+ permeability in patch clamp studies. The results suggest that whereas the GluRB subunit controls Ca2+ permeability, Ca2+ signaling mediated by AMPA receptors correlates poorly with the presence of GluRB.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Calcium / metabolism*
  • Cell Line
  • Cell Membrane Permeability / drug effects
  • Cell Membrane Permeability / physiology
  • Electrophysiology
  • Excitatory Amino Acid Agonists / pharmacology
  • Fura-2
  • Humans
  • Membrane Potentials / drug effects
  • Membrane Potentials / physiology
  • Patch-Clamp Techniques
  • Receptors, AMPA / agonists
  • Receptors, AMPA / metabolism*
  • Recombinant Proteins / metabolism

Substances

  • Excitatory Amino Acid Agonists
  • Receptors, AMPA
  • Recombinant Proteins
  • Calcium
  • Fura-2