Mammalian ionotropic glutamate receptors

Curr Opin Neurobiol. 1993 Jun;3(3):291-8. doi: 10.1016/0959-4388(93)90120-n.


Exciting new milestones in glutamate receptor (GluR) channel research include the following: the cloning of N-methyl-D-aspartate (NMDA) receptors; delineation of molecular determinants for ion flow through glutamate-gated channels; the discovery that Ca2+ permeability of non-NMDA receptor channels is determined by RNA editing; the construction of antibodies and their use in immunocytochemical localizations of alpha-amino-3-hydroxy-5-methyl isoxazole-4-propionic acid (AMPA) receptor subunits in the rat brain; and the return to prominence of the high-affinity kainate site with the publication of cDNA sequences for subunits (GluR-5, -6, -7; KA-1, -2) constituting subtypes of this site. Major unresolved issues comprise the transmembrane topology and subunit stoichiometries of native receptor channels.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Humans
  • Molecular Sequence Data
  • Receptors, AMPA
  • Receptors, Glutamate / physiology*
  • Receptors, Kainic Acid
  • Receptors, N-Methyl-D-Aspartate / physiology


  • Receptors, AMPA
  • Receptors, Glutamate
  • Receptors, Kainic Acid
  • Receptors, N-Methyl-D-Aspartate