Ion channel properties of a protein complex with characteristics of a glutamate/N-methyl-D-aspartate receptor

Gary L Aistrup, Marilyn Szentirmay, Keshava N. Kumar, Kent K. Babcock, Richard L. Schowen, Elias K. Michaelis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The functional reconstitution of glutamate receptor proteins purified from mammalian brain has been difficult to accomplish. However, channels activated by L-glutamate (L-Glu) and N-methyl-D-aspartate (NMDA) were detected in planar lipid bilayer membranes (PLMs) following the reconstitution of a complex of proteins with binding sites for NMDA receptor (NMDAR) ligands. The presence of glycine was necessary for optimal activation. A linear current-voltage relationship was observed with the reversal potential being zero. Channels activated by L-Glu had conductances of 23, 47 and 65 pS, and were suppressed partially by competitive and fully by noncompetitive inhibitors of NMDARs. Magnesium had little effect on the reconstituted channels.

Original languageEnglish (US)
Pages (from-to)141-148
Number of pages8
JournalFEBS Letters
Volume394
Issue number2
DOIs
StatePublished - Sep 30 1996

Keywords

  • Glutamate receptor
  • Ion channel reconstitution
  • NMDA activation
  • Planar bilayer membranes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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