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

doi:10.1016/0014-5793(96)00938-6

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

Medicine, Cardiology Division

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	141-148
Number of pages	8
Journal	FEBS Letters
Volume	394
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(96)00938-6
State	Published - 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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title = "Ion channel properties of a protein complex with characteristics of a glutamate/N-methyl-D-aspartate receptor",

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.",

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AU - Aistrup, Gary L

AU - Szentirmay, Marilyn

AU - Kumar, Keshava N.

AU - Babcock, Kent K.

AU - Schowen, Richard L.

AU - Michaelis, Elias K.

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