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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10.1016/0014-5793(96)00938-6

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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.",

keywords = "Glutamate receptor, Ion channel reconstitution, NMDA activation, Planar bilayer membranes",

author = "Aistrup, {Gary L.} and Marilyn Szentirmay and Kumar, {Keshava N.} and Babcock, {Kent K.} and Schowen, {Richard L.} and Michaelis, {Elias K.}",

note = "Funding Information: Acknowledgements: This work was supported by Grants AA 04732 from NIAAA and DAAL03-91-G-00167 from the ARO, AG 12993 from the NIA, and by the Center for Neurobiology and Immunology Research.",

year = "1996",

month = sep,

day = "30",

doi = "10.1016/0014-5793(96)00938-6",

language = "English (US)",

volume = "394",

pages = "141--148",

journal = "FEBS Letters",

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T1 - Ion channel properties of a protein complex with characteristics of a glutamate/N-methyl-D-aspartate receptor

AU - Aistrup, Gary L.

AU - Szentirmay, Marilyn

AU - Kumar, Keshava N.

AU - Babcock, Kent K.

AU - Schowen, Richard L.

AU - Michaelis, Elias K.

N1 - Funding Information: Acknowledgements: This work was supported by Grants AA 04732 from NIAAA and DAAL03-91-G-00167 from the ARO, AG 12993 from the NIA, and by the Center for Neurobiology and Immunology Research.

PY - 1996/9/30

Y1 - 1996/9/30

N2 - 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.

AB - 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.

KW - Glutamate receptor

KW - Ion channel reconstitution

KW - NMDA activation

KW - Planar bilayer membranes

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JO - FEBS Letters

JF - FEBS Letters

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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