Cited by 173Neuroscience and Neuropharmacology ResearchAmino Acid Enzymes and MetabolismNicotinic Acetylcholine Receptors Study

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N-methyl-D-aspartate receptors: different subunit requirements for binding of glutamate antagonists, glycine antagonists, and channel-blocking agents

Lynch, D R, Anegawa, N J, Verdoorn, T, Pritchett, D B·1994·Molecular Pharmacology

DOI 10.1016/s0026-895x(25)10028-x

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Abstract

Expression of the NR-1 subunit in Xenopus oocytes produces channels that respond to glutamate and are blocked by competitive and noncompetitive antagonists of the N-methyl-D-aspartate (NMDA) receptor. Ionic conductances through these channels are increased by coexpression with NR-2 receptor subunits. We have characterized the pharmacological properties of NMDA receptors assembled from combinations of subunits expressed in transfected cells, to determine the minimum subunit requirements for binding of competitive glutamate antagonists, glycine antagonists, and channel-blocking agents, as detected by ligand-binding experiments. Expression of NR-1a alone produced glycine antagonist binding, whereas the combination of NR-1a and NR-2A was needed to produce binding sites for glutamate antagonists and channel-blocking agents. These results suggest that functional NMDA receptors assemble from these subunits. However, differences in the pharmacological effects of NMDA and polyamines show that not all characteristics of native NMDA receptors are reproduced by this combination of subunits.

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Authors: Lynch, D. R., Anegawa, N. J., Verdoorn, T., & Pritchett, D. B.
Affiliations: University of Pennsylvania (US)
ORCID: Lynch, D R
Verdoorn, T
Venue: Molecular Pharmacology
Publisher: Elsevier BV
Published: 1994-03
Volume: 45
Issue: 3
Pages: 540-545
ISSN: 0026-895X (ISSN-L)
DOI: 10.1016/s0026-895x(25)10028-x
OpenAlex: W1839333079
Cited by: 173
References: 19
Citations by year: 2025: 2 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 4 · 2014: 2 · 2013: 4 · 2012: 1
FWCI: 4.78
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Molecular Pharmacology (publishedVersion)
PubMed (publishedVersion)
PubMed
Funders: National Institutes of Health (5r01da007130-08)
National Institute on Drug Abuse (DA 07130-02)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
Keywords: NMDA receptor, NR1 subunit, NR2A subunit, subunit assembly, glutamate receptor antagonists, glycine antagonist, ligand binding, polyamines, competitive antagonism, non-competitive antagonism, ion channel pharmacology
MeSH terms: Binding Sites, Cells, Cultured, Glutamates, Glycine, Humans, Ion Channels, Kynurenic Acid, Transfection, Receptors, N-Methyl-D-Aspartate, Dizocilpine Maleate, Excitatory Amino Acid Antagonists, Glutamic Acid

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N-methyl-D-aspartate receptors: different subunit requirements for binding of glutamate antagonists, glycine antagonists, and channel-blocking agents

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