Subunit- and site-specific pharmacology of the NMDA receptor channel

@article{Yamakura1999SubunitAS,
  title={Subunit- and site-specific pharmacology of the NMDA receptor channel},
  author={Tomohiro Yamakura and Koki Shimoji},
  journal={Progress in Neurobiology},
  year={1999},
  volume={59},
  pages={279-298}
}
NMDA receptor subunits: function and pharmacology.
NMDA Receptor Subunits: Function and Pharmacology
Physiology and pathology of NMDA receptors.
TLDR
The aim of this review is to summarize the recent data about the structural and functional properties of NMDA receptors and their role in long-term potentiation and excitotoxicity.
NMDA-gated ion channel research and its therapeutic potentials in neurodegenerative diseases: a review
TLDR
Open-channel blockers with uncompetitive antagonism and drugs modulating NMDAR activities are appealing therapeutic strategies because, in theory, these properties could decrease neurotoxicity due to excessive levels of glutamate while sparing physiological neurotransmission.
Imaging the PCP site of the NMDA ion channel.
  • R. Waterhouse
  • Biology, Psychology
    Nuclear medicine and biology
  • 2003
TLDR
Progress made towards the development of radiolabeled agents for PCP sites of the NMDA ion channel is outlined and the animal and pharmacological models used for in vitro and in vivo assessment of NMDA receptor targeted agents are discussed.
Molecular basis of NMDA receptor functional diversity
  • P. Paoletti
  • Biology
    The European journal of neuroscience
  • 2011
TLDR
This review gives an overview of the current knowledge of the molecular basis underlying NMDAR functional heterogeneity and presents recent studies revealing the central, and largely unsuspected, role of the extracellular N‐terminal region in generating functional diversity of N MDARs.
Imaging the PCP site of the NMDA ion channel.
Haloperidol regulates the binding of guanine nucleotides to synaptic membranes through the NMDA receptor
TLDR
It has been found that haloperidol, a therapeutically useful antipsychotic drug, inhibits neuronal NMDA responses and has neuroprotective effects against NMDA-induced neurotoxicity, and results from Whittemore et al. suggest that a noncompetitive allosteric modulator site expressed by isoforms of the receptor containing the NR1/NR2B subunit mediates hal operidol’s action on the NMDA receptor.
Principles of N-Methyl-d-aspartate Receptor Allosteric Modulation
TLDR
A detailed mechanistic characterization of NMDA receptor allosteric effectors may identify function-specific modulators and provides a road map for the development of combinatorial strategies for local, transient tuning of specific receptor functions.
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References

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Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs
TLDR
The identification and primary structure of a novel mouse NMDA receptor channel subunit, designated as ɛl, is reported, which shows 11-18% amino-acid sequence identity with rodent GluR channel subunits that have been characterized so far and has structural features common to neurotransmitter-gated ion channels.
Identification by mutagenesis of a Mg2+ -block site of the NMDA receptor channel
TLDR
It is suggested that the conserved asparagine residue in segment M2 constitutes a Mg2+-block site of the NMDA receptor channel, and that the MK-801 site overlaps the Mg 2+ site.
Differential Tyrosine Phosphorylation of N-Methyl-D-aspartate Receptor Subunits (*)
TLDR
Immunocytochemical staining with an anti-phosphotyrosine antibody demonstrates that there are high levels of phosphotYrosine, which co-localizes with glutamate receptors at excitatory synapses on cultured hippocampal neurons and suggests that tyrosine phosphorylation of the NR2 subunits may be important for regulating NMDA receptor function.
Heteromeric NMDA Receptors: Molecular and Functional Distinction of Subtypes
TLDR
Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% ientical in sequence, and these are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor sub Units.
Molecular diversity of the NMDA receptor channel
TLDR
Findings suggest that the molecular diversity of the ɛ subunit family underlies the functional heterogeneity of the NMDA receptor channel.
Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine
TLDR
Using a fast perfusion system, glycine regulates desensitization at NMDA receptors; this has a major effect on the response to NMDA measured at equilibrium, as would occur with slower applications of agonist.
Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
TLDR
Direct evidence is presented that NMDA receptors exist in rat neocortex as heteromeric complexes of considerable heterogeneity, some containing both NR2A and NR2B subunits.
Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain
TLDR
Examination of the phosphorylation of the NMDA receptor subunit NMDAR1 (NR1) by protein kinase C (PKC) in cells transiently expressing recombinant NR1 and in primary cultures of cortical neurons provides evidence that the C-terminal domain of the NR1 protein is located intracellularly, suggesting that the proposed transmembrane topology model for glutamate receptors may be incorrect.
Modification of NMDA Receptor Channels and Synaptic Transmission by Targeted Disruption of the NR2C Gene
TLDR
It is concluded that the NR2C subunit contributes to functional heteromeric NMDA receptor-subunit assemblies at the mossy fiber synapse and extrasynaptic sites during maturation, and the conductance level exhibited by a given receptor macromolecule may reflect the stochiometry of subunit composition.
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