Glycine‐Like Modulation of N‐Methyl‐d‐Aspartate Receptors by a Monoclonal Antibody That Enhances Long‐Term Potentiation

@article{Haring1991GlycineLikeMO,
  title={Glycine‐Like Modulation of N‐Methyl‐d‐Aspartate Receptors by a Monoclonal Antibody That Enhances Long‐Term Potentiation},
  author={Rachel Haring and Patric K. Stanton and Mark A. Scheideler and J. R. Moskal},
  journal={Journal of Neurochemistry},
  year={1991},
  volume={57}
}
Abstract: We have identified a monoclonal antibody, B6 B21, that significantly elevates long‐term potentiation when applied to CA1 pyramidal cell apical dendrites in rat hippocampal slices and characterized its binding to N‐methyl‐d‐aspartate‐receptor complexes using extensively washed hippocampal membranes. Five micrograms of affinity‐purified B6B21 per 100 μg of membranes gave a two‐to threefold elevation in N‐[1‐(2‐thienyl)cyclohexyl]‐3,4‐[3H]piperidine ([3H]TCP) binding. When [3H]TCP… 
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ZK200775: a phosphonate quinoxalinedione AMPA antagonist for neuroprotection in stroke and trauma.
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  • Chemistry, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 1998
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The results show that simultaneous occupancy of the glycine and the glutamate sites of the NMDA receptor is essential for their functional activation, and support two concepts suggested by previous electrophysiological experiments.
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The data suggest that [3H]MK‐801 labels a high‐affinity site on the NMDA receptor channel complex, distinct from theNMDA recognition site, which is responsible for the blocking action of MK‐801 and other noncompetitive NMda receptor antagonists.
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TLDR
It is reported here that rat brain synaptic plasma membranes contain a distinct population of L-[3H]glutamate binding sites with pharmacological properties indicative of the N-Me-D-Asp receptor, and showed that regions in rodent and primate brain that are especially sensitive to anoxic and excitotoxic neuronal damage have a high level of N- me-D -Asp sites.
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