Glycine and D-serine increase the affinity of N-methyl-D-aspartate sensitive glutamate binding sites in rat brain synaptic membranes.
In previously frozen and extensively washed brain membranes [3H]glutamate binds to a single population of sites characteristic of the NMDA-sensitive glutamate receptor subtype. This binding cannot be displaced by glycine and D-serine, but actually is enhanced by these amino acids in a dose-dependent manner. Glycine and D-serine increase the affinity of glutamate binding without changing the density of binding sites. These results delineate glycine as an allosteric modulator of the recognition site for the NMDA-sensitive glutamate receptor.
Fadda
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E
Fidia-Georgetown Institute for the Neurosciences, Georgetown University School of Medicine, Washington, D.C. 20007.
Danysz
W
W
Wroblewski
J T
JT
Costa
E
E
D000818:Animals; D001224:Aspartic Acid / Q000031:analogs & derivatives* / Q000494:pharmacology; D001921:Brain / Q000187:drug effects*; D005971:Glutamates; D005998:Glycine / Q000494:pharmacology*; D008297:Male; D016202:N-Methylaspartate; D051381:Rats; D011919:Rats, Inbred Strains; D017470:Receptors, Glutamate; D017981:Receptors, Neurotransmitter / Q000187:drug effects*; D012694:Serine / Q000494:pharmacology*; D013570:Synaptic Membranes / Q000187:drug effects
D005971:Glutamates; D017470:Receptors, Glutamate; D017981:Receptors, Neurotransmitter; D001224:Aspartic Acid; D012694:Serine; D016202:N-Methylaspartate; D005998:Glycine