Glycine modulation of the phencyclidine binding site in mammalian brain.
Neurophysiological studies have shown that glycine potentiates the NMDA response in cultured neurons by a strychnine-insensitive mechanism. Autoradiographic data have demonstrated a correspondence between strychnine-insensitive [3H]glycine binding sites and NMDA-sensitive [3H]glutamate binding sites. Here we report that in synaptic plasma membranes from rat brain, the binding of a PCP analog, [3H]TCP, was enhanced more than 5-fold by 1 microM glycine. This glycine stimulation of binding of [3H]TCP was blocked by the competitive NMDA-receptor antagonist, D-AP7. These data provide support for the hypothesis that a unique amino acid recognition site is associated with the proposed NMDA/PCP receptor complex in brain.
Thomas
J W
JW
Searle Research and Development, G.D. Searle Co., Saint Louis, MO 63198.
Hood
W F
WF
Monahan
J B
JB
Contreras
P C
PC
O'Donohue
T L
TL
D000818:Animals; D001921:Brain / Q000378:metabolism*; D005998:Glycine / Q000494:pharmacology*; D007700:Kinetics; D010622:Phencyclidine / Q000378:metabolism*; D051381:Rats; D017981:Receptors, Neurotransmitter / Q000187:drug effects / Q000378:metabolism*; D017478:Receptors, Phencyclidine; D013570:Synaptic Membranes / Q000378:metabolism
D017981:Receptors, Neurotransmitter; D017478:Receptors, Phencyclidine; D010622:Phencyclidine; D005998:Glycine