L-glutamate receptor heterogeneity: labeling of distinct receptor sub-types using radioligand binding techniques.
This study demonstrates (1) that L-[3H]glutamate labels 3 distinct binding sites (types A1, A2 and A4) in isolated rat brain membranes and (2) that only the N-methyl-aspartate (A1) and quisqualate (A2) receptor classes are associated with the postsynaptic density (PSD). L-[3H]glutamate bound to PSDs with Kd 339 nM and Bmax 6 X 1 pmol/mg protein. These sites were resolved into 2 distinct sub-types on the basis of inhibition studies. N-Methyl-aspartate maximally inhibited 57% of PSD-located L-glutamate binding sites (the A1 site) and quisqualate 43% (the A2 site); the effects of both substances were additive. The ligand selectivities of these 2 sites indicated their identity with the N-methyl-D-aspartate and quisqualate receptor classes defined electrophysiologically. The C1--dependent population of L-glutamate binding sites (the A4 site) which predominates in synaptic membranes was absent from PSDs.
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D011869:Radioligand Assay; D051381:Rats; D017470:Receptors, Glutamate; D017981:Receptors, Neurotransmitter / Q000378:metabolism*; D013570:Synaptic Membranes / Q000378:metabolism
D005971:Glutamates; D017470:Receptors, Glutamate; D017981:Receptors, Neurotransmitter