Article date: 1990/12/10
PubMed ID: 2176160
Journal name: FEBS letters (ISSN: 0014-5793)
Antibodies were made to a thirteen amino acid synthetic peptide corresponding to the C-terminal portion of the glutamate (glu) receptor, GluR-A. The immunoprecipitation of kainic acid (KA) and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) binding sites by the anti-peptide antibodies was studied using a detergent-solubilized preparation of rat brain membranes. Under these conditions a subpopulation of AMPA binding sites was recognized by the antibodies, but no KA binding sites were recognized. Scatchard analysis of this subpopulation of AMPA binding sites yields a curvilinear plot which fits a two-site model with dissociation constants of 4.6 and 323 nM. These studies show that the glu receptor complex, GluR-A, binds AMPA but not KA and suggest that (i) the binding sites for these two ligands reside on different proteins, and (ii) the KA receptor identified physiologically is not equivalent to the KA binding sites identified with 3H-labelled KA.
Author List: Wenthold R J, Hunter C, Wada K, Dechesne C J
Publication Types: Journal Article
Substances mentioned in the article: Antibodies; Glutamates; Peptide Fragments; Peptides; Receptors, Glutamate; Receptors, Neurotransmitter; Ibotenic Acid; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid; Kainic Acid;
Mesh terms: Amino Acid Sequence; Animals; Antibodies; Binding Sites; Binding, Competitive; Brain/metabolism; Cell Membrane/metabolism; Glutamates/metabolism; Ibotenic Acid/analogs & derivatives; Kainic Acid/metabolism; Kinetics; Molecular Sequence Data; Peptide Fragments/isolation & purification; Peptides/chemical synthesis; Rats; Receptors, Glutamate; Receptors, Neurotransmitter/immunology; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid;