Article date: 1989/11/1
PubMed ID: 2577369
Journal name: The New biologist (ISSN: 1043-4674)
The kainate (KA) and the quisqualate (QUIS) receptors that activate cation channels in the central nervous system have previously been defined as two of the major glutamate receptor types. In amphibian brain, an exceptionally rich source of these sites, they can be coextracted by octylglucoside and shown to behave as one entity in all analyses made in solution. When partly purified by lectin affinity, ion-exchange chromatography or by sucrose gradient centrifugation, the two activities comigrate in a 1:1 ratio. When the QUIS component is bound to an immobilized specific QUIS agonist, the KA component is extracted in parallel with it. There are equivalent numbers of the QUIS and KA sites and the two sites show a single affinity series for the binding of glutamatergic agonists. We deduce that KA or QUIS select different conformations of a single KA/QUIS receptor binding site, leading thus to the different channel-opening events that have been reported for these two agonists.
Author List: Henley J M, Ambrosini A, Krogsgaard-Larsen P, Barnard E A
Publication Types: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
Substances mentioned in the article: Quinoxalines; Receptors, AMPA; Receptors, Glutamate; Receptors, Kainic Acid; Receptors, Neurotransmitter; Ibotenic Acid; 6-Cyano-7-nitroquinoxaline-2,3-dione; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid; Quisqualic Acid; Kainic Acid;
Mesh terms: 6-Cyano-7-nitroquinoxaline-2,3-dione; Animals; Brain Chemistry; Ibotenic Acid/analogs & derivatives; Ion Channel Gating/drug effects; Kainic Acid/metabolism; Kinetics; Protein Conformation; Quinoxalines/pharmacology; Quisqualic Acid/metabolism; Receptors, AMPA; Receptors, Glutamate; Receptors, Kainic Acid; Receptors, Neurotransmitter/classification; Xenopus laevis; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid;