Binding sites for [3H]glutamate and [3H]aspartate in human cerebellum.

Article date: 1986/11/1

PubMed ID: 2876054

Journal name: Journal of neurochemistry (ISSN: 0022-3042)


The binding of [3H]aspartate and [3H]glutamate to membranes prepared from frozen human cerebellar cortex was studied. The binding sites differed in their relative proportions, their inhibition by amino acids and analogues, and by the effects of cations. A proportion (about 30%) of [3H]glutamate binding was to sites similar to those labelled by [3H]aspartate. An additional component of [3H]glutamate binding (about 50%) was displaced by quisqualate and alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid, and may represent a “quisqualate-preferring” receptor. Neither N-methyl-D-aspartic acid-sensitive nor DL-2-amino-4-phosphonobutyric acid-sensitive [3H]glutamate binding was detected.

Author List: Cross A, Skan W, Slater P

Publication Types: Journal Article; Research Support, Non-U.S. Gov't

Substances mentioned in the article: Dicarboxylic Acids; Glutamates; Oxadiazoles; Ibotenic Acid; Aspartic Acid; Glutamic Acid; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid; Quisqualic Acid; N-acetylaspartate; Calcium Chloride;

Mesh terms: Aspartic Acid/analogs & derivatives; Binding Sites; Calcium Chloride/pharmacology; Cerebellum/metabolism; Dicarboxylic Acids/pharmacology; Glutamates/metabolism; Glutamic Acid; Humans; Ibotenic Acid/analogs & derivatives; Oxadiazoles/pharmacology; Quisqualic Acid; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid;

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