The Binding of [3H]AMPA, a Structural Analogue of Glutamic Acid, to Rat Brain Membranes
The Binding of [3H]AMPA, a Structural Analogue of Glutamic Acid, to Rat Brain Membranes
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谷氨酸结构类似物 [3H]AMPA 与大鼠脑膜的结合
DOI：
10.1111/j.1471-4159.1982.tb10868.x
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发表时间：
1982
影响因子：
4.7
通讯作者：
P. Krogsgaard‐Larsen
中科院分区：
文献类型：
--
作者：
T. Honoré;J. Lauridsen;P. Krogsgaard‐Larsen
翻译后摘要：结合[3H] AMPA大鼠脑细胞膜进行了研究。结合在生理pH下是可饱和的和可逆的。结合数据的计算机辅助Scatchard分析（通过使用l-谷氨酸（l-GLU）确定非特异性结合）表明存在两个独立的结合位点，KD分别为9和2440 nm。额外的冷冻、解冻和洗涤序列得到仅具有一个结合位点的膜，KD为278 nm。[3H] AMPA结合在纹状体膜中表现出最高的b水平。测试了一系列GLU和天冬氨酸（ASP）类似物作为[3 H] AMPA结合抑制剂。主要与N-甲基-d-天冬氨酸（NMDA）受体位点相互作用的l-ASP和化合物作为[3H] AMPA结合抑制剂无活性，而主要与谷氨酸二乙酯受体位点相互作用的l-GLU和化合物是具有与体内兴奋作用所示相同效力顺序的抑制剂。结果提示[~3H] AMPA可能与兴奋性GLU受体结合。
Abstract: Binding of [3H]AMPA to rat brain membranes was investigated. The binding was saturable and reversible at physiological pH. Computer‐aided Scatchard analysis of the binding data, as determined by using l‐glutamic acid (l‐GLU) to define nonspecific binding, suggested the presence of two independent binding sites, with KDs of 9 and 2440 nm, respectively. Additional freezing, thawing and washing sequences gave membranes with only one binding site, with a KD of 278 nm. [3H]AMPA binding exhibited the highest blevel in striatal membranes. A series of analogues of GLU and aspartic acid (ASP) were tested as inhibitors of [3H]AMPA binding. l‐ASP and compounds which interact predominantly with N‐methyl‐d‐aspartic acid (NMDA) receptor sites were inactive as inhibitors of [3H]AMPA binding, whereas l‐GLU and compounds which interact predominantly with glutamic acid diethyl ester receptor sites were inhibitors with the same order of potency as that shown by the excitatory action in vivo. The result suggests that [3H]AMPA might represent binding to an excitatory GLU receptor.