Trans-ACPD, a selective agonist of the phosphoinositide-coupled excitatory amino acid receptor.
Trans-ACPD, a selective agonist of the phosphoinositide-coupled excitatory amino acid receptor.
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Trans-ACPD，磷酸肌醇偶联兴奋性氨基酸受体的选择性激动剂。
DOI：
10.1016/0014-2999(89)90383-x
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发表时间：
1989
影响因子：
5
通讯作者：
Cotman,CW
中科院分区：
文献类型：
--
作者：
Palmer,E;Monaghan,DT;Cotman,CW
兴奋性氨基酸(EAA)被认为通过至少五种受体亚型介导其作用。其中四种类型似乎是门控离子通道，并被命名为选择性激活它们的激动剂：N-甲基-D-天冬氨酸(N-甲基-D-天冬氨酸)、红藻氨酸(KA)、a-amino-3-hydroxy-5-methylisoxazole-4-propionlc酸(AMPA)、奎斯奎宁和2-氨基-4-膦酸丁酸酯(AP4)。现在有令人信服的证据来自对磷脂酰肌醇(PI)代谢的研究，表明存在第五种不同的EAA受体类别(参考Monaghan等人，1989)。在注射核糖核酸的卵母细胞和大鼠海马片上，谷氨酸、鹅膏和蛋氨酸均能激活PI代谢。这似乎代表了一个不同的受体类别，因为TINS位点不被N-甲基-D-天冬氨酸、红藻氨酸、AMPA或L-AP4激活，也不被它们的拮抗剂阻断。到目前为止，由于缺乏选择性激动剂，PI偶联的EAA受体的药理分析受到阻碍。这给该受体的表征带来了一个特殊的问题，因为同时激活其他EAA受体(NMDA、海人藻酸或AMPA)以及PI偶联受体可以抑制随后的PI代谢(Palmer等人，1988年)。在这项研究中，我们报告了谷氨酸类似物
Excitatory amino acids (EAA) are thought to mediate their actions through at least five receptor subtypes. Four of these types appear to gate ion channels and have been named for agonists by which they are selectively activated: N-methyl-D-aspartate (NMDA), kainate, a-amino-3-hydroxy-5-methylisoxazole-4-propionlc acid (AMPA), quisqualate and 2-amino-4-phosphonobutyrate (AP4). There is now compelling evidence from studies of phospholnositlde (PI) metabolism indicating that there is a fifth distinct EAA receptor class (for references see Monaghan et al., 1989). In both mRNA-injected oocytes and rat Inppocampal slices PI metabolism is activated by L-glutamate, ibotenate and quisqualate. This appears to represent a distinct receptor class because tins site is not activated by NMDA, kainate, AMPA or L-AP4, nor is it blocked by their antagonists.To date, pharmacological analysis of the PI-coupled EAA receptor has been hampered by the absence of a selective agonist. This presents a particular problem for the characterization of this receptor because simultaneous activation of the other EAA receptors (NMDA, kainate or AMPA) along with the PI-coupled receptor can inhibit subsequent PI metabohsm (Palmer et al., 1988). In this study, we report that the glutamate analogue