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在人工双层膜中重构的AMPA和海人藻酸激活的通道。

AMPA and kainate-operated channels reconstituted in artificial bilayers.

作者信息

Ambrosini A, Barnard E A, Prestipino G

机构信息

Molecular Neurobiology Unit, MRC Centre, Cambridge, UK.

出版信息

FEBS Lett. 1991 Apr 9;281(1-2):27-9. doi: 10.1016/0014-5793(91)80350-c.

Abstract

Cationic channels which can be activated by alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) and kainate play a key role in the generation of excitatory postsynaptic potentials in the brain of all vertebrates. On a protein carrying binding sites for both these ligands, affinity-purified from the Xenopus nervous system, electrical measurements have been performed to investigate its functional properties after the pure complex had been incorporated into planar lipid bilayers. Domoate, AMPA or kainate added to the reconstituted protein activated cationic channels, which were blocked by typical antagonists for this neurotransmitter system. These data suggest that the reconstituted protein is an ionotropic receptor of the unitary non-NMDA subtype.

摘要

可被α-氨基-3-羟基-5-甲基异恶唑-4-丙酸(AMPA)和海人酸激活的阳离子通道在所有脊椎动物大脑兴奋性突触后电位的产生中起关键作用。从非洲爪蟾神经系统中亲和纯化出一种携带这两种配体结合位点的蛋白质,在将纯复合物整合到平面脂质双分子层后,进行了电学测量以研究其功能特性。添加到重组蛋白中的软骨藻酸、AMPA或海人酸激活了阳离子通道,这些通道被该神经递质系统的典型拮抗剂阻断。这些数据表明,重组蛋白是单一非NMDA亚型的离子型受体。

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