Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes

Draguhn, Andreas; Jahn, Werner; Witzemann, Veit

doi:10.1016/0304-3940(91)90298-8 Get

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Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes

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Draguhn, Andreas
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Jahn, Werner
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Witzemann, Veit
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society;
Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0304394091902988/pdf?md5=868b9e106c6deafd15c46464c784ade3&pid=1-s2.0-0304394091902988-main.pdf
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https://doi.org/10.1016/0304-3940(91)90298-8
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引用

Draguhn, A., Jahn, W., & Witzemann, V. (1991). Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes. Neuroscience Letters, 132(2), 187-190. doi:10.1016/0304-3940(91)90298-8 Get.

引用: https://hdl.handle.net/11858/00-001M-0000-0019-AC75-A

要旨

Argiotoxin636, a component of the spider venom of argiope species, was chemically synthesized together with a number of derivatives in order to analyse their blocking activity on mammalian glutamate receptors. Xenopus laevis oocytes injected with rat brain mRNA served as assay system. The results showed that argiotoxin636 had a higher affinity for N-methyl-D-aspartate (NMDA) than for kainate receptors, blocking the corresponding ion channels in a voltage-dependent manner. Modifications of the polyamine tail or the terminal arginine residue strongly reduced the blocking potency. The iodinated monohydroxyl phenylderivatives, however, retained their NMDA-selective binding and could serve as non-competitive antagonists for radioligand binding assays aiding in the biochemical isolation of glutamate receptors.