Chang Huai-Ren, Kuo Chung-Chin
Department of Physiology, National Taiwan University College of Medicine.
Biophys J. 2007 Sep 15;93(6):1981-92. doi: 10.1529/biophysj.106.103176. Epub 2007 May 18.
Felbamate (FBM) is a potent nonsedative anticonvulsant whose clinical effect is chiefly related to gating modification (and thus use-dependent inhibition) rather than pore block of N-methyl-D-aspartate (NMDA) channels at pH 7.4. Using whole-cell recording in rat hippocampal neurons, we examined the effect of extracellular pH on FBM action. In sharp contrast to the findings at pH 7.4, the inhibitory effect of FBM on NMDA currents shows much weakened use-dependence at pH 8.4. Moreover, FBM neither accelerates the activation kinetics of the NMDA channel, nor enhances the currents elicited by very low concentrations of NMDA at pH 8.4. These differential effects of FBM between pH 7.4 and 8.4 are abolished in the mutant NMDA channels which lack proton sensitivity. Most interestingly, the inhibitory effect of FBM becomes flow-dependent and is evidently stronger in inward than in outward NMDA currents at pH 8.4. These findings indicate that FBM has a significantly more manifest pore-blocking effect on the NMDA channel at pH 8.4 than at pH 7.4. FBM therefore acts as an opportunistic pore blocker modulated by extracellular proton, suggesting that the FBM binding site is located at the junction of a widened and a narrow part of the ion conduction pathway. Also, we find that the inhibitory effect of FBM on NMDA currents is antagonized by external but not internal Na+, and that increase of external Na+ decreases the binding rate without altering the unbinding rate of FBM. These findings indicate that the FBM binding site faces the extracellular rather than the intracellular solution, and coincides with the outmost ionic (e.g., Na+) site in the NMDA channel pore. We conclude that the FBM binding site very likely is located in the external pore mouth, where extracellular proton, Na+, FBM, and NMDA channel gating have an orchestrating effect.
非氨酯(FBM)是一种强效非镇静性抗惊厥药,其临床效果主要与门控修饰(以及因此的使用依赖性抑制)有关,而非在pH 7.4时对N-甲基-D-天冬氨酸(NMDA)通道的孔道阻断作用。我们使用大鼠海马神经元的全细胞记录,研究了细胞外pH对FBM作用的影响。与在pH 7.4时的发现形成鲜明对比的是,FBM在pH 8.4时对NMDA电流的抑制作用显示出明显减弱的使用依赖性。此外,在pH 8.4时,FBM既不加速NMDA通道的激活动力学,也不增强极低浓度NMDA引发的电流。在缺乏质子敏感性的突变型NMDA通道中,FBM在pH 7.4和8.4之间的这些差异效应消失了。最有趣的是,在pH 8.4时,FBM的抑制作用变得与电流方向有关,并且向内的NMDA电流中的抑制作用明显强于向外的NMDA电流。这些发现表明,与pH 7.4相比,FBM在pH 8.4时对NMDA通道具有明显更显著的孔道阻断作用。因此,FBM作为一种受细胞外质子调节的机会性孔道阻断剂,这表明FBM结合位点位于离子传导途径的宽部和窄部的交界处。此外,我们发现FBM对NMDA电流的抑制作用受到细胞外而非细胞内Na +的拮抗,并且细胞外Na +的增加会降低结合速率,而不会改变FBM的解离速率。这些发现表明,FBM结合位点面向细胞外溶液而非细胞内溶液,并且与NMDA通道孔道中最外层的离子(例如Na +)位点重合。我们得出结论,FBM结合位点很可能位于外部孔口,在那里细胞外质子、Na +、FBM和NMDA通道门控具有协同作用。