Saegusa Hironao, Wakamori Minoru, Matsuda Yoshihiro, Wang Junyang, Mori Yasuo, Zong Shuqin, Tanabe Tsutomu
Department of Pharmacology and Neurobiology, Graduate School of Medicine, Tokyo Medical and Dental University, 1-5-45 Yushima, Tokyo 113-8519, Japan.
Mol Cell Neurosci. 2007 Feb;34(2):261-70. doi: 10.1016/j.mcn.2006.11.006. Epub 2006 Dec 22.
Spinocerebellar ataxia type 6 (SCA6) is caused by polyglutamine expansion in P/Q-type Ca2+ channels (Ca(v)2.1) and is characterized by predominant degeneration of cerebellar Purkinje cells. To characterize the Ca(v)2.1 channel with an SCA6 mutation in cerebellar Purkinje cells, we have generated knock-in mouse models that express human Ca(v)2.1 with 28 polyglutamine repeats (disease range) and with 13 polyglutamine repeats (normal range). Patch-clamp recordings of the Purkinje cells from homozygous control or SCA6 knock-in mice revealed a non-inactivating current that is highly sensitive to a spider toxin omega-Agatoxin IVA, indicating that the human Ca(v)2.1 expressed in Purkinje cells exhibits typical P-type properties in contrast to the previous data showing Q-type properties, when it was expressed in cultured cell lines. Furthermore, the voltage dependence of activation and inactivation and current density were not different between SCA6 and control, though these properties were altered in previous reports using non-neuronal cells as expression systems. Therefore, our results do not support the notion that the alteration of the channel properties may underlie the pathogenic mechanism of SCA6.
6型脊髓小脑共济失调(SCA6)由P/Q型Ca2+通道(Ca(v)2.1)中的多聚谷氨酰胺扩增引起,其特征是小脑浦肯野细胞的主要退化。为了在小脑浦肯野细胞中表征具有SCA6突变的Ca(v)2.1通道,我们构建了基因敲入小鼠模型,该模型表达具有28个多聚谷氨酰胺重复序列(疾病范围)和13个多聚谷氨酰胺重复序列(正常范围)的人Ca(v)2.1。对来自纯合对照或SCA6基因敲入小鼠的浦肯野细胞进行膜片钳记录,发现一种对蜘蛛毒素ω-芋螺毒素IVA高度敏感的非失活电流,这表明在浦肯野细胞中表达的人Ca(v)2.1表现出典型的P型特性,这与之前在培养细胞系中表达时显示Q型特性的数据形成对比。此外,SCA6和对照之间的激活和失活的电压依赖性以及电流密度没有差异,尽管在之前使用非神经元细胞作为表达系统的报告中这些特性发生了改变。因此,我们的结果不支持通道特性改变可能是SCA6致病机制基础这一观点。