Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin

作     者：Chuang, RSI Jaffe, H Cribbs, L Perez-Reyes, E Swartz, KJ 

作者机构：NINDS Mol Physiol & Biophys Unit NIH Bethesda MD 20892 USA NINDS Prot Peptide Sequencing Facil NIH Bethesda MD 20892 USA Loyola Univ Med Ctr Dept Physiol Maywood IL 60153 USA 

出 版 物：《NATURE NEUROSCIENCE》 (自然神经科学)

年 卷 期：1998年第1卷第8期

页      面：668-674页

核心收录：

学科分类：0710[理学-生物学] 1001[医学-基础医学(可授医学、理学学位)] 07[理学] 071003[理学-生理学] 

基　　金：Intramural NIH HHS [ZIA NS002945-13] Funding Source: Medline 

主　　题：结合 竞争性/生理学 钙通道/药物作用 钙通道/代谢 钙通道 T型 电生理学 离子通道闸门/药物作用 离子通道闸门/生理学 神经毒素类/代谢 神经毒素类/药理学 卵母细胞/代谢 蝎毒液类/代谢 蝎毒液类/药理学 钠通道/药物作用 钠通道/代谢 光滑爪蟾 动物 女(雌)性 

摘      要：The biophysical properties of T-type voltage-gated calcium channels are well suited to pacemaking and to supporting calcium flux near the resting membrane potential in both excitable and nonexcitable cells. We have identified a new scorpion toxin (kurtoxin) that binds to the alpha(1G) T-type calcium channel with high affinity and inhibits the channel by modifying voltage-dependent gating. This toxin distinguishes between alpha(1G) T-type calcium channels and other types of voltage-gated calcium channels, including alpha(1A), alpha(1B), alpha(1C) and alpha(1E). Like the other alpha-scorpion toxins to which it is related, kurtoxin also interacts with voltage-gated sodium channels and slows their inactivation. Kurtoxin will facilitate characterization of the subunit composition of T-type calcium channels and help determine their involvement in electrical and biochemical signaling.