IR@PKUHSC  > 北京大学药学院
学科主题药学
Divalent cations potentiate TRPV1 channel by lowering the heat activation threshold
Cao, Xu1,2; Ma, Linlin2,3; Yang, Fan2; Wang, KeWei1,4; Zheng, Jie2
刊名JOURNAL OF GENERAL PHYSIOLOGY
2014
DOI10.1085/jgp.201311025
143期:1页:75-90
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Physiology
研究领域[WOS]Physiology
关键词[WOS]CAPSAICIN RECEPTOR TRPV1 ; EXTERNAL PROTONATION SITES ; 2 INACTIVATION MECHANISMS ; ROOT GANGLION NEURONS ; POTASSIUM CHANNELS ; ION-CHANNEL ; K+ CHANNEL ; VANILLOID RECEPTOR-1 ; PROTEIN-KINASE ; PORE TURRET
英文摘要

Transient receptor potential vanilloid type 1 (TRPV1) channel responds to a wide spectrum of physical and chemical stimuli. In doing so, it serves as a polymodal cellular sensor for temperature change and pain. Many chemicals are known to strongly potentiate TRPV1 activation, though how this is achieved remains unclear. In this study we investigated the molecular mechanism underlying the gating effects of divalent cations Mg2+ and Ba2+. Using a combination of fluorescence imaging and patch-clamp analysis, we found that these cations potentiate TRPV1 gating by most likely promoting the heat activation process. Mg2+ substantially lowers the activation threshold temperature; as a result, a significant fraction of channels are heat-activated at room temperature. Although Mg2+ also potentiates capsaicin- nd voltage-dependent activation, these processes were found either to be not required (in the case of capsaicin) or insufficient (in the case of voltage) to mediate the activating effect. In support of a selective effect on heat activation, Mg2+ and Ba2+ cause a Ca2+-independent desensitization that specifically prevents heat-induced channel activation but does not prevent capsaicin-induced activation. These results can be satisfactorily explained within an allosteric gating framework in which divalent cations strongly promote the heat-dependent conformational change or its coupling to channel activation, which is further coupled to the voltage-and capsaicin-dependent processes.

语种英语
WOS记录号WOS:000329129800011
项目编号R01NS072377 ; B07001 ; 2013CB531302 ; 81221002 ; APP1035102 ; 10PRE4170142
资助机构National Institutes of Health ; UC Davis Health System Research Award ; Ministry of Education of China 111 Project ; Ministry of Science and Technology of China ; National Science Foundation of China ; Australian National Health and Medical Research Council fellowship ; American Heart Association predoctoral fellowship
引用统计
被引频次:17[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/63656
专题北京大学药学院
北京大学药学院_分子与细胞药理学系
作者单位1.Peking Univ, Sch Pharmaceut Sci, Dept Mol & Cellular Pharmacol, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
2.Univ Calif Davis, Sch Med, Dept Physiol & Membrane Biol, Davis, CA 95616 USA
3.Univ Queensland, Inst Mol Biosci, St Lucia, Qld 4072, Australia
4.Peking Univ, IDG McGovern Inst Brain Res, Beijing 100871, Peoples R China
推荐引用方式
GB/T 7714
Cao, Xu,Ma, Linlin,Yang, Fan,et al. Divalent cations potentiate TRPV1 channel by lowering the heat activation threshold[J]. JOURNAL OF GENERAL PHYSIOLOGY,2014,143(1):75-90.
APA Cao, Xu,Ma, Linlin,Yang, Fan,Wang, KeWei,&Zheng, Jie.(2014).Divalent cations potentiate TRPV1 channel by lowering the heat activation threshold.JOURNAL OF GENERAL PHYSIOLOGY,143(1),75-90.
MLA Cao, Xu,et al."Divalent cations potentiate TRPV1 channel by lowering the heat activation threshold".JOURNAL OF GENERAL PHYSIOLOGY 143.1(2014):75-90.
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Cao, Xu]的文章
[Ma, Linlin]的文章
[Yang, Fan]的文章
百度学术
百度学术中相似的文章
[Cao, Xu]的文章
[Ma, Linlin]的文章
[Yang, Fan]的文章
必应学术
必应学术中相似的文章
[Cao, Xu]的文章
[Ma, Linlin]的文章
[Yang, Fan]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。