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学科主题基础医学
Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations
Cui, Yuanyuan1,3; Yang, Fan1,2; Cao, Xu1,3; Yarov-Yarovoy, Vladimir1; Wang, KeWei3; Zheng, Jie1
刊名JOURNAL OF GENERAL PHYSIOLOGY
2012-04-01
DOI10.1085/jgp.201110724
139期:4页:273-283
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]SPECIES-SPECIFIC SENSITIVITY ; RECEPTOR POTENTIAL CHANNELS ; 2 INACTIVATION MECHANISMS ; K+ CHANNEL ; POTASSIUM CHANNELS ; ION-CHANNEL ; CHEMICAL STIMULI ; COLD RECEPTOR ; VOLTAGE ; DOMAIN
英文摘要

The capsaicin receptor transient receptor potential vanilloid (TRPV) 1 is a highly heat-sensitive ion channel. Although chemical activation and heat activation of TRPV1 elicit similar pungent, painful sensation, the molecular mechanism underlying synergistic activation remains mysterious. In particular, where the temperature sensor is located and whether heat and capsaicin share a common activation pathway are debated. To address these fundamental issues, we searched for channel mutations that selectively affected one form of activation. We found that deletion of the first 10 amino acids of the pore turret significantly reduced the heat response amplitude and shifted the heat activation threshold, whereas capsaicin activation remained unchanged. Removing larger portions of the turret disrupted channel function. Introducing an artificial sequence to replace the deleted region restored sensitive capsaicin activation in these nonfunctional channels. The heat activation, however, remained significantly impaired, with the current exhibiting diminishing heat sensitivity to a level indistinguishable from that of a voltage-gated potassium channel, Kv7.4. Our results demonstrate that heat and capsaicin activation of TRPV1 are structurally and mechanistically distinct processes, and the pore turret is an indispensible channel structure involved in the heat activation process but is not part of the capsaicin activation pathway. Synergistic effect of heat and capsaicin on TRPV1 activation may originate from convergence of the two pathways on a common activation gate.

语种英语
WOS记录号WOS:000302713600002
项目编号R01NS072377 ; 30970919 ; B07001
资助机构National Institutes of Health ; UC Davis Health System Research Award ; National Science Foundation of China ; Ministry of Education of China ; American Heart Association
引用统计
被引频次:41[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/52271
专题北京大学基础医学院_神经生物学系
北京大学药学院_分子与细胞药理学系
作者单位1.Univ Calif Davis, Dept Physiol & Membrane Biol, Sch Med, Davis, CA 95616 USA
2.Univ Calif Davis, Mol Cellular & Integrat Physiol Grad Grp, Davis, CA 95616 USA
3.Peking Univ Hlth Sci Ctr, Dept Neurobiol, Neurosci Res Inst, Beijing 100083, Peoples R China
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GB/T 7714
Cui, Yuanyuan,Yang, Fan,Cao, Xu,et al. Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations[J]. JOURNAL OF GENERAL PHYSIOLOGY,2012,139(4):273-283.
APA Cui, Yuanyuan,Yang, Fan,Cao, Xu,Yarov-Yarovoy, Vladimir,Wang, KeWei,&Zheng, Jie.(2012).Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations.JOURNAL OF GENERAL PHYSIOLOGY,139(4),273-283.
MLA Cui, Yuanyuan,et al."Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations".JOURNAL OF GENERAL PHYSIOLOGY 139.4(2012):273-283.
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