TRPV1 splice variants: structure and function.

TRPV1 splice variants: structure and function.
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DOI:
10.2741/3651
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发表时间:
2010-06-01
期刊:
Frontiers in bioscience (Landmark edition)
影响因子:
--
通讯作者:
Eilers H
Eilers H
中科院分区:
其他
文献类型:
--
作者:
Schumacher MA;Eilers H

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辣椒素受体(TRPV1)是一种非选择性阳离子通道,主要在检测疼痛刺激的特殊感觉神经元中表达。尽管它的许多功能作用仍在继续被揭示,但它已被证实在外周炎症性痛觉过敏和疼痛的知觉中发挥关键作用。TRPV1不仅在包括炎症和神经损伤在内的多种条件下被致敏和/或激活,而且在这些相同的病理条件下也会经历表达水平的变化。就在我们对TRPV1激活的结构要求的理解不断加深的同时,有证据表明TRPV1形成了异构体通道复合体。本文就TRPV1剪接变异体:VR.5‘SV、TRPV1b/beta和TRPV1var的结构和功能效应作一综述。通过它们与TRPV1的共表达和形成异构体复合体,它们被证明能够调节TRPV1的激活。此外,TRPV1剪接变异亚单位也可能有助于独特的激活特性,如检测高渗状态。
The capsaicin receptor (TRPV1) is a non-selective cation channel predominantly expressed in specialized sensory neurons that detect painful stimuli. Although its many functional roles continue to be revealed, it has been confirmed to play a critical role in the perception of peripheral inflammatory hyperalgesia and pain. TRPV1 not only is sensitized and/or activated under a wide range of conditions including inflammation and nerve injury but also undergoes changes in expressed levels in response to these same pathologic conditions. Just as our understanding of the structural requirements of TRPV1 activation has grown, there is evidence that TRPV1 forms heteromeric channel complexes. This review is focused on the structural and functional consequence of TRPV1 splice variants: VR.5’sv, TRPV1b/beta and TRPV1var. Through their co-expression and formation of heteromeric complexes with TRPV1, they have been shown to modulate TRPV1 activation. Moreover, TRPV1 splice variant subunits may also contribute unique properties of activation such as the detection of hypertonic conditions.
DOI: 10.1053/jpsu.2001.27959
发表时间: 2001-11-01
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影响因子: --
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