Department of Anesthesia and Perioperative Care, University of California, San Francisco, CA 94143-0427, USA.
Front Biosci (Landmark Ed). 2010 Jun 1;15(3):872-82. doi: 10.2741/3651.
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.
辣椒素受体（TRPV1）是一种非选择性阳离子通道，主要表达在专门的感觉神经元中，这些神经元可以检测到疼痛刺激。尽管它的许多功能作用仍在不断被揭示，但已经证实它在感知外周炎症性痛觉过敏和疼痛方面起着关键作用。TRPV1 不仅在包括炎症和神经损伤在内的广泛条件下被敏化和/或激活，而且还会对这些相同的病理条件做出表达水平的变化。正如我们对 TRPV1 激活的结构要求的理解不断加深，有证据表明 TRPV1 形成异源通道复合物。这篇综述集中于 TRPV1 剪接变体：VR.5'sv、TRPV1b/beta 和 TRPV1var 的结构和功能后果。通过它们与 TRPV1 的共表达和形成异源复合物，已经表明它们可以调节 TRPV1 的激活。此外，TRPV1 剪接变体亚基也可能对激活产生独特的特性，例如检测高渗条件。
