IMR Press / FBL / Volume 15 / Issue 3 / DOI: 10.2741/3651

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
TRPV1 splice variants: structure and function
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1 Department of Anesthesia and Perioperative Care; University of California, San Francisco 513 Parnassus Ave. Rm. S436 (Box 0427) San Francisco, CA 94143-0427 , USA
Academic Editor:Mark Schumacher
Front. Biosci. (Landmark Ed) 2010, 15(3), 872–882; https://doi.org/10.2741/3651
Published: 1 June 2010
Abstract

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.

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