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J. Biol. Chem., Vol. 279, Issue 36, 37423-37430, September 3, 2004

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An Alternative Splicing Product of the Murine trpv1 Gene Dominant Negatively Modulates the Activity of TRPV1 Channels^*

Chunbo Wang, Hong-Zhen Hu¶, Craig K. Colton, Jackie D. Wood¶, and Michael X. Zhu||

From the Department of Neuroscience and Center for Molecular Neurobiology and the ^¶Department of Physiology and Cell Biology, The Ohio State University, Columbus, Ohio 43210

Transient receptor potential vanilloid 1 (TRPV1), or vanilloid receptor 1, is the founding member of the vanilloid type of TRP superfamily of nonselective cation channels. TRPV1 is activated by noxious heat, acid, and alkaloid irritants as well as several endogenous ligands and is sensitized by inflammatory factors, thereby serving important functions in detecting noxious stimuli in the sensory system and pathological states in different parts of the body. Whereas numerous studies have been carried out using the rat and human TRPV1 cDNA, the mouse TRPV1 cDNA has not been characterized. Here, we report molecular cloning of two TRPV1 cDNA variants from dorsal root ganglia of C57BL/6 mice. The deduced proteins are designated TRPV1 and TRPV1 and contain 839 and 829 amino acids, respectively. TRPV1 arises from an alternative intron recognition signal within exon 7 of the trpv1 gene. We found a predominant expression of TRPV1 in many tissues and significant expression of TRPV1 in dorsal root ganglia, skin, stomach, and tongue. When expressed in HEK 293 cells or Xenopus oocytes, TRPV1 formed a Ca²⁺-permeable channel activated by ligands known to stimulate TRPV1. TRPV1 was not functional by itself but its co-expression inhibited the function of TRPV1. Furthermore, although both isoforms were synthesized at a similar rate, less TRPV1 than TRPV1 protein was found in cells and on the cell surface, indicating that the isoform is highly unstable. Our data suggest that TRPV1 is a naturally occurring dominant-negative regulator of the responses of sensory neurons to noxious stimuli.

Received for publication, June 28, 2004

^* This work was supported by National Institutes of Health Grants NS42183 (to M. X. Z.) and DK057075 (to J. D. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^|| To whom correspondence should be addressed: Center for Molecular Neurobiology, The Ohio State University, 168 Rightmire Hall, 1060 Carmack Rd., Columbus, OH 43210. Tel.: 614-292-8173; Fax: 614-292-5379; E-mail: zhu.55{at}osu.edu.

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