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TRPV3 is a temperature-sensitive vanilloid receptor-like protein

Author

Listed:
  • G. D. Smith

    (Neurology-CEDD, GlaxoSmithKline)

  • M. J. Gunthorpe

    (Neurology-CEDD, GlaxoSmithKline)

  • R. E. Kelsell

    (Genetics Research, GlaxoSmithKline)

  • P. D. Hayes

    (Genetics Research, GlaxoSmithKline)

  • P. Reilly

    (Neurology-CEDD, GlaxoSmithKline)

  • P. Facer

    (Imperial College, Hammersmith Hospital)

  • J. E. Wright

    (Neurology-CEDD, GlaxoSmithKline)

  • J. C. Jerman

    (Discovery Research, GlaxoSmithKline)

  • J.-P. Walhin

    (Genetics Research, GlaxoSmithKline)

  • L. Ooi

    (Neurology-CEDD, GlaxoSmithKline)

  • J. Egerton

    (Neurology-CEDD, GlaxoSmithKline)

  • K. J. Charles

    (Neurology-CEDD, GlaxoSmithKline)

  • D. Smart

    (Neurology-CEDD, GlaxoSmithKline)

  • A. D. Randall

    (Neurology-CEDD, GlaxoSmithKline)

  • P. Anand

    (Imperial College, Hammersmith Hospital)

  • J. B. Davis

    (Neurology-CEDD, GlaxoSmithKline)

Abstract

Vanilloid receptor-1 (VR1, also known as TRPV1) is a thermosensitive, nonselective cation channel that is expressed by capsaicin-sensitive sensory afferents and is activated by noxious heat, acidic pH and the alkaloid irritant capsaicin1. Although VR1 gene disruption results in a loss of capsaicin responses, it has minimal effects on thermal nociception2,3. This and other experiments—such as those showing the existence of capsaicin-insensitive heat sensors in sensory neurons4—suggest the existence of thermosensitive receptors distinct from VR1. Here we identify a member of the vanilloid receptor/TRP gene family, vanilloid receptor-like protein 3 (VRL3, also known as TRPV3), which is heat-sensitive but capsaicin-insensitive. VRL3 is coded for by a 2,370-base-pair open reading frame, transcribed from a gene adjacent to VR1, and is structurally homologous to VR1. VRL3 responds to noxious heat with a threshold of about 39 °C and is co-expressed in dorsal root ganglion neurons with VR1. Furthermore, when heterologously expressed, VRL3 is able to associate with VR1 and may modulate its responses. Hence, not only is VRL3 a thermosensitive ion channel but it may represent an additional vanilloid receptor subunit involved in the formation of heteromeric vanilloid receptor channels.

Suggested Citation

  • G. D. Smith & M. J. Gunthorpe & R. E. Kelsell & P. D. Hayes & P. Reilly & P. Facer & J. E. Wright & J. C. Jerman & J.-P. Walhin & L. Ooi & J. Egerton & K. J. Charles & D. Smart & A. D. Randall & P. An, 2002. "TRPV3 is a temperature-sensitive vanilloid receptor-like protein," Nature, Nature, vol. 418(6894), pages 186-190, July.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6894:d:10.1038_nature00894
    DOI: 10.1038/nature00894
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    Cited by:

    1. Arthur Neuberger & Kirill D. Nadezhdin & Alexander I. Sobolevsky, 2022. "Structural mechanism of TRPV3 channel inhibition by the anesthetic dyclonine," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Jing Lei & Reiko U. Yoshimoto & Takeshi Matsui & Masayuki Amagai & Mizuho A. Kido & Makoto Tominaga, 2023. "Involvement of skin TRPV3 in temperature detection regulated by TMEM79 in mice," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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