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Spider toxins activate the capsaicin receptor to produce inflammatory pain

Author

Listed:
  • Jan Siemens

    (University of California–San Francisco)

  • Sharleen Zhou

    (University of California–Berkeley)

  • Rebecca Piskorowski

    (University of California–San Francisco
    HHMI Columbia University)

  • Tetsuro Nikai

    (University of California–San Francisco)

  • Ellen A. Lumpkin

    (University of California–San Francisco
    Baylor College of Medicine)

  • Allan I. Basbaum

    (University of California–San Francisco)

  • David King

    (University of California–Berkeley)

  • David Julius

    (University of California–San Francisco)

Abstract

A taste for pain Three peptides isolated from the venom of the West Indian tarantula Psalmopoeus cambridgei have been found to promote pain and inflammation by activating the same neuronal receptor as capsaicin, the hot component of chilli peppers. This suggests that tarantulas and chillis use similar tactics to deter predators. The newly discovered peptides are also unusual because they trigger an excitatory response. Peptides with similar structures that bind to other ion channels are already known, but are inhibitory.

Suggested Citation

  • Jan Siemens & Sharleen Zhou & Rebecca Piskorowski & Tetsuro Nikai & Ellen A. Lumpkin & Allan I. Basbaum & David King & David Julius, 2006. "Spider toxins activate the capsaicin receptor to produce inflammatory pain," Nature, Nature, vol. 444(7116), pages 208-212, November.
  • Handle: RePEc:nat:nature:v:444:y:2006:i:7116:d:10.1038_nature05285
    DOI: 10.1038/nature05285
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    Cited by:

    1. Li, Yangyang & Jin, Yiying & Li, Jinhui & Li, Hailong & Yu, Zhixin, 2016. "Effects of pungency degree on mesophilic anaerobic digestion of kitchen waste," Applied Energy, Elsevier, vol. 181(C), pages 171-178.
    2. Maxim V Nikolaev & Natalia A Dorofeeva & Margarita S Komarova & Yuliya V Korolkova & Yaroslav A Andreev & Irina V Mosharova & Eugene V Grishin & Denis B Tikhonov & Sergey A Kozlov, 2017. "TRPV1 activation power can switch an action mode for its polypeptide ligands," PLOS ONE, Public Library of Science, vol. 12(5), pages 1-16, May.

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