Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 30 May 2000
Vol. 2000, Issue 34, p. tw3
[DOI: 10.1126/scisignal.342000tw3]

EDITORS' CHOICE

Physiology More Painful Ligands

Certain sensory neurons express the cell surface receptor for capsaicin, the agent in hot peppers that causes the sensation of thermal and chemical pain. Capsaicin binds to the intracellular domain of its receptor, a ligand-gated nonselective cation channel, suggesting that there may be endogenous intracellular activators. Hwang et al. demonstrate that certain products of lipoxygenases, called eicosanoids, directly activate the capsaicin receptor. Activation by eicosanoids was blocked by an antagonist of the receptor. Prostaglandins, thought to play a role in mediating inflammatory pain, failed to activate the receptor. Structural similarities between capsaicin and the eicosanoids may explain their use of a common receptor.

Hwang, S.W., Cho, H., Kwak, J., Lee, S.-Y., Kang, C.-J., Jung, J., Cho, S., Minm K.H., Suh, Y.-G., Kin, D., and Oh, U. (2000) Direct activation of capsaicin receptors by products of lipoxygenases: Endogenous capsaicin-like substances. Proc. Natl. Acad. Sci. U.S.A. 97: 6155-6160. [Abstract] [Full Text]

Citation: More Painful Ligands. Sci. STKE 2000, tw3 (2000).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882