Thimerosal decreases TRPV1 activity by oxidation of extracellular sulfhydryl residues

Yunju Jin, Dong Kwan Kim, Lee Yong Khil, Uhtaek Oh, Jun Kim, Jiyeon Kwak

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


TRPV1, a receptor for capsaicin, plays a key role in mediating thermal and inflammatory pain. Because the modulation of ion channels by the cellular redox state is a significant determinant of channel function, we investigated the effects of sulfhydryl modification on the activity of TRPV1. Thimerosal, which oxidizes sulfhydryls, blocked the capsaicin-activated inward current (I cap) in cultured sensory neurons, in a reversible and dose-dependent manner, which was prevented by the co-application of the reducing agent, dithiothreitol. Among the three cysteine residues of TRPV1 that are exposed to the extracellular space, the oxidation-induced effect of thimerosal on I cap was blocked only by a point mutation at Cys621. These results suggest that the modification of an extracellular thiol group can alter the activity of TRPV1. Consequently, we propose that such a modulation of the redox state might regulate the physiological activity of TRPV1.

Original languageEnglish (US)
Pages (from-to)250-255
Number of pages6
JournalNeuroscience Letters
Issue number3
StatePublished - Oct 21 2004


  • Capsaicin
  • Dorsal root ganglion
  • Sulfhydryl oxidation
  • TRPV1
  • Thimerosal

ASJC Scopus subject areas

  • General Neuroscience


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