Journal
NEUROSCIENCE LETTERS
Volume 369, Issue 3, Pages 250-255Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2004.07.059
Keywords
thimerosal; sulfhydryl oxidation; capsaicin; TRPV1; dorsal root ganglion
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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. (C) 2004 Elsevier Ireland Ltd. All rights reserved.
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