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Potentiation of TRPV3 channel function by unsaturated fatty acids
Author(s) -
Hu HongZhen,
Xiao Rui,
Wang Chunbo,
Gao Na,
Colton Craig K.,
Wood Jackie D.,
Zhu Michael X.
Publication year - 2006
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.20648
Subject(s) - trpv , transient receptor potential channel , long term potentiation , trpv1 , chemistry , lipoxygenase , arachidonic acid , patch clamp , protein kinase c , biochemistry , intracellular , microbiology and biotechnology , biophysics , kinase , biology , enzyme , receptor
Abstract Transient receptor potential vanilloid (TRPV) channels are polymodal detectors of multiple environmental factors, including temperature, pH, and pressure. Inflammatory mediators enhance TRPV function through multiple signaling pathways. The lipoxygenase and epoxygenase products of arachidonic acid (AA) metabolism have been shown to directly activate TRPV1 and TRPV4, respectively. TRPV3 is a thermosensitive channel with an intermediate temperature threshold of 31–39°C. We have previously shown that TRPV3 is activated by 2‐aminoethoxydiphenyl borate (2APB). Here we show that AA and other unsaturated fatty acids directly potentiate 2APB‐induced responses of TRPV3 expressed in HEK293 cells, Xenopus oocytes, and mouse keratinocytes. The AA‐induced potentiation is observed in intracellular Ca 2+ measurement, whole‐cell and two‐electrode voltage clamp studies, as well as single channel recordings of excised inside‐out and outside‐out patches. The fatty acid‐induced potentiation is not blocked by inhibitors of protein kinase C and thus differs from that induced by the kinase. The potentiation does not require AA metabolism but is rather mimicked by non‐metabolizable analogs of AA. These results suggest a novel mechanism regulating the TRPV3 response to inflammation, which differs from TRPV1 and TRPV4, and involves a direct action of free fatty acids on the channel. J. Cell. Physiol. © 2006 Wiley‐Liss, Inc.