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Howard Hughes Medical Institute, Children's Hospital, Boston, Massachusetts (D.E.C.); Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland C.M.); Pharmakologisches Institut, Freie Universitaet Berlin, Berlin, Germany (G.S.); and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California (D.J.)
The transient receptor potential (TRP) proteins are six transmembrane-containing subunits that combine to form cation-selective ion channels. TRP channels are present in yeast, Drosophila, Caenorhabditis elegans, and mammals. They are widely distributed and sense local changes in stimuli ranging from light to temperature and osmolarity. Mammals contain at least 22 distinct genes encoding these ion channels. This summary article presents an overview of the molecular relationships among the TRP channels and a standard nomenclature for them, which is derived from the IUPHAR Compendium of Voltage-Gated Ion Channels.1 The complete Compendium, including data tables for each member of the TRP channel family, can be found at http://www.iuphar-db.org/iuphar-ic/.
Abstract Introduction Structural Features TRP Channel Functional Features TRPC (Short, Canonical TRPC) Family TRPV (osm-9-Like or Vanilloid Receptor TRP) Family TRPM (Long TRPC, Melastatin) Family TRPA Ankyrin-Repeat TRP Channel Family Conclusion
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