Abstract
TRPA1 is an ion channel expressed by nociceptors and activated by irritant compounds such as mustard oil. The endogenous function of TRPA1 has remained unclear, a fact highlighted by ongoing debate over its potential role as a sensor of noxious cold. Here we show that intracellular Ca(2+) activates human TRPA1 via an EF-hand domain and that cold sensitivity occurs indirectly (and nonphysiologically) through increased [Ca(2+)](i) during cooling in heterologous systems.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Analgesics, Non-Narcotic / pharmacology
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Calcium / metabolism*
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Calcium Channels / physiology*
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Carbachol / pharmacology
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Cell Line
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Cold Temperature
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Diagnostic Imaging / methods
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Dose-Response Relationship, Drug
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EF Hand Motifs / physiology
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Humans
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Intracellular Fluid / metabolism
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Luminescent Proteins / metabolism
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Membrane Proteins / physiology*
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Mutagenesis / physiology
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Nerve Tissue Proteins / physiology*
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Patch-Clamp Techniques / methods
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TRPA1 Cation Channel
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Transfection / methods
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Transient Receptor Potential Channels / drug effects
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Transient Receptor Potential Channels / physiology
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Transient Receptor Potential Channels / radiation effects
Substances
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Analgesics, Non-Narcotic
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Calcium Channels
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Luminescent Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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TRPA1 Cation Channel
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TRPA1 protein, human
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Transient Receptor Potential Channels
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Carbachol
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Calcium