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• W2030689683 abstract "The transient receptor potential ankyrin 1 (TRPA1) is a Ca(2+)-permeable, nonselective cation channel mainly expressed in a subset of nociceptive neurons. TRPA1 functions as a cellular sensor detecting mechanical, chemical, and thermal stimuli. Because TRPA1 is considered to be a key player in nociception and inflammatory pain, TRPA1 antagonists have been developed as analgesic agents. Recently, by utilizing species differences, we identified the molecular basis of the antagonistic action of A967079, one of the most potent mammalian TRPA1 antagonists. Here, we show a unique effect of A967079 on TRPA1 from diverse vertebrate species, i.e. it acts as an agonist but not as an antagonist for chicken and frog TRPA1s. By characterizing chimeric channels of human and chicken TRPA1s, as well as point mutants, we found that a single specific amino acid residue located within the putative fifth transmembrane domain was involved in not only the stimulatory but also the inhibitory actions of A967079. AP18, structurally related to A967079, exerted similar pharmacological properties to A967079. Our findings and previous reports on species differences in the sensitivity to TRPA1 antagonists supply useful information in the search for novel analgesic medicines targeting TRPA1." @default.
• W2030689683 created "2016-06-24" @default.
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• W2030689683 date "2014-11-01" @default.
• W2030689683 modified "2023-10-16" @default.
• W2030689683 title "Molecular Basis Determining Inhibition/Activation of Nociceptive Receptor TRPA1 Protein" @default.
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• W2030689683 doi "https://doi.org/10.1074/jbc.m114.586891" @default.
• W2030689683 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4231671" @default.
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