Source:http://linkedlifedata.com/resource/pubmed/id/15140906
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2004-8-27
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pubmed:abstractText |
Sour (acid) taste is postulated to result from intracellular acidification that modulates one or more acid-sensitive ion channels in taste receptor cells. The identity of such channel(s) remains uncertain. Potassium channels, by regulating the excitability of taste cells, are candidates for acid transducers. Several 2-pore domain potassium leak conductance channels (K(2)P family) are sensitive to intracellular acidification. We examined their expression in mouse vallate and foliate taste buds using RT-PCR, and detected TWIK-1 and -2, TREK-1 and -2, and TASK-1. Of these, TWIK-1 and TASK-1 were preferentially expressed in taste cells relative to surrounding nonsensory epithelium. The related TRESK channel was not detected, whereas the acid-insensitive TASK-2 was. Using confocal imaging with pH-, Ca(2+)-, and voltage-sensitive dyes, we tested pharmacological agents that are diagnostic for these channels. Riluzole (500 microM), selective for TREK-1 and -2 channels, enhanced acid taste responses. In contrast, halothane (< or = approximately 17 mM), which acts on TREK-1 and TASK-1 channels, blocked acid taste responses. Agents diagnostic for other 2-pore domain and voltage-gated potassium channels (anandamide, 10 microM; Gd(3+), 1 mM; arachidonic acid, 100 microM; quinidine, 200 microM; quinine, 100 mM; 4-AP, 10 mM; and TEA, 1 mM) did not affect acid responses. The expression of 2-pore domain channels and our pharmacological characterization suggest that a matrix of ion channels, including one or more acid-sensitive 2-pore domain K channels, could play a role in sour taste transduction. However, our results do not unambiguously identify any one channel as the acid taste transducer.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Citric Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnk1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Tandem Pore...,
http://linkedlifedata.com/resource/pubmed/chemical/potassium channel protein TREK-1
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-3077
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1928-36
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15140906-Animals,
pubmed-meshheading:15140906-Citric Acid,
pubmed-meshheading:15140906-Membrane Potentials,
pubmed-meshheading:15140906-Mice,
pubmed-meshheading:15140906-Mice, Inbred C57BL,
pubmed-meshheading:15140906-Potassium Channels,
pubmed-meshheading:15140906-Potassium Channels, Tandem Pore Domain,
pubmed-meshheading:15140906-Protein Structure, Tertiary,
pubmed-meshheading:15140906-Taste,
pubmed-meshheading:15140906-Taste Buds
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pubmed:year |
2004
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pubmed:articleTitle |
Acid-sensitive two-pore domain potassium (K2P) channels in mouse taste buds.
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pubmed:affiliation |
Dept. of Physiology and Biophysics, University of Miami School of Medicine, 1600 NW 10th Avenue, Miami, FL 33136, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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