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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1997-12-4
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pubmed:abstractText |
The nematode Caenorhabditis elegans exhibits behavioral responses to many volatile odorants. Chemotaxis toward one such odorant, diacetyl (butanedione), requires the function of a seven-transmembrane receptor protein encoded by the odr-10 gene. To determine directly whether ODR-10 protein is an odorant receptor, it is necessary to express the protein in a heterologous system and show that it responds to diacetyl by activation of a G protein signaling pathway. Here we demonstrate that human cells expressing ODR-10 on their surfaces exhibit a transient elevation in intracellular Ca2+ levels after diacetyl application. Volatile compounds that differ from diacetyl only by the addition of a methyl group (2,3-pentanedione) or the absence of a keto group (butanone) are not ODR-10 agonists. Behavioral responses to these compounds are not dependent on odr-10 function, so ODR-10 specificity in human cells resembles in vivo specificity. The apparent affinity of ODR-10 for diacetyl observed in human cells is consistent with the diacetyl concentration ranges that allow efficient nematode chemotaxis. ODR-10 expressed in human cells also responds to two anionic compounds, pyruvate and citrate, which are metabolic precursors used for diacetyl production by certain bacterial species. Ca2+ elevation in response to ODR-10 activation is due to release from intracellular stores.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-1112927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-1840504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-7585938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-7605064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-7897503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-7926732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8348618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8601313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8833453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8893025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8893026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9342380-8893027
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12162-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9342380-Animals,
pubmed-meshheading:9342380-Caenorhabditis elegans,
pubmed-meshheading:9342380-Caenorhabditis elegans Proteins,
pubmed-meshheading:9342380-Calcium,
pubmed-meshheading:9342380-Cells, Cultured,
pubmed-meshheading:9342380-Chemotaxis,
pubmed-meshheading:9342380-Citric Acid,
pubmed-meshheading:9342380-Diacetyl,
pubmed-meshheading:9342380-Dose-Response Relationship, Drug,
pubmed-meshheading:9342380-GTP-Binding Proteins,
pubmed-meshheading:9342380-Helminth Proteins,
pubmed-meshheading:9342380-Humans,
pubmed-meshheading:9342380-Protein Conformation,
pubmed-meshheading:9342380-Pyruvic Acid,
pubmed-meshheading:9342380-Receptors, Odorant,
pubmed-meshheading:9342380-Recombinant Proteins,
pubmed-meshheading:9342380-Signal Transduction,
pubmed-meshheading:9342380-Structure-Activity Relationship,
pubmed-meshheading:9342380-Transfection
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pubmed:year |
1997
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pubmed:articleTitle |
The Caenorhabditis elegans seven-transmembrane protein ODR-10 functions as an odorant receptor in mammalian cells.
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pubmed:affiliation |
Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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