Zhang, Yinong and Chou, Joseph H. and Bradley, Jonathan and Bargmann, Cornelia I. and Zinn, Kai (1997) The Caenorhabditis elegans seven-transmembrane protein ODR-10 functions as an odorant receptor in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America, 94 (22). pp. 12162-12167. ISSN 0027-8424. PMCID PMC23737. http://resolver.caltech.edu/CaltechAUTHORS:ZHApnas97b
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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.
|Additional Information:||Copyright © 1997 by the National Academy of Sciences. Communicated by Norman Davidson, California Institute of Technology, Pasadena, CA, August 26, 1997 (received for review July 20, 1997). We thank Henry A. Lester, Norman Davidson, David J. Anderson, Barbara Imperiali, Chand Desai, Yasuhito Uezono, and the members of the Zinn and Bargmann groups for helpful discussions; Rochelle Diamond for flow cytometry; Gary Belford for advice on calcium imaging; Marc Caron for the HA-b2AdR plasmid; and Bo Yu for the M1AChR plasmid. We also thank the Caltech Cell Sorting facility for access to flow cytometry equipment and the Beckman Imaging Center for use of the imaging facility. This work was supported by grants from the National Institute of Mental Health to K.Z. and from the American Cancer Society to C.I.B. C.I.B. is an Assistant Investigator of the Howard Hughes Medical Institute. Y.Z. was supported by a National Research Service Award postdoctoral fellowship from the National Institutes of Health (National Institute on Deafness and Other Communication Disorders). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.|
|Subject Keywords:||OLFACTION; G PROTEIN-COUPLED RECEPTOR; SIGNAL TRANSDUCTION; CHEMOTAXIS; NUCLEOTIDE-GATED CHANNEL; C-ELEGANS; NEURONS|
|PubMed Central ID:||PMC23737|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||01 Feb 2006|
|Last Modified:||05 Apr 2016 20:05|
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