1
40
2
-
Text
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n/a
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Pages
244-251
Issue
1
Volume
23
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Dublin Core
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Title
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EFFECT OF INDUCERS AND AGING ON RABBIT LIVER MICROSOMAL DRUG-METABOLIZING-ENZYMES
Publisher
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Molecular Pharmacology
Date
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1983
1983
Subject
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Pharmacology & Pharmacy
Creator
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Chiang J Y L; Dilella A G; Steggles A W
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n/a
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Journal Article or Conference Abstract Publication
1983
Chiang J Y L
Dilella A G
Journal Article or Conference Abstract Publication
Molecular pharmacology
Pharmacology & Pharmacy
Steggles A W
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1124/mol.63.1.183" target="_blank" rel="noreferrer noopener">http://doi.org/10.1124/mol.63.1.183</a>
Pages
183–191
Issue
1
Volume
63
Dublin Core
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Title
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Specificity of metabotropic glutamate receptor 2 coupling to G proteins.
Publisher
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Molecular pharmacology
Date
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2003
2003-01
Subject
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Amino Acid; Amino Acid Sequence; Animals; Calcium/metabolism; Electrophysiology; Gi-Go/metabolism; GTP-Binding Protein alpha Subunits; GTP-Binding Proteins/*metabolism; Metabotropic Glutamate/*metabolism; Molecular Sequence Data; Neurons/*drug effects/metabolism; Pertussis Toxin/*pharmacology; Rats; Receptors; Sequence Homology; Superior Cervical Ganglion/cytology; Wistar
Creator
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Kammermeier Paul J; Davis Margaret I; Ikeda Stephen R
Description
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Metabotropic glutamate receptor 2 (mGluR2) is a class 3 G protein-coupled receptor and an important mediator of synaptic activity in the central nervous system. Previous work demonstrated that mGluR2 couples to pertussis toxin (PTX)-sensitive G proteins. However, the specificity of mGluR2 coupling to individual members of the G(i/o) family is not known. Using heterologously expressed mGluR2 in rat sympathetic neurons from the superior cervical ganglion (SCG), the mGluR2/G protein coupling profile was characterized by reconstituting coupling in PTX-treated cells expressing PTX-insensitive mutant Galpha proteins and Gbetagamma. By employing this method, it was demonstrated that mGluR2 coupled strongly with Galphaob, Galphai1, Galphai2, and Galphai3, although coupling to Galphaoa was less efficient. In addition, mGluR2 did not seem to couple to the most divergent member of the G(i/o) family, Galphaz, although Galphaz coupled strongly to the endogenous alpha2 adrenergic receptor. To determine which Galpha proteins may be natively expressed in SCG neurons, the presence of mRNA for various Galpha proteins was tested using reverse transcription-polymerase chain reaction. Strong bands were detected for all members of the G(i/o) family (Galphao, Galphai1, Galphai2, Galphai3, Galphaz) as well as for Galpha11 and Galphas. A weak signal was detected for Galphaq and no Galpha15 mRNA was detected.
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<a href="http://doi.org/10.1124/mol.63.1.183" target="_blank" rel="noreferrer noopener">10.1124/mol.63.1.183</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2003
Amino Acid
Amino Acid Sequence
Animals
Calcium/metabolism
Davis Margaret I
Electrophysiology
Gi-Go/metabolism
GTP-Binding Protein alpha Subunits
GTP-Binding Proteins/*metabolism
Ikeda Stephen R
Kammermeier Paul J
Metabotropic Glutamate/*metabolism
Molecular pharmacology
Molecular Sequence Data
Neurons/*drug effects/metabolism
Pertussis Toxin/*pharmacology
Rats
Receptors
Sequence Homology
Superior Cervical Ganglion/cytology
Wistar