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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1995-4-13
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pubmed:abstractText |
Rat 1 fibroblasts which had been transfected to express the human alpha 2C10 adrenoceptor (clone 1C) were further co-transfected with a plasmid containing the hygromycin-B-resistance gene and a plasmid containing a cDNA encoding the alpha-subunit of the rat pertussis-toxin-sensitive G-protein G(o)1. In clone 3 the receptor was expressed at some 2.2 pmol/mg of membrane protein, and G(o)1 alpha at approx. 100 pmol/mg of membrane protein. The interaction of these two polypeptides and that between the receptor and Gi2 alpha (endogenously expressed at some 50 pmol/mg of membrane protein) were studied. Agonist activation of G(o)1 alpha was observed in membranes of the alpha 2C10-adrenoceptor(+)-G(o)1 alpha+ cells (clone 3), but not in alpha 2C10-adrenoceptor(+)-G(o)alpha-cells (clone 1C), whereas similar agonist-dependent activation of Gi2 alpha was observed in both cell types. alpha 2C10-adrenoceptor activation of G(o)1 alpha and Gi2 alpha in clone-3 membranes was produced with similar agonist-dose-effect curves. These observations indicate that the receptor interacts with equivalent affinity with each of these G-proteins. Agonist-dependent cholera-toxin-catalysed [32P]ADP-ribosylation of G(o)1 alpha was terminated when the alpha 2-adrenoceptor antagonist yohimbine was added subsequent to agonist-induced initiation of the reaction and release of GDP, demonstrating the conformational requirement for this reaction to be the ternary complex of agonist-occupied receptor and guanine-nucleotide-denuded G-protein.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1316767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1317000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1318036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1322406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1346392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1349607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1353077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1354394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1614821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1658606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1679199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1847497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1848855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-1849000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2108170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2159280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2169434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2172464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2510151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2560391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2822023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-2823383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-3036816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-3137927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-7907086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-8099279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-8226727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-8296400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-8449930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887906-8484716
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Adrenergic alpha-Agonists,
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Quinoxalines,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella,
http://linkedlifedata.com/resource/pubmed/chemical/Yohimbine,
http://linkedlifedata.com/resource/pubmed/chemical/brimonidine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
306 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
525-30
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7887906-Adenosine Diphosphate Ribose,
pubmed-meshheading:7887906-Adrenergic alpha-Agonists,
pubmed-meshheading:7887906-Animals,
pubmed-meshheading:7887906-Cholera Toxin,
pubmed-meshheading:7887906-Fibroblasts,
pubmed-meshheading:7887906-GTP-Binding Proteins,
pubmed-meshheading:7887906-Gene Expression,
pubmed-meshheading:7887906-Guanosine Diphosphate,
pubmed-meshheading:7887906-Humans,
pubmed-meshheading:7887906-Immunosorbent Techniques,
pubmed-meshheading:7887906-NAD,
pubmed-meshheading:7887906-Pertussis Toxin,
pubmed-meshheading:7887906-Quinoxalines,
pubmed-meshheading:7887906-Rats,
pubmed-meshheading:7887906-Receptors, Adrenergic, alpha,
pubmed-meshheading:7887906-Transfection,
pubmed-meshheading:7887906-Virulence Factors, Bordetella,
pubmed-meshheading:7887906-Yohimbine
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pubmed:year |
1995
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pubmed:articleTitle |
Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts.
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pubmed:affiliation |
Molecular Pharmacology Group, University of Glasgow, Scotland, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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