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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 5
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pubmed:dateCreated |
2004-10-20
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pubmed:abstractText |
Complexes of alpha(2A)-ARs (alpha(2A)-adrenergic receptors) and MORs (mu-opioid receptors), probably hetero-oligomers, were detected by co-immunoisolation after extraction from HEK-293 cells (human embryonic kidney 293 cells). Functional communication between these receptors is revealed by alpha(2A)-AR activation of a pertussis toxin-insensitive G(i)alpha subunit (termed as G(i)1) when fused with the MOR and evaluated in membranes from pertussis toxin-treated cells. However, the alpha(2A)-AR does not require transactivation through MOR, since quantitatively indistinguishable results were observed in cells co-expressing alpha(2A)-AR and a fusion protein of G(i)1 with the first transmembrane span of MOR (myc-MOR-TM1). Functional cross-talk among these alpha(2A)-AR-MOR complexes does not occur for internalization profiles; incubation with adrenaline (epinephrine) leads to endocytosis of alpha(2A)-AR but not MOR, while incubation with DAMGO ([D-Ala,NMe-Phe,Gly-ol]enkephalin) leads to endocytosis of MOR but not alpha(2A)-AR in cells co-expressing both the receptors. Hence, alpha(2A)-AR and MOR hetero-oligomers, although they occur, do not have an obligatory functional influence on one another in the paradigms studied.
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pubmed:grant |
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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/ADRA2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Analgesics, Opioid,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Enkephalin, Ala(2)-MePhe(4)-Gly(5)-,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha-2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Opioid, mu,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0300-5127
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
856-60
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15494033-Analgesics, Opioid,
pubmed-meshheading:15494033-Blotting, Western,
pubmed-meshheading:15494033-Cell Line,
pubmed-meshheading:15494033-DNA, Complementary,
pubmed-meshheading:15494033-Endocytosis,
pubmed-meshheading:15494033-Enkephalin, Ala(2)-MePhe(4)-Gly(5)-,
pubmed-meshheading:15494033-GTP-Binding Proteins,
pubmed-meshheading:15494033-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:15494033-Humans,
pubmed-meshheading:15494033-Immunoprecipitation,
pubmed-meshheading:15494033-Microscopy, Fluorescence,
pubmed-meshheading:15494033-Neurons,
pubmed-meshheading:15494033-Pertussis Toxin,
pubmed-meshheading:15494033-Protein Binding,
pubmed-meshheading:15494033-Receptors, Adrenergic, alpha-2,
pubmed-meshheading:15494033-Receptors, Opioid, mu,
pubmed-meshheading:15494033-Recombinant Fusion Proteins,
pubmed-meshheading:15494033-Transcriptional Activation,
pubmed-meshheading:15494033-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Hetero-oligomers of alpha2A-adrenergic and mu-opioid receptors do not lead to transactivation of G-proteins or altered endocytosis profiles.
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pubmed:affiliation |
Department of Pharmacology and Center for Molecular Neuroscience, Vanderbilt University Medical Center, 2200 Pierce Ave., 464A RRB, Nashville, TN 37232-6600, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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