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rdf:type |
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lifeskim:mentions |
umls-concept:C0001492,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0034826,
umls-concept:C0037083,
umls-concept:C0043342,
umls-concept:C0752312,
umls-concept:C1160185,
umls-concept:C1554184,
umls-concept:C1710082,
umls-concept:C1879547
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pubmed:issue |
1
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pubmed:dateCreated |
1997-6-30
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pubmed:abstractText |
Using transient transfection of COS-7 and human embryonic kidney 293 cells, we studied the functional properties of a previously cloned muscarinic Xenopus receptor [Herrera et al. (1994): FEBS Lett 352:175-179] and its coupling to adenylyl cyclase (AC) and mitogen-activated protein kinase (MAPK) pathways. Expression of the Xenopus muscarinic receptor results in the inhibition of AC activity and activation of the MAPK pathway through a mechanism that involves a Pertussis-toxin-sensitive G-protein and the G beta gamma subunits. The signal transduction properties of this receptor are similar to the mammalian m2 and m4 muscarinic receptors. These results strongly support the idea that inhibition of AC and MAPK activation, signaled out from the muscarinic oocyte receptor, are involved in the oocyte maturation process.
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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/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Atropine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Carbachol,
http://linkedlifedata.com/resource/pubmed/chemical/Muscarinic Agonists,
http://linkedlifedata.com/resource/pubmed/chemical/Muscarinic Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Muscarinic,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0730-2312
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
75-82
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9138082-Adenylate Cyclase,
pubmed-meshheading:9138082-Adenylate Cyclase Toxin,
pubmed-meshheading:9138082-Animals,
pubmed-meshheading:9138082-Atropine,
pubmed-meshheading:9138082-COS Cells,
pubmed-meshheading:9138082-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9138082-Carbachol,
pubmed-meshheading:9138082-Cell Line,
pubmed-meshheading:9138082-Cloning, Molecular,
pubmed-meshheading:9138082-Humans,
pubmed-meshheading:9138082-Muscarinic Agonists,
pubmed-meshheading:9138082-Muscarinic Antagonists,
pubmed-meshheading:9138082-Pertussis Toxin,
pubmed-meshheading:9138082-Receptors, Muscarinic,
pubmed-meshheading:9138082-Signal Transduction,
pubmed-meshheading:9138082-Transfection,
pubmed-meshheading:9138082-Type C Phospholipases,
pubmed-meshheading:9138082-Virulence Factors, Bordetella,
pubmed-meshheading:9138082-Xenopus laevis
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pubmed:year |
1997
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pubmed:articleTitle |
Dual transduction signaling by a Xenopus muscarinic receptor: adenylyl cyclase inhibition and MAP kinase activation.
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pubmed:affiliation |
Molecular Signaling Unit, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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