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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-1-26
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pubmed:abstractText |
The ligand-induced proteolytic cleavage of the V2 vasopressin receptor transiently expressed in COS cells was investigated. After incubation of the cell membranes with a photoreactive ligand possessing full agonistic properties for V2 receptors, approximately 90% of the porcine and bovine V2 vasopressin receptors were cleaved in the upper part of transmembrane helix 2 at a heptapeptide sequence conserved in both vasopressin and oxytocin receptors. The oxytocin receptor was completely resistant to proteolysis after binding the same photoreactive ligand, which is only a partial agonist for this receptor. Chimeric V2/oxytocin receptors obtained by transfer of extracellular domains of the oxytocin receptor into the V2 receptor showed an increase in binding affinity for oxytocin versus vasopressin and a diminished cleavage. The proteolysis-resistant chimeric V2/oxytocin receptor, which contains the first three extracellular domains of the oxytocin receptor, stimulated cAMP accumulation to a larger extent in response to vasopressin than the wild-type receptor and showed impaired desensitization of the adenylate cyclase system. Our data indicate that the proteolytic cleavage of the V2 receptor requires a defined conformation, especially of the first two extracellular domains that is induced by agonist binding. Furthermore, the results suggest that the proteolytic V2 receptor cleavage might play a role in signal termination at elevated hormone concentrations.
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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/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Oxytocin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vasopressin,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
538-48
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10561596-Adenylate Cyclase,
pubmed-meshheading:10561596-Amino Acid Sequence,
pubmed-meshheading:10561596-Animals,
pubmed-meshheading:10561596-COS Cells,
pubmed-meshheading:10561596-Cattle,
pubmed-meshheading:10561596-Cloning, Molecular,
pubmed-meshheading:10561596-Cyclic AMP,
pubmed-meshheading:10561596-DNA, Complementary,
pubmed-meshheading:10561596-Dose-Response Relationship, Drug,
pubmed-meshheading:10561596-Enzyme Activation,
pubmed-meshheading:10561596-Humans,
pubmed-meshheading:10561596-Ligands,
pubmed-meshheading:10561596-Microscopy, Fluorescence,
pubmed-meshheading:10561596-Models, Molecular,
pubmed-meshheading:10561596-Molecular Sequence Data,
pubmed-meshheading:10561596-Mutagenesis, Site-Directed,
pubmed-meshheading:10561596-Point Mutation,
pubmed-meshheading:10561596-Protein Binding,
pubmed-meshheading:10561596-Protein Conformation,
pubmed-meshheading:10561596-Protein Structure, Tertiary,
pubmed-meshheading:10561596-Proteins,
pubmed-meshheading:10561596-Receptors, Oxytocin,
pubmed-meshheading:10561596-Receptors, Vasopressin,
pubmed-meshheading:10561596-Sequence Homology, Amino Acid,
pubmed-meshheading:10561596-Swine,
pubmed-meshheading:10561596-Time Factors,
pubmed-meshheading:10561596-Transfection,
pubmed-meshheading:10561596-Type C Phospholipases
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pubmed:year |
1999
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pubmed:articleTitle |
Structural requirements for V2 vasopressin receptor proteolytic cleavage.
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pubmed:affiliation |
Institut für Biohemie, Johannes Gutenberg-Universität, Mainz, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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