rdf:type |
|
lifeskim:mentions |
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0086418,
umls-concept:C0167117,
umls-concept:C0185117,
umls-concept:C0205245,
umls-concept:C0231491,
umls-concept:C0243192,
umls-concept:C0247947,
umls-concept:C0378073,
umls-concept:C0597357,
umls-concept:C2911684
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pubmed:issue |
11
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pubmed:dateCreated |
1993-11-22
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pubmed:databankReference |
|
pubmed:abstractText |
A complementary DNA for a glucagon-like peptide-1 receptor was isolated from a human pancreatic islet cDNA library. The isolated clone encoded a protein with 90% identity to the rat receptor. In stably transfected fibroblasts, the receptor bound [125I]GLP-1 with high affinity (Kd = 0.5 nM) and was coupled to adenylate cyclase as detected by a GLP-1-dependent increase in cAMP production (EC50 = 93 pM). Two peptides from the venom of the lizard Heloderma suspectum, exendin-4 and exendin-(9-39), displayed similar ligand binding affinities to the human GLP-1 receptor. Whereas exendin-4 acted as an agonist of the receptor, inducing cAMP formation, exendin-(9-39) was an antagonist of the receptor, inhibiting GLP-1-induced cAMP production. Because GLP-1 has been proposed as a potential agent for treatment of NIDDM, our present data will contribute to the characterization of the receptor binding site and the development of new agonists of this receptor.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/exenatide,
http://linkedlifedata.com/resource/pubmed/chemical/glucagon-like peptide receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0012-1797
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1678-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8405712-Amino Acid Sequence,
pubmed-meshheading:8405712-Amino Acids,
pubmed-meshheading:8405712-Base Sequence,
pubmed-meshheading:8405712-Cloning, Molecular,
pubmed-meshheading:8405712-Cyclic AMP,
pubmed-meshheading:8405712-DNA,
pubmed-meshheading:8405712-Diabetes Mellitus, Type 2,
pubmed-meshheading:8405712-Gene Expression,
pubmed-meshheading:8405712-Humans,
pubmed-meshheading:8405712-Islets of Langerhans,
pubmed-meshheading:8405712-Ligands,
pubmed-meshheading:8405712-Molecular Sequence Data,
pubmed-meshheading:8405712-Peptide Fragments,
pubmed-meshheading:8405712-Peptides,
pubmed-meshheading:8405712-Receptors, Cell Surface,
pubmed-meshheading:8405712-Receptors, Glucagon,
pubmed-meshheading:8405712-Venoms
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning and functional expression of the human islet GLP-1 receptor. Demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist of the receptor.
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pubmed:affiliation |
Department of Pharmacology and Toxicology, University of Lausanne, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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