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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1996-12-18
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pubmed:abstractText |
We have demonstrated specific binding sites for [125I]glucagon-like peptide 1 (GLP-1) on membranes from the rodent thyrotrope cell line, alpha-TSH. Specific [125I]GLP-1 binding was saturable and time dependent. Equilibrium saturation binding analysis was consistent with the presence of a single class of binding site (binding capacity, 85 +/- 7 fmol/mg protein) with a dissociation constant (Kd) of 28 +/- 13 pM. The specific GLP-1 receptor agonists, exendin-4 and exendin-3, and the antagonist, exendin-(9-39), bound to the receptor sites with high affinity (Ki = 190 +/- 70 pM; 130 +/- 50 and 1200 +/- 470 pM, respectively). Chemical cross-linking of [125I]GLP-1-receptor complexes revealed a single band of 64,300 +/- 100 Mr in alpha-TSH membranes. In addition, specific PCR studies demonstrated the presence of GLP-1 receptor messenger RNA. Binding of the peptide to alpha-TSH cell membranes resulted in increased intracellular cAMP concentrations (10 nM GLP-1, 1010 +/- 83 pmol/10(6) cells.h; control, 175 +/- 60 pmol/10(6) cells.h; P < 0.002), indicating that the receptor is linked to stimulation of adenylyl cyclase. GLP-1-mediated increases in cAMP were inhibited by exendin-(9-39) in a dose-dependent manner. Furthermore, GLP-1 stimulates basal TSH release from dispersed anterior pituitary cells in a concentration-dependent manner (100 nM GLP-1, 63 +/- 3 fmol/10(6) cells.h; control, 35 +/- 1 fmol/10(6) cells.h; P < 0.0005), but had no effect on basal PRL, GH, or LH release.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Glp-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thyrotropin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0013-7227
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4130-8
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:8828468-Animals,
pubmed-meshheading:8828468-Binding Sites,
pubmed-meshheading:8828468-Blotting, Southern,
pubmed-meshheading:8828468-Caenorhabditis elegans Proteins,
pubmed-meshheading:8828468-Cell Line,
pubmed-meshheading:8828468-Cross-Linking Reagents,
pubmed-meshheading:8828468-Cyclic AMP,
pubmed-meshheading:8828468-Male,
pubmed-meshheading:8828468-Membrane Glycoproteins,
pubmed-meshheading:8828468-Pituitary Gland, Anterior,
pubmed-meshheading:8828468-Polymerase Chain Reaction,
pubmed-meshheading:8828468-Rats,
pubmed-meshheading:8828468-Rats, Wistar,
pubmed-meshheading:8828468-Thyrotropin
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pubmed:year |
1996
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pubmed:articleTitle |
Glucagon-like peptide-1 (GLP-1) releases thyrotropin (TSH): characterization of binding sites for GLP-1 on alpha-TSH cells.
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pubmed:affiliation |
Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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