| Sensing of amino acids by the gut-expressed taste receptor T1R1-T1R3 stimulates CCK secretion. | |
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MedLine Citation:
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PMID: 23203156 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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CCK is secreted by endocrine cells of the proximal intestine in response to dietary components, including amino acids. CCK plays a variety of roles in digestive processes, including inhibition of food intake, consistent with a role in satiety. In the lingual epithelium, the sensing of a broad spectrum of L-amino acids is accomplished by the heteromeric amino acid (umami) taste receptor (T1R1-T1R3). T1R1 and T1R3 subunits are also expressed in the intestine. A defining characteristic of umami sensing by T1R1-T1R3 is its potentiation by IMP or GMP. Furthermore, T1R1-T1R3 is not activated by Trp. We show here that, in response to L-amino acids (Phe, Leu, Glu, and Trp), but not D-amino acids, STC-1 enteroendocrine cells and mouse proximal small intestinal tissue explants secrete CCK and that IMP enhances Phe-, Leu-, and Glu-induced, but not Trp-induced, CCK secretion. Furthermore, small interfering RNA inhibition of T1R1 expression in STC-1 cells results in significant diminution of Phe-, Leu-, and Glu-stimulated, but not Trp-stimulated, CCK release. In STC-1 cells and mouse intestine, gurmarin inhibits Phe-, Leu-, and Glu-induced, but not Trp-stimulated, CCK secretion. In contrast, the Ca(2+)-sensing receptor antagonist NPS2143 inhibits Phe-stimulated CCK release partially and Trp-induced CCK secretion totally in mouse intestine. However, NPS2143 has no effect on Leu- or Glu-induced CCK secretion. Collectively, our data demonstrate that functional characteristics and cellular location of the gut-expressed T1R1-T1R3 support its role as a luminal sensor for Phe-, Leu-, and Glu-induced CCK secretion. |
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Authors:
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Kristian Daly; Miran Al-Rammahi; Andrew Moran; Marco Marcello; Yuzo Ninomiya; Soraya P Shirazi-Beechey |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-11-29 |
Journal Detail:
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Title: American journal of physiology. Gastrointestinal and liver physiology Volume: 304 ISSN: 1522-1547 ISO Abbreviation: Am. J. Physiol. Gastrointest. Liver Physiol. Publication Date: 2013 Feb |
Date Detail:
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Created Date: 2013-02-04 Completed Date: 2013-03-19 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 100901227 Medline TA: Am J Physiol Gastrointest Liver Physiol Country: United States |
Other Details:
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Languages: eng Pagination: G271-82 Citation Subset: IM |
Affiliation:
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Epithelial Function and Development Group, Department of Functional and Comparative Genomics, University of Liverpool, Liverpool, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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antagonists & inhibitors,
pharmacology* Animals Blotting, Western Cell Membrane / metabolism Cells, Cultured Cholecystokinin / metabolism* Female Gastrointestinal Tract / drug effects, physiology* Immunohistochemistry Inositol Phosphates / metabolism Isomerism Male Mice Mice, Inbred C57BL Microscopy, Confocal Naphthalenes / pharmacology Peptides / pharmacology Plant Proteins / pharmacology Protein Hydrolysates / pharmacology RNA Interference Receptors, G-Protein-Coupled / drug effects, physiology* Stimulation, Chemical |
| Grant Support | |
ID/Acronym/Agency:
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//Wellcome Trust |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Inositol Phosphates; 0/N-(2-hydroxy-3-(2-cyano-3-chlorophenoxy)propyl)-1,1-dimethyl-2-(2-nephthyl)ethylamine; 0/Naphthalenes; 0/Peptides; 0/Plant Proteins; 0/Protein Hydrolysates; 0/Receptors, G-Protein-Coupled; 0/taste receptors, type 1; 138464-10-5/Gurmarin protein, Gymnema sylvestre; 9011-97-6/Cholecystokinin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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