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rdf:type |
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lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0033684,
umls-concept:C0039337,
umls-concept:C0205246,
umls-concept:C0391871,
umls-concept:C0596235,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1424635,
umls-concept:C1515655,
umls-concept:C1537081,
umls-concept:C1963578,
umls-concept:C1999216
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pubmed:issue |
5
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pubmed:dateCreated |
2008-9-22
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pubmed:abstractText |
In a search for sweet taste receptor interacting proteins, we have identified the calcium- and integrin-binding protein 1 (CIB1) as specific binding partner of the intracellular carboxyterminal domain of the rat sweet taste receptor subunit Tas1r2. In heterologous human embryonic kidney 293 (HEK293) cells, the G protein chimeras Galpha(16gust44) and Galpha(15i3) link the sweet taste receptor dimer TAS1R2/TAS1R3 to an inositol 1,4,5-trisphosphate (InsP3)-dependent Ca2+ release pathway. To demonstrate the influence of CIB1 on the cytosolic Ca2+ concentration, we used sweet and umami compounds as well as other InsP3-generating ligands in FURA-2-based Ca2+ assays in wild-type HEK293 cells and HEK293 cells expressing functional human sweet and umami taste receptor dimers. Stable and transient depletion of CIB1 by short-hairpin RNA increased the Ca2+ response of HEK293 cells to the InsP3-generating ligands ATP, UTP and carbachol. Over-expression of CIB1 had the opposite effect as shown for the sweet ligand saccharin, the umami receptor ligand monosodium glutamate and UTP. The CIB1 effect was dependent on the thapsigargin-sensitive Ca2+ store of the endoplasmic reticulum (ER) and independent of extracellular Ca2+. The function of CIB1 on InsP3-evoked Ca2+ release from the ER is most likely mediated by its interaction with the InsP3 receptor. Thus, CIB1 seems to be an inhibitor of InsP3-dependent Ca2+ release in vivo.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/CIB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbachol,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fura-2,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Triphosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1471-4159
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2249-62
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18627437-Adenosine Triphosphate,
pubmed-meshheading:18627437-Animals,
pubmed-meshheading:18627437-Calcium,
pubmed-meshheading:18627437-Calcium Signaling,
pubmed-meshheading:18627437-Calcium-Binding Proteins,
pubmed-meshheading:18627437-Carbachol,
pubmed-meshheading:18627437-Cell Line,
pubmed-meshheading:18627437-Down-Regulation,
pubmed-meshheading:18627437-Endoplasmic Reticulum,
pubmed-meshheading:18627437-Enzyme Inhibitors,
pubmed-meshheading:18627437-Fura-2,
pubmed-meshheading:18627437-Humans,
pubmed-meshheading:18627437-Indicators and Reagents,
pubmed-meshheading:18627437-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:18627437-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:18627437-Ligands,
pubmed-meshheading:18627437-RNA Interference,
pubmed-meshheading:18627437-Rats,
pubmed-meshheading:18627437-Sensory Receptor Cells,
pubmed-meshheading:18627437-Taste,
pubmed-meshheading:18627437-Taste Buds,
pubmed-meshheading:18627437-Tongue,
pubmed-meshheading:18627437-Uridine Triphosphate
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pubmed:year |
2008
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pubmed:articleTitle |
Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3-dependent Ca2+ release in vivo.
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pubmed:affiliation |
Institut für Biochemie und Molekularbiologie II, Molekulare Zellbiologie, Zentrum für Experimentelle Medizin, Hamburg, Germany
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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