Characterization of human bitter taste receptor T2R1

dc.contributor.authorUpadhyaya, Jasbir Deol
dc.contributor.examiningcommitteeParkinson, Fiona (Pharmacology and Therapeutics) Bhullar, Raj (Oral Biology)en
dc.contributor.supervisorChelikani, Prashen (Oral Biology)en
dc.date.accessioned2010-09-10T16:12:57Z
dc.date.available2010-09-10T16:12:57Z
dc.date.issued2010-09-10T16:12:57Z
dc.degree.disciplineOral Biologyen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractBitter taste signaling in humans is mediated by a group of 25 bitter receptors (T2Rs) that belong to the G-protein coupled receptor (GPCR) family. Previously, several bitter peptides were isolated and characterized from bitter tasting food protein derived extracts, such as pea protein and soya bean extracts. However, their molecular targets in humans were poorly characterized. In this study, we tested the ability of the bitter tasting tri- and di-peptides to activate the human bitter receptor, T2R1. Using a heterologous expression system, T2R1 gene was transiently expressed in C6-glioma cells and changes in intracellular calcium were measured following addition of the peptides. We found that the bitter tasting tri-peptides are more potent in activating T2R1 than the di-peptides tested. Furthermore, to elucidate the potential ligand binding pocket of T2R1 we used homology molecular modeling. The ligand binding pocket in T2R1 is present on the extracellular surface of the receptor, and is formed by the transmembrane helices 1, 2, 3 and 7 and with extracellular loops 1 and 2.en
dc.description.noteOctober 2010en
dc.format.extent3586648 bytes
dc.format.mimetypeapplication/pdf
dc.identifier.citationUpadhyaya, Jasbir (2010) BBRC 398 (2) : 331-335en
dc.identifier.urihttp://hdl.handle.net/1993/4129
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.subjectT2R1en
dc.subjectPeptidesen
dc.subjectMolecular modelingen
dc.subjectC6 glial cellsen
dc.titleCharacterization of human bitter taste receptor T2R1en
dc.typemaster thesisen_US
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