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dc.contributor.authorTrang, Amy
dc.contributor.authorAdams, Elizabeth
dc.contributor.authorAcevedo, Aja
dc.contributor.authorMiller, Donnyell
dc.contributor.authorFarooq, Maheen
dc.contributor.authorLittle, Lauren
dc.contributor.authorLambert, Nevin
dc.date.accessioned2018-02-12T17:19:35Z
dc.date.available2018-02-12T17:19:35Z
dc.date.issued2018-02-12
dc.date.submitted27-JAN-2018 10:18PM
dc.identifier.urihttp://hdl.handle.net/10675.2/621730
dc.descriptionPresentation given at the 19th Annual Phi Kappa Phi Student Research and Fine Arts Conferenceen
dc.description.abstractG protein-coupled receptors (GPCRs) are receptors that act in signal transduction pathways via activation of guanosine nucleotide-binding proteins, known as G proteins. An extra-cellular signal (a ligand) activates a receptor from outside the cell and working through a G protein, the external signal is transmitted inside the cell. There are four main classes of G proteins: Gs, Gi, Gqand G12. When activated, eachof these G protein types is responsible for a specific intracellular event, often determined by measuring how the concentration of a second messenger changes as a function of the concentration of the external signal. This indirect approach limits our understanding of the role of each type of G protein in signaling pathways. Our group is currently using Bioluminescence Resonance Energy Transfer (BRET) to directly measure G protein activation by GPCRs in response to external stimuli (includingboth endogenous and synthetic ligands). We have generated recombinant DNA for nanoluciferase fused to GPCRs in the serotonin (5-hydroxytryptamine, 5-HT) receptor family. These genetic fusions, along with fusions of yellow fluorescent protein and various G proteins were co-transfected into HEK293 cells for BRET assays. Initial results show that activation of receptors 5-HT1D and 5-HT1F with serotonin are coupled to Gi. Future studies will include a G protein profile for all twelve receptors in the serotonin family.
dc.subjectGPCRen
dc.subjectBRETen
dc.subject5-HT receptorsen
dc.titleCharacterization of Serotonin Receptors in Response to Ligand Binding Using BRETen
dc.typeOral Presentationen
dc.contributor.departmentDepartment of Biological Sciencesen
dc.contributor.departmentDepartment of Chemistry and Physicsen
dc.contributor.departmentDepartment of Pharmacology and Toxicologyen
dc.contributor.sponsorSpencer, Angieen
dc.contributor.sponsorDepartment of Chemistry and Physicsen
dc.contributor.affiliationAugusta Universityen
html.description.abstractG protein-coupled receptors (GPCRs) are receptors that act in signal transduction pathways via activation of guanosine nucleotide-binding proteins, known as G proteins. An extra-cellular signal (a ligand) activates a receptor from outside the cell and working through a G protein, the external signal is transmitted inside the cell. There are four main classes of G proteins: Gs, Gi, Gqand G12. When activated, eachof these G protein types is responsible for a specific intracellular event, often determined by measuring how the concentration of a second messenger changes as a function of the concentration of the external signal. This indirect approach limits our understanding of the role of each type of G protein in signaling pathways. Our group is currently using Bioluminescence Resonance Energy Transfer (BRET) to directly measure G protein activation by GPCRs in response to external stimuli (includingboth endogenous and synthetic ligands). We have generated recombinant DNA for nanoluciferase fused to GPCRs in the serotonin (5-hydroxytryptamine, 5-HT) receptor family. These genetic fusions, along with fusions of yellow fluorescent protein and various G proteins were co-transfected into HEK293 cells for BRET assays. Initial results show that activation of receptors 5-HT1D and 5-HT1F with serotonin are coupled to Gi. Future studies will include a G protein profile for all twelve receptors in the serotonin family.


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