A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization

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dc.contributor.advisorDavidson, James Sen_ZA
dc.contributor.authorPawson, Adam Jamesen_ZA
dc.date.accessioned2018-01-09T14:10:18Z
dc.date.available2018-01-09T14:10:18Z
dc.date.issued1999en_ZA
dc.description.abstractThe G protein-coupled receptor (GPCR) family is the largest group of homologous proteins in the human genome. GPCRs are of prime physiological and medical importance as the actions of a wide range of hormones and drugs are mediated by these receptors. The gonadotropin-releasing hormone (GnRH) receptor is a member of the GPCR family, and plays a central role in the reproductive system. GnRH analogues are used therapeutically in a number of human disorders. All GPCRs contain 7 largely α-helical transmembrane domains. An arginine residue located at the cytosolic boundary of the third transmembrane domain is conserved in all members of the rhodopsin-like subfamily of GPCRs, and is nearly always preceded by an acidic residue (DR motif). This arginine has been proposed to play a critical role in receptor activation. In this thesis, the effects of mutating these residues (Asp¹³⁸ and Arg¹³⁹ respectively, in the mouse GnRH receptor) to neutral amide residues, on coupling of the mouse GnRH receptor, were examined. In addition, the relationship of coupling to internalization in these mutant receptors was explored.en_ZA
dc.identifier.apacitationPawson, A. J. (1999). <i>A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology. Retrieved from http://hdl.handle.net/11427/26779en_ZA
dc.identifier.chicagocitationPawson, Adam James. <i>"A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1999. http://hdl.handle.net/11427/26779en_ZA
dc.identifier.citationPawson, A. 1999. A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Pawson, Adam James AB - The G protein-coupled receptor (GPCR) family is the largest group of homologous proteins in the human genome. GPCRs are of prime physiological and medical importance as the actions of a wide range of hormones and drugs are mediated by these receptors. The gonadotropin-releasing hormone (GnRH) receptor is a member of the GPCR family, and plays a central role in the reproductive system. GnRH analogues are used therapeutically in a number of human disorders. All GPCRs contain 7 largely α-helical transmembrane domains. An arginine residue located at the cytosolic boundary of the third transmembrane domain is conserved in all members of the rhodopsin-like subfamily of GPCRs, and is nearly always preceded by an acidic residue (DR motif). This arginine has been proposed to play a critical role in receptor activation. In this thesis, the effects of mutating these residues (Asp¹³⁸ and Arg¹³⁹ respectively, in the mouse GnRH receptor) to neutral amide residues, on coupling of the mouse GnRH receptor, were examined. In addition, the relationship of coupling to internalization in these mutant receptors was explored. DA - 1999 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 1999 T1 - A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization TI - A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization UR - http://hdl.handle.net/11427/26779 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/26779
dc.identifier.vancouvercitationPawson AJ. A mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalization. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1999 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/26779en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDivision of Chemical Pathologyen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherChemical Pathologyen_ZA
dc.titleA mutational analysis of the roles of cytoplasmic domains of the gonadotropin-releasing hormone receptor in coupling and internalizationen_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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