Functional characterization of naturally occurring mutant transglutaminase 2

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dc.contributor.authorSalter, Neil William
dc.contributor.examiningcommitteeDodd, Janice (Physiology) Nyomba, Gregoire (Physiology) Murphy, Leigh (Biochemistry and Medical Genetics)en_US
dc.contributor.supervisorMishra, Suresh (Physiology)en_US
dc.date.accessioned2011-09-01T19:21:19Z
dc.date.available2011-09-01T19:21:19Z
dc.date.issued2011-09-01
dc.degree.disciplinePhysiologyen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractTransglutaminase 2 (TG2) is a functionally and structurally complex ubiquitous protein. TG2 has Ca2+-dependent transamidating activity, can bind and hydrolyze ATP/GTP, function as a G-protein in intracellular signaling, and has reported kinase activity. TG2 knockout mice are observed to have impaired glucose-stimulated insulin secretion (GSIS). Three naturally occurring mutations, including Met330Arg, Ile331Asn, and Asn333Ser, have been reported in the TG2 protein and observed to be related with maturity onset diabetes of the young (MODY). Overexpression of the naturally occurring Myc-tag mutants in INS-1E cells generated a loss in GSIS compared to wild type-TG2 overexpression. Each mutant was shown to have diminished transamidation and kinase activities, along with altered GTP-binding which was responsive to glucose stimulation. Naturally occurring mutations in TG2 impact the transamidation, kinase, and GTP-binding functions of TG2. The GTP-binding function of TG2 has a significant impact on GSIS from pancreatic beta cells in addition to its transamidating activity.en_US
dc.description.noteOctober 2011en_US
dc.identifier.urihttp://hdl.handle.net/1993/4825
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.subjectTG2en_US
dc.subjectDiabetesen_US
dc.titleFunctional characterization of naturally occurring mutant transglutaminase 2en_US
dc.typemaster thesisen_US
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