Examining the effects of SERCA2a acetylation in the heart

dc.contributor.authorSusser, Shanel
dc.contributor.examiningcommitteeCzubryt, Michael (Physiology and Pathophysiology) Gardiner, Phillip (Physiology and Pathophysiology) Dolinsky, Vernon (Pharmacology and Therapeutics)en_US
dc.contributor.supervisorDuhamel, Todd (Physiology and Pathophysiology)en_US
dc.date.accessioned2016-01-14T17:01:23Z
dc.date.available2016-01-14T17:01:23Z
dc.date.issued2015
dc.degree.disciplinePhysiology and Pathophysiologyen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractThe sarcoplasmic reticulum Ca2+-ATPase (SERCA2a) is responsible for calcium transport in the heart and its dysfunction in heart disease and diabetes make it a target for treatment strategies. SERCA2a structure can be modified post-translationally by the addition of an acetyl protein via acetylation. Sirtuin3 (SIRT) is a deacetylase, which may interact with SERCA2a to reverse its acetylation. The aim of this study was to determine if SERCA2a function is altered by acetylation, if this occurs in the diabetic heart, and if SIRT3 influences SERCA2a acetylation. Our data indicates that modification to three SERCA2a acetylation sites impairs its activity in a cell culture model and that SERCA2a acetylation occurs at higher levels in the diabetic heart. Furthermore, SERCA2a is acetylated at higher levels in absence of SIRT3, suggesting that SIRT3 activity influences SERCA2a. Our data identifies possible therapeutic strategies to target and reduce SERCA2a acetylation in the diabetic heart.en_US
dc.description.noteFebruary 2016en_US
dc.identifier.urihttp://hdl.handle.net/1993/31073
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.subjectSERCA2aen_US
dc.subjectAcetylationen_US
dc.subjectHearten_US
dc.subjectSirtuin3en_US
dc.titleExamining the effects of SERCA2a acetylation in the hearten_US
dc.typemaster thesisen_US
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