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dc.contributor.supervisor Duhamel, Todd (Physiology and Pathophysiology) en_US
dc.contributor.author Susser, Shanel
dc.date.accessioned 2016-01-14T17:01:23Z
dc.date.available 2016-01-14T17:01:23Z
dc.date.issued 2015
dc.identifier.uri http://hdl.handle.net/1993/31073
dc.description.abstract The 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.subject SERCA2a en_US
dc.subject Acetylation en_US
dc.subject Heart en_US
dc.subject Sirtuin3 en_US
dc.title Examining the effects of SERCA2a acetylation in the heart en_US
dc.degree.discipline Physiology and Pathophysiology en_US
dc.contributor.examiningcommittee Czubryt, Michael (Physiology and Pathophysiology) Gardiner, Phillip (Physiology and Pathophysiology) Dolinsky, Vernon (Pharmacology and Therapeutics) en_US
dc.degree.level Master of Science (M.Sc.) en_US
dc.description.note February 2016 en_US


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