Show simple item record

dc.contributor.authorChoptiany, Jonathan Robert
dc.date.accessioned2013-08-01T19:09:16Z
dc.date.available2013-08-01T19:09:16Z
dc.date.issued2013-08-01
dc.identifier.urihttp://hdl.handle.net/10464/4722
dc.description.abstractPyruvate dehydrogenase phosphatase (PDP) regulates carbohydrate oxidation through the pyruvate dehydrogenase (PDH) complex. PDP activates PDH, enabling increased carbohydrate flux towards oxidative energy production. In culture myoblasts, both PDP1 and PDP2 undergo covalent activation in response to insulin–stimulation by protein kinase C delta (PKCδ). Our objective was to examine the effect of insulin on PDP phosphorylation and PDH activation in skeletal muscle. Intact rat extensor digitorum longus muscles were incubated (oxygenated at 25°C, 1g of tension) for 30min in basal or insulin–stimulated (10 mU/mL) media. PDH activity increased 58% following stimulation, (p=0.057, n=11). Serine phosphorylation of PDP1 (p=0.047) and PDP2 (p=0.006) increased by 29% and 48%, respectively (n=8), and mitochondrial PKCδ protein content was enriched by 45% in response to stimulation (p=0.0009, n=8). These data suggest that the insulin–stimulated increase in PDH activity in whole tissue is mediated through mitochondrial migration of PKCδ and subsequent PDP phosphorylation.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectPyruvate Dehydrogenase Complexen_US
dc.subjectPyruvate Dehydrogenase Phosphataseen_US
dc.subjectSkeletal Muscle Metabolismen_US
dc.subjectInsulin Stimulationen_US
dc.titlePhosphorylation of Skeletal Muscle Pyruvate Dehydrogenase Phosphatase in Response to Insulin Stimulationen_US
dc.typeElectronic Thesis or Dissertationen
dc.degree.nameM.Sc. Applied Health Sciencesen_US
dc.degree.levelMastersen_US
dc.contributor.departmentApplied Health Sciences Programen_US
dc.degree.disciplineFaculty of Applied Health Sciencesen_US
dc.embargo.termsNoneen_US
refterms.dateFOA2021-08-08T02:20:30Z


Files in this item

Thumbnail
Name:
Brock_Choptiany_Jonathan_2013.pdf
Size:
4.829Mb
Format:
PDF
Description:
Masters Thesis

This item appears in the following Collection(s)

Show simple item record