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dc.contributor.authorDunford, Emily.en_US
dc.date.accessioned2010-02-16T15:45:58Z
dc.date.available2010-02-16T15:45:58Z
dc.date.issued2009-02-16T15:45:58Z
dc.identifier.urihttp://hdl.handle.net/10464/2914
dc.description.abstractPyruvate dehydrogenase (PDH) plays an important role in regulating carbohydrate oxidation in skeletal muscle. PD H is deactivated by a set of PD H kinases (PD K 1-4) with PDK2 and 4 being the predominant isoforms in skeletal muscle. PDK2 is highly sensitive to pyruvate inhibition, and is the most abundant isoform, while PDKI and 4 protein content are normally lower. This study examined the PDK isoform content and PDHa activation in muscle at rest and 10 and 40 Hz stimulation from PDK2 knockout (PDK2KO) mice to delineate the role of PDK2 in activating the PDH complex during low and moderate intensity muscle contraction. PDHa activity was lower in PDK2KO mice during contraction while total PDK actitvity was -4 fold lower. PDK4 protein was not different, however PDKI partially compensated for the lack of PDK2 and was -56% higher than WT. PDKI is a very potent inhibitor of the PDH complex due to its phosphorylation site specificity and allosteric regulation. These results suggest that the site specificity and allosteric regulatory properties of the individual PDK isoforms are more important than total PDK activity in determining transformation of the complex and PDHa activity during acute muscle contraction.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectMuscles--Metabolism.en_US
dc.subjectPyruvate kinase.en_US
dc.subjectMuscle contraction.en_US
dc.titlePyruvate dehydrogenase activity in response to skeletal muscle contraction at two stimulation frequencies in pyruvate dehydrogenase kinase 2 knockout miceen_US
dc.typeElectronic Thesis or Dissertationen_US
dc.degree.nameM.Sc. Applied Health Sciencesen_US
dc.degree.levelMastersen_US
dc.contributor.departmentApplied Health Sciences Programen_US


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