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dc.contributor.authorEngland, Eric M.en_US
dc.date.accessioned2015-07-22T08:01:00Z
dc.date.available2015-07-22T08:01:00Z
dc.date.issued2015-07-21en_US
dc.identifier.othervt_gsexam:6050en_US
dc.identifier.urihttp://hdl.handle.net/10919/54580
dc.description.abstractOnce an animal is harvested for meat, skeletal muscle attempts to maintain ATP at or near antemortem levels. To maintain ATP levels postmortem, stored glycogen is catabolized to produce ATP through glycolysis and possibly oxidative metabolism. Hydrolysis of the produced ATP acidifies muscle until an ultimate pH is reached. The ultimate pH of meat directly impacts the quality characteristics of color, texture, and water holding capacity. Therefore, our research intends to describe the contributions glycolysis and oxidative metabolism play in determining ultimate pH and fresh meat quality. Traditionally, glycogen content at death was thought to be responsible for dictating ultimate pH. This was especially true in oxidative muscle with limited glycogen stores. Yet, our research indicated that in the presence of excess glycogen, oxidative muscle maintains a high ultimate pH. Rather, pH inactivation of phosphofructokinase is responsible for terminating postmortem glycolysis and brackets ultimate pH between 5.9 – 5.5. Meat with a pH below this range is uncommon. However, AMPK γ3R200Q mutant pigs produce meat with an ultimate pH near 5.3. Due to lower AMP deaminase abundance in their muscle, AMP levels are elevated late postmortem. Because AMP is a potent activator of phosphofructokinase, the aberrant meat quality from AMPK γ3R200Q mutant pigs is caused by extended postmortem glycolysis. Combined, these data further our understanding of the factors that contribute to the formation of fresh meat quality. We also characterized AMPK γ3R200Q muscle by investigating antemortem skeletal muscle lactate transport. Lactate is transported in or out of tissues by proton-linked iii monocarboxylate transporters (MCTs). Previous reports indicated that acute activation of AMPK increased monocarboxylate transporter expression in skeletal muscle of other species. Yet, it was unknown the impact chronic activation of AMPK will have on MCT1, MCT2, and MCT4 expression in pigs. Compared to wild-type pigs, the longissimus lumborum of AMPK γ3R200Q pigs increased both MCT2 and MCT4 protein expression. Our data suggest glycolytic skeletal muscle from the AMPK γ3R200Q pigs has increased capacity for antemortem lactate export from muscle and possibly increased pyruvate transport into the mitochondria.en_US
dc.format.mediumETDen_US
dc.publisherVirginia Techen_US
dc.rightsThis Item is protected by copyright and/or related rights. Some uses of this Item may be deemed fair and permitted by law even without permission from the rights holder(s), or the rights holder(s) may have licensed the work for use under certain conditions. For other uses you need to obtain permission from the rights holder(s).en_US
dc.subjectpork qualityen_US
dc.subjectskeletal muscleen_US
dc.subjectultimate pHen_US
dc.subjectmitochondriaen_US
dc.subjectAMPK γ3R200Qen_US
dc.titlePostmortem metabolism in porcine skeletal muscleen_US
dc.typeDissertationen_US
dc.contributor.departmentAnimal and Poultry Sciencesen_US
dc.description.degreePh. D.en_US
thesis.degree.namePh. D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen_US
thesis.degree.disciplineAnimal and Poultry Sciencesen_US
dc.contributor.committeechairGerrard, David E.en_US
dc.contributor.committeememberSobrado, Pabloen_US
dc.contributor.committeememberRhoads, Robert P.en_US
dc.contributor.committeememberPuolanne, T. Eero J.en_US


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