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dc.contributor.authorVandommele, Cody
dc.date.accessioned2013-02-12T15:49:38Z
dc.date.available2013-02-12T15:49:38Z
dc.date.issued2013-02-12
dc.identifier.urihttp://hdl.handle.net/10464/4195
dc.description.abstractThe purpose of this study was to examine the effect of hyper-osmotic stress on protein turnover in skeletal muscle tissue using an established in-vitro model. Rat EDL muscles were incubated in either hyper-osmotic (400 ± 10 Osm) or isoosmotic (290 ± 10 Osm) custom-modified media (Gibco). L-[14C]-U-phenylalanine (n=8) and cycloheximide (n=8) were used to quantify protein synthesis and degradation, respectively. Western blotting analyses was performed to determine the activation of protein synthesis and degradation pathways. During hyperosmotic stress, protein degradation increased (p<0.05), while protein synthesis was decreased (p<0.05) as compared to the iso-osmotic condition. The decline in protein synthesis was accompanied by a decrease (p<0.05) in p70s6 kinase phosphorylation, while the increase in protein degradation was associated with an increase (p<0.05) in autolyzed calpain. Therefore, hyper-osmotic extracellular stress results in an intracellular catabolic environment in mammalian skeletal muscle tissue.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectosmoticen_US
dc.subjectstressen_US
dc.subjectskeletal muscleen_US
dc.subjectprotein turnoveren_US
dc.titleRegulation of Protein Turnover during Hyper-osmotic Stress in Skeletal Muscleen_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
dc.degree.disciplineFaculty of Applied Health Sciencesen_US


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