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dc.contributor.authorBunda, Jordan
dc.date.accessioned2015-09-22T14:16:13Z
dc.date.available2015-09-22T14:16:13Z
dc.identifier.urihttp://hdl.handle.net/10464/7234
dc.description.abstractActivated by elevations in myoplasmic calcium concentration, myosin light chain kinase (skMLCK) phosphorylates the regulatory light chains (RLCs) of fast muscle myosin. This covalent modification potentiates force production, but requires an investment of ATP. Our objective was to investigate the effect of RLC phosphorylation on the contractile economy (mechanical output:metabolic input) of fast twitch skeletal muscle. Extensor digitorum longus muscles isolated from Wildtype and skMLCK-/- mice mounted in vitro (25°C) were subjected to repetitive low-frequency stimulation (10Hz,15s) known to cause activation of skMLCK, and staircase potentiation of force. With a 3-fold increase in RLC phosphate content, Wildtype generated 44% more force than skMLCK-/- muscles over the stimulation period (P = .002), without an accompanied increase in energy cost (P = .449). Overall, the contractile economy of Wildtype muscles, with an intact RLC phosphorylation mechanism, was 73% greater than skMLCK /- muscles (P = .043), demonstrating an important physiological function of skMLCK during repetitive contractile activity.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectSkeletal muscleen_US
dc.subjectPotentiationen_US
dc.subjectMyosin light chain kinaseen_US
dc.subjectEconomyen_US
dc.subjectMyosin regulatory light chainen_US
dc.titleMyosin Regulatory Light Chain Phosphorylation and Its Effect on the Contractile Economy of Mouse Fast 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
refterms.dateFOA2021-07-16T10:30:31Z


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