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dc.contributor.authorGittings, William J.en_US
dc.date.accessioned2010-02-16T15:46:01Z
dc.date.available2010-02-16T15:46:01Z
dc.date.issued2009-02-16T15:46:01Z
dc.identifier.urihttp://hdl.handle.net/10464/2921
dc.description.abstractABSTRACT The myosm regulatory light chain (RLC) of type II fibres is phosphorylated by Ca2+ -calmodulin dependent myosin light chain kinase (skMLCK) during muscular activation. The purpose of this study was to explore the effect of skMLCK gene ablation on the fatigability of mouse skeletal muscles during repetitive stimulation. The absence of myosin RLC phosphorylation in skMLCK knockout muscles attenuated contractile performance without a significant metabolic cost. Twitch force was potentiated to a greater extent in wildtype muscles until peak force had diminished to ~60% of baseline (37.2 ± 0.05% vs. 14.3 ± 0.02%). Despite no difference in peak force (Po) and shortening velocity (Vo), rate of force development (+dP/dt) and shortening-induced deactivation (SID) were almost two-fold greater in WT muscles. The present results demonstrate that myosin RLC phosphorylation may improve contractile performance during fatigue; providing a contractile advantage to working muscles and protecting against progressive fatigue.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectMuscle contraction.en_US
dc.subjectMyosin.en_US
dc.titleThe influence of myosin regulatory light chain phosphorylation on the contractile performance of fatigued mammalian 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
refterms.dateFOA2021-07-30T01:50:08Z


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