The influence of myosin regulatory light chain phosphorylation on the contractile performance of fatigued mammalian skeletal muscle

ABSTRACT 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.

Name thesis:degree_name

M.Sc. Applied Health Sciences

Level thesis:degree_level

Masters

Discipline thesis:degree_discipline

Faculty of Applied Health Sciences

Department dc:contributor.department

Applied Health Sciences Program

Grantor

Brock University

Year dc:date.issued

2009

Author dc:creator

• Gittings, William J.

• Muscle contraction.
• Myosin.

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/10464/2921

OAI identifier oai:identifier

oai:brocku.scholaris.ca:10464/2921