Residual force enhancement has been observed consistently in skeletal muscles. Despite an abundance of experimental observations, there has been no information about the metabolic cost of the force observed after stretch. Our aim was to investigate the energy cost of force production after active stretch in skinned fibres isolated from rabbit psoas muscle, by quantifying the ATPase activity using an enzyme-coupled assay. Fibres were actively stretched from an average sarcomere length of 2.4 μm to average sarcomere lengths of 2.8 and 3.2 μm. Purely isometric reference contractions were performed at average sarcomere lengths of 2.8 and 3.2 μm. Simultaneously with the force measurements, the ATP cost per unit of force produced was measured during the last 40 s of isometric contraction. Results showed that ATPase activity per unit of force was reduced by 17.2±4.1% in the isometric contractions after active stretch, compared to the purely isometric contraction at the corresponding lengths for both stretch magnitudes. Fibres stretched to an average sarcomere length of 3.2 μm showed a higher reduction in ATPase activity per unit of force compared to fibres stretched to an average sarcomere length of 2.8 μm (20.7±4.4 versus 12.4±3.2% respectively). Passive force enhancement was observed in all fibres and was correlated with the decrease in ATPase activity. No difference in stiffness was observed between reference and active stretch contractions. These results suggest that skeletal muscles become more efficient after stretch, either by increasing the amount of force produced per cross bridge or by engaging a passive element.
Keywords:
ATPase activity; Residual force enhancement; Passive force enhancement; Cross bridge cycling; Stiffness; Force per cross bridge; Titin; Metabolic cost; Evolution