title: Measured and modeled properties of mammalian skeletal muscle. I. The effects of post-activation potentiation on the time course and velocity dependencies of force production.
abstract: Activation of mammalian fast-twitch skeletal muscle induces a persistent effect known as post-activation potentiation (PAP), classically defined as an increase in force production at sub-maximal levels of activation. The underlying mechanism is thought to be phosphorylation of the myosin regulatory light chain (MRLC), which leads to an increase in the rate constant for cross-bridge attachment (Sweeney et al., 1993). If true, this suggests the hypothesis that other contractile properties should be affected during PAP. Using a feline fast-twitch whole-muscle preparation (caudofemoralis) at 37 degrees C, we observed that PAP greatly increased tetanic forces during active lengthening decreased isometric tetanic rise times and delayed isometric tetanic force relaxation. The first two of these effects were length dependent with a greater effect occurring at shorter lengths. These findings confirmed that PAP has other functionally important effects beyond a simple increase in sub-maximal isometric forces. Furthermore, length was found to have an effect independent of PAP on the shortening half of the FV relationship (less force was produced at longer lengths) and on the rate of force relaxation during the later stages of isometric tetanic force decay (slower relaxation at longer lengths). All of these findings can be explained with a simplified, two-state model of cross-bridge dynamics that accounts for the interaction of both interfilament spacing and MRLC phosphorylation on the apparent rate constants for cross-bridge attachment and detachment. These findings are largely consistent with data collected previously from reduced preparations such as skinned fibers at cold, unphysiological temperatures (e.g. 5 degrees C). One finding that could not be explained by our model was that twitch fall times in the dispotentiated state were parabolically correlated with length, whereas in the potentiated state the relationship was linear. The time course of decay of this effect did not follow the time course of force dispotentiation, suggesting that there are other activation-dependent processes occurring in parallel with MRLC phosphorylation.
authors.affiliation: Division of Biology, California Institute of Technology, Pasadena 91125, USA.
authors.forename: I E
authors.initials: IE
authors.lastname: Brown
authors.forename: G E
authors.initials: GE
authors.lastname: Loeb
mesh_terms: D008841:Actin Cytoskeleton / Q000502:physiology; D000200:Action Potentials / Q000502:physiology; D000818:Animals; D002415:Cats; D005260:Female; D007537:Isometric Contraction / Q000502:physiology*; D008297:Male; D008322:Mammals; D018656:Muscle Fibers, Fast-Twitch / Q000502:physiology*; D018657:Muscle Fibers, Slow-Twitch / Q000502:physiology; D018482:Muscle, Skeletal / Q000166:cytology / Q000502:physiology*; D018994:Myosin Light Chains / Q000378:metabolism; D010766:Phosphorylation; D013997:Time Factors
chemical_list: D018994:Myosin Light Chains