title: Tension and stiffness of frog muscle fibres at full filament overlap.
abstract: Stiffness measurements in activated skeletal muscle fibres are often used as one means of estimating the number of attached crossbridges on the assumption that myofilament compliances do not contribute significantly to the fibre compliance. This assumption was tested by studying the effects of sarcomere length on fibre stiffness in the plateau region of the length-tension diagram (from 1.96 to 2.16 microns sarcomere length in the tibialis anterior muscle of the frog). Lengthening of the sarcomere across this region in fact, produces only an increase in the proportion of actin filament free from cross-bridges without altering the amount of effective overlap; no change in fibre stiffness is therefore expected if actin filaments are perfectly rigid. The results show that while tetanic tension remained constant within 1.5%, as the sarcomere length was increased from 1.96 to 2.16 microns fibre stiffness decreased by about 4%, indicating that a significant proportion of sarcomere compliance is localized in the actin filaments. A simple model based on the sliding filament theory was used in order to calculate the relative contribution of actin filaments to fibre compliance. In the model it was assumed that fibre compliance resulted from the combination of crossbridge compliance (distributed over the overlap zone) in series with thin filament and tendon compliances. The calculations show that the experimental data could be adequately predicted only assuming that about 19% of sarcomere compliance is due to actin filament compliance.
authors: Dipartimento di Scienze Fisiologiche, Università degli Studi di Firenze, Italy.
authors: M A
authors: MA
authors: Bagni
authors: G
authors: G
authors: Cecchi
authors: F
authors: F
authors: Colomo
authors: C
authors: C
authors: Poggesi
mesh_terms: D000199:Actins / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D001696:Biomechanical Phenomena; D066298:In Vitro Techniques; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology*; D011893:Rana esculenta; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure
chemical_list: D000199:Actins