C-protein limits shortening velocity of rabbit skeletal muscle fibres at low levels of Ca2+ activation.

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1. Effects on maximum shortening velocity (Vmax) due to partial extraction of C-protein were investigated in skinned fibres from rabbit psoas muscles. Up to 80% of endogenous C-protein was extracted, as assessed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of fibre segments obtained before and after the extraction protocol. Vmax was obtained at 15 degrees C by measuring the times required to take up various amounts of slack imposed at one end of the fibre. 2. During maximal activation with Ca2+, Vmax in control fibres was 4.26 +/- 0.16 (mean +/- S.E.M., n = 7) muscle lengths per second (ML/s). Following extraction of approximately 40% of endogenous C-protein, Vmax in these same fibres was 4.41 +/- 0.24 ML/s. 3. At sufficiently low levels of submaximal activation, high- and low-velocity phases of unloaded shortening were observed. Partial extraction of C-protein significantly increased Vmax in the low-velocity phase but had no effect on the high-velocity phase. The effect on low-velocity Vmax was fully reversed by re-addition of purified C-protein. 4. At low levels of activation, the amount of shortening to the break-point between the high- and low-velocity phases was not significantly affected by C-protein extraction. Under control conditions the average break-point was 85.6 +/- 3.1 nm/half-sarcomere, while 84.1 +/- 3.1 nm/half-sarcomere was obtained following partial extraction of C-protein. 5. These results are considered in terms of a model in which an internal load slows Vmax at low levels of activation once a given amount of active shortening has occurred. C-protein may contribute to this internal load either by binding to actin and myosin or by influencing mechanical properties of myosin cross-bridges.

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