Huxley_1985_J.Exp.Biol_115_17

The basic features of the sliding-filament crossbridge mechanism are reviewed briefly, and some recent objections involving supposed changes in A-filament lengths are discussed. X-ray diffraction studies on live muscles show no sign of a decrease in axial spacing during contraction, and it is unlikely that a stepwise shortening or depolymerization of A-filaments would provide a plausible contraction mechanism. Thus electron microscope observations which occasionally are reported to show such length changes probably arise from experimental artefact, of which there are many sources. The factors which govern tension and speed in muscle contraction are described. Since all vertebrate striated muscles which have been studied have A-bands of at least approximately the same length, they are likely to have rather similar maximum isometric tensions. The design probably matches this tension to the strength of the filaments themselves. The large variations in shortening speeds between different muscles and different animals arise because of corresponding variations in the rates of particular steps in the crossbridge cycle and in the rate of ATP splitting by the actin-myosin complex involved. Questions concerning the nature and the speed of the activation mechanism are also discussed.