Influence of V1 and V3 isomyosins on the mechanical behaviour of rat papillary muscle as studied by pseudo-random binary noise modulated length perturbations.

Abstract

Experiments were done on four-week-old rats, containing biochemically verified V1 only, and thyroidectomized adult rats, treated with propylthiouracil, verified to contain V3 only. Contracture tension was induced in isolated papillary muscles either by high potassium solution or 0.5 mmol l-1 Ba2+. Small amplitude length perturbations with peak-to-peak value not exceeding 0.15% L0 were applied to the activated muscle. Both the applied length perturbations and the corresponding resulting force changes were analysed by computer for dynamic stiffness and phase values. In order to reduce data acquisition time, pseudo-random binary noise length changes, rather than the conventional sinusoidal length changes, were used. The plot of the dynamic stiffness against frequency displays a minimum, akin to a resonance phenomenon. The frequency, fmin, at which this resonance occurs, reflects crossbridge kinetics. It was found that the fmin values for the two types of papillary muscles differed by a factor of two. Experiments were also done on chemically skinned muscles containing V1 or V3 isomyosin activated by different concentrations of either barium or calcium ions. It was found that fmin values of skinned fibres were higher than those obtained from intact fibres. However, for each type of muscle the fmin was independent of the activator used as well as the level of activation. The ratio of fmin for V3 to that for V1 remained the same as for intact preparations. We conclude that the difference in mechanical parameters did not arise a possible difference in excitation-contraction coupling mechanism, but rather is a difference in the dynamic properties of the two types of crossbridges.