Crossbridge and non-crossbridge contributions to force in shortening and lengthening muscle

Adv Exp Med Biol. 2010:682:207-21. doi: 10.1007/978-1-4419-6366-6_12.

Abstract

Analysis of tension responses to ramp length changes in muscle can provide important information about the crossbridge cycle. During a ramp length change, the force response of an active muscle shows an early change in slope (the P₁ transition) followed by a later, gradual change in slope (the P₂ transition). Modeling shows that the first transition reflects the tension change associated with the crossbridge power stroke in shortening and with its reversal in lengthening; the reduction in slope at the second transition occurs when most of the crossbridges (myosin heads) that were attached at the start of the ramp become detached; the steady tension during shortening is borne mainly by post-stroke heads whereas tension during lengthening is borne mostly by pre-stroke heads. After the P₂ transition, the tension reaches a steady level in the model whereas in the experiments the tension continues to increase during lengthening or to decrease during shortening; this tension change is seen at a wide range of sarcomere lengths and even when active force is reduced by a myosin inhibitor. It appears that some non-crossbridge components in muscle fibers stiffen upon activation and contribute to the continued tension rise during lengthening; release of such tension leads to tension decline during shortening. Thus, non-crossbridge visco-elasticity in sarcomeres may also contribute to energy storage and release during in situ muscle function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Animals
  • Male
  • Models, Biological
  • Muscle Contraction / physiology*
  • Muscle Relaxation / physiology*
  • Muscle, Skeletal / physiology*
  • Myosins / physiology
  • Rats
  • Sarcomeres / physiology
  • Stress, Mechanical

Substances

  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Myosins