Sarcomere Stiffness during Stretching and Shortening of Rigor Skeletal Myofibrils

Biophys J. 2017 Dec 19;113(12):2768-2776. doi: 10.1016/j.bpj.2017.10.007.

Abstract

In this study, we measured the stiffness of skeletal muscle myofibrils in rigor. Using a custom-built atomic force microscope, myofibrils were first placed in a rigor state then stretched and shortened at different displacements (0.1-0.3 μm per sarcomere) and nominal speeds (0.4 and 0.8 μm/s). During stretching, the myofibril stiffness was independent of both displacement and speed (average of 987 nN/μm). During shortening, the myofibril stiffness was independent of displacement, but dependent on speed (1234 nN/μm at 0.4 μm/s; 1106 nN/μm at 0.8 μm/s). Furthermore, the myofibril stiffness during shortening was greater than that during stretching and the difference depended on speed (31% at 0.4 μm/s; 8% at 0.8 μm/s). The results suggest that the myofibrils exhibit nonlinear viscoelastic properties that may be derived from myofibril filaments, similar to what has been observed in muscle fibers.

MeSH terms

  • Animals
  • Biomechanical Phenomena
  • Cytoskeletal Proteins / metabolism
  • Female
  • Mechanical Phenomena*
  • Microscopy, Atomic Force
  • Rabbits
  • Sarcomeres / metabolism*

Substances

  • Cytoskeletal Proteins