Reversal of the myosin power stroke induced by fast stretching of intact skeletal muscle fibers.

Biophysical Journal
Barbara ColombiniM Angela Bagni

Abstract

Force generation and movement in skeletal muscle result from a cyclical interaction of overlapping myosin and actin filaments that permits the free energy of ATP hydrolysis to be converted into mechanical work. The rapid force recovery that occurs after a step release imposed on a muscle is thought to result from a synchronized tilting of myosin lever arms toward a position of lower free energy (the power stroke). We investigated the power stroke mechanism in intact muscle fibers of Rana esculenta using a fast stretch to detach forcibly cross-bridges. Stretches were applied either with or without a conditioning step release. Cross-bridge rupture tension was not significantly influenced by the release, whereas sarcomere elongation at the rupture point increased immediately after the release and returned to the prerelease condition within 15-20 ms, following a slower time course compared to the recovery of tension. These observations suggest that the rupture force of a bridge is unaltered by a conditioning release, but rupture must first be preceded by a power stroke reversal, which restores the prepower stroke state. The sarcomere extension at the rupture point indicates both the extent of this power stroke reversal and the time...Continue Reading

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Feb 29, 2008·American Journal of Physiology. Cell Physiology·Barbara ColombiniM Angela Bagni
Mar 28, 2009·Proceedings of the National Academy of Sciences of the United States of America·Julien S Davis, Neal D Epstein

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Citations

Jun 23, 2015·Biochemical and Biophysical Research Communications·Fábio C MinozzoDilson E Rassier
May 12, 2015·BioMed Research International·Alf MånssonGeorgios Tsiavaliaris
Aug 20, 2010·American Journal of Physiology. Cell Physiology·Fabio C Minozzo, Dilson E Rassier
Jan 9, 2013·Journal of Muscle Research and Cell Motility·Marta NocellaBarbara Colombini
Nov 7, 2019·Chemical Reviews·Julien Robert-PaganinAnne Houdusse

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