Literature DB >> 19765710

Sarcomere dynamics in skeletal muscle myofibrils during isometric contractions.

Ivan Pavlov1, Rowan Novinger, Dilson E Rassier.   

Abstract

The main goal of this study was to evaluate the dynamics of sarcomeres during isometric activation of skeletal muscle myofibrils. Rabbit psoas myofibrils (n=14) were attached between a pair of cantilevers for force measurements at one side and a rigid glass needle at the other side, and their images were used for measurements of individual sarcomere lengths (SL) during contractions. Myofibrils were set at average SL between 2.13 and 3.06 microm, and were activated and held isometric for 20-35s during which SL and force were continuously measured. SL dispersion increased from the rest state to activation, but it remained mostly constant during the activation period. Even with the length non-uniformity developed during myofibril activation, most sarcomeres stabilized their length changes during the isometric contraction. As a result, sarcomeres contracted at different degrees of filament overlap while producing similar forces. When the myofibrils were separated in two groups that produced force at averaged short (< or =2.5 microm) or long (> or =2.5 microm) SL, the initial non-uniformity was greater in long lengths, but changes observed in sarcomeres during the activation period were similar, suggesting that sarcomere stability is not length-dependent.

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Year:  2009        PMID: 19765710     DOI: 10.1016/j.jbiomech.2009.08.011

Source DB:  PubMed          Journal:  J Biomech        ISSN: 0021-9290            Impact factor:   2.712


  11 in total

Review 1.  The mechanisms of the residual force enhancement after stretch of skeletal muscle: non-uniformity in half-sarcomeres and stiffness of titin.

Authors:  Dilson E Rassier
Journal:  Proc Biol Sci       Date:  2012-04-25       Impact factor: 5.349

2.  The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.

Authors:  Anabelle S Cornachione; Felipe Leite; Maria Angela Bagni; Dilson E Rassier
Journal:  Am J Physiol Cell Physiol       Date:  2015-09-24       Impact factor: 4.249

3.  A new experimental model for force enhancement: steady-state and transient observations of the Drosophila jump muscle.

Authors:  Ryan A Koppes; Douglas M Swank; David T Corr
Journal:  Am J Physiol Cell Physiol       Date:  2015-08-19       Impact factor: 4.249

4.  Sarcomere length non-uniformities dictate force production along the descending limb of the force-length relation.

Authors:  Ricarda Haeger; Felipe de Souza Leite; Dilson E Rassier
Journal:  Proc Biol Sci       Date:  2020-10-28       Impact factor: 5.349

5.  Length-dependent Ca2+ activation in skeletal muscle fibers from mammalians.

Authors:  Dilson E Rassier; Fábio C Minozzo
Journal:  Am J Physiol Cell Physiol       Date:  2016-05-25       Impact factor: 4.249

Review 6.  Sarcomere Length Nonuniformity and Force Regulation in Myofibrils and Sarcomeres.

Authors:  Felipe de Souza Leite; Dilson E Rassier
Journal:  Biophys J       Date:  2020-11-18       Impact factor: 4.033

7.  Force produced after stretch in sarcomeres and half-sarcomeres isolated from skeletal muscles.

Authors:  Fábio C Minozzo; Bruno M Baroni; José A Correa; Marco A Vaz; Dilson E Rassier
Journal:  Sci Rep       Date:  2013       Impact factor: 4.379

8.  Sarcomere Lengths Become More Uniform Over Time in Intact Muscle-Tendon Unit During Isometric Contractions.

Authors:  Eng Kuan Moo; Walter Herzog
Journal:  Front Physiol       Date:  2020-05-12       Impact factor: 4.566

9.  The role of sarcomere length non-uniformities in residual force enhancement of skeletal muscle myofibrils.

Authors:  Kaleena Johnston; Azim Jinha; Walter Herzog
Journal:  R Soc Open Sci       Date:  2016-03-30       Impact factor: 2.963

10.  Titin-mediated thick filament activation stabilizes myofibrils on the descending limb of their force-length relationship.

Authors:  Gudrun Schappacher-Tilp
Journal:  J Sport Health Sci       Date:  2018-05-17       Impact factor: 7.179

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