Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies

  • Robert Stehle
  • Johannes Solzin
  • Bogdan Iorga
  • Corrado Poggesi
Muscle Physiology


Muscle contraction results from force-generating interactions between myosin cross-bridges on the thick filament and actin on the thin filament. The force-generating interactions are regulated by Ca2+ via specialised proteins of the thin filament. It is controversial how the contractile and regulatory systems dynamically interact to determine the time course of muscle contraction and relaxation. Whereas kinetics of Ca2+-induced thin-filament regulation is often investigated with isolated proteins, force kinetics is usually studied in muscle fibres. The gap between studies on isolated proteins and structured fibres is now bridged by recent techniques that analyse the chemical and mechanical kinetics of small components of a muscle fibre, subcellular myofibrils isolated from skeletal and cardiac muscle. Formed of serially arranged repeating units called sarcomeres, myofibrils have a complete fully structured ensemble of contractile and Ca2+ regulatory proteins. The small diameter of myofibrils (few micrometres) facilitates analysis of the kinetics of sarcomere contraction and relaxation induced by rapid changes of [ATP] or [Ca2+]. Among the processes studied on myofibrils are: (1) the Ca2+-regulated switch on/off of the troponin complex, (2) the chemical steps in the cross-bridge adenosine triphosphatase cycle, (3) the mechanics of force generation and (4) the length dynamics of individual sarcomeres. These studies give new insights into the kinetics of thin-filament regulation and of cross-bridge turnover, how cross-bridges transform chemical energy into mechanical work, and suggest that the cross-bridge ensembles of each half-sarcomere cooperate with each other across the half-sarcomere borders. Additionally, we now have a better understanding of muscle relaxation and its impairment in certain muscle diseases.


Muscle contraction Muscle relaxation Myocardial contraction Myocardial relaxation Myofibrils Sarcomeres Calcium Thin-filament regulation Cross-bridge kinetics Relaxation Cross-bridge Muscle mechanics Cardiac sarcomere Cardiac muscle Cardiac function Caged calcium Calcium regulation Skinned fibre 



The authors thank Prof. Gabriele Pfitzer for valuable contributions on the manuscript. This work was supported by grants from the German Research Foundation (DFG SFB-612/A2), the Centre of Molecular Medicine Cologne (A6), the Faculty of Medicine Cologne (Köln-Fortune 6/2008) to R.S. The support of Telethon Italy (grant n. GGP07133), MiUR (PRIN 2006), and Ente Cassa di Risparmio di Firenze to C.P. is also acknowledged.


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Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Robert Stehle
    • 1
    • 2
  • Johannes Solzin
    • 1
    • 2
  • Bogdan Iorga
    • 1
    • 3
  • Corrado Poggesi
    • 4
  1. 1.Institute of PhysiologyUniversity of CologneCologneGermany
  2. 2.Centre for Molecular Medicine of CologneCologneGermany
  3. 3.Department of Physics and Applied Mathematics, Faculty of ChemistryUniversity of BucharestBucharestRomania
  4. 4.Dipartimento di Scienze FisiologicheUniversità di FirenzeFirenzeItaly

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