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Biophys J, October 2002, p. 2152-2161, Vol. 83, No. 4

Force Kinetics and Individual Sarcomere Dynamics in Cardiac Myofibrils after Rapid Ca2+ Changes

R. Stehle, M. Krüger, and G. Pfitzer

Institute of Physiology, University Cologne, D-50931 Köln, Germany

Kinetics of force development and relaxation after rapid application and removal of Ca2+ were measured by atomic force cantilevers on subcellular bundles of myofibrils prepared from guinea pig left ventricles. Changes in the structure of individual sarcomeres were simultaneously recorded by video microscopy. Upon Ca2+ application, force developed with an exponential rate constant kACT almost identical to kTR, the rate constant of force redevelopment measured during steady-state Ca2+ activation; this indicates that kACT reflects isometric cross-bridge turnover kinetics. The kinetics of force relaxation after sudden Ca2+ removal were markedly biphasic. An initial slow linear decline (rate constant kLIN) lasting for a time tLIN was abruptly followed by an ~20 times faster exponential decay (rate constant kREL). kLIN is similar to kTR measured at low activating [Ca2+], indicating that kLIN reflects isometric cross-bridge turnover kinetics under relaxed-like conditions (see also Tesi et al., 2002. Biophys. J. 83:2142-2151). Video microscopy revealed the following: invariably at tLIN a single sarcomere suddenly lengthened and returned to a relaxed-type structure. Originating from this sarcomere, structural relaxation propagated from one sarcomere to the next. Propagated sarcomeric relaxation, along with effects of stretch and Pi on relaxation kinetics, supports an intersarcomeric chemomechanical coupling mechanism for rapid striated muscle relaxation in which cross-bridges conserve chemical energy by strain-induced rebinding of Pi.

Biophys J, October 2002, p. 2152-2161, Vol. 83, No. 4
© 2002 by the Biophysical Society   0006-3495/02/10/2152/10  $2.00



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