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