Abstract
The contractility of cardiac muscle is controlled by a dual-filament mechanism in which calcium-dependent structural changes in the thin filament gate the access of the myosin motors to the actin-binding sites, whereas regulatory structural changes in the thick filament modulate the number of motors available for the actomyosin interaction. Here we investigated the role of those structural changes in determining the kinetics of force generation during maximal activation by photolysis of caged calcium (NP-EGTA) in demembranated rat cardiac trabeculae at 27°C with lattice compression by Dextran, conditions in which the native OFF state of the thick filament is preserved in the absence of calcium.
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