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- W1972896858 abstract "It has been proposed that the rate limiting step of cardiac muscle relaxation resides in the myofilaments. The primary mechanism is thought to be the rate of cross-bridge detachment (strongly governed by ADP) since it is generally assumed to be substantially slower than the rate at which the thin filament inactivates (governed by Ca2+ dissociation from TnC). This stems from the fact that the rate of Ca2+ dissociation from isolated TnC is orders of magnitude faster than the rate of relaxation. However, TnC does not function in isolation but as an integral component of the myofilament contractile system. Furthermore, the Ca2+ binding properties of TnC can be drastically affected by the other thin filament proteins and by myosin binding to actin. Thus, we wanted to determine the Ca2+ dissociation rate from TnC in cardiac myofibrils during different cross-bridge states. To achieve this goal, rabbit ventricular myofibrils were exchanged with human cardiac troponin containing a TnC (C35S, C84S, T53C) fluorescently labeled with IANBD. Unexpectedly, via the change in TnC fluorescence, not only could we observe the rate of Ca2+ dissociation from TnC in the myofibrils, but also what we think is the rate of cross-bridge detachment. At 15oC and in the presence of ADP, the cross-bridge detachment rate was ∼7/s, three times slower than the rate of Ca2+ dissociation from TnC (∼21/s). However, at near physiological temperature (35oC) the two rates were very similar (∼60/s). Based on the temperature dependence of the rates, at temperatures below 25oC, cross-bridge detachment may very well be rate limiting for relaxation, but at higher temperatures both rates may be able to modulate the rate of relaxation." @default.
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- W1972896858 date "2010-01-01" @default.
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- W1972896858 title "Effect of Temperature on The Rates of Calcium Dissociation and Cross-Bridge Detachment in Cardiac Myofibrils Reported by Troponin C" @default.
- W1972896858 doi "https://doi.org/10.1016/j.bpj.2009.12.812" @default.
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