Key result
Exchanging native cardiac troponin C for purified skeletal TnC in Syrian hamster right ventricular muscle decreased Ca2+ sensitivity to 62% of its original value and increased thin-filament cooperativity.
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The troponin C moiety regulates thin-filament cooperativity and Ca2+ sensitivity in cardiac muscle activation, with modifications associated with alterations in its primary structure.
This study describes the effects of exchanging native cardiac troponin C (CTnC) from the right ventricular muscle of Syrian hamster for purified skeletal (S) TnC from fast twitch muscles in triggering cardiac contraction. Ca2+ sensitivity of the myocardium became decreased with STnC to 62% of the original value with CTnC. Furthermore, the slope of the pCa-force curve of cardiac muscle was found to be increased with STnC. The results show that the TnC moiety, as part of the switching mechanism during activation, also regulates thin-filament cooperativity in muscle. Modifications in both the Ca2+ sensitivity and cooperativity are associated with alterations in the primary structure of TnC.
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Gulati et al. (1988) studied Cardiac muscle contraction. Purified skeletal (S) TnC from fast twitch muscles vs. Native cardiac troponin C (CTnC) was evaluated on Ca2+ sensitivity of the myocardium. Exchanging native cardiac troponin C for purified skeletal TnC in Syrian hamster right ventricular muscle decreased Ca2+ sensitivity to 62% of its original value and increased thin-filament cooperativity.
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