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of Illinois at Chicago, Chicago, Illinois Powers, Frances M., R. John Solaro. cardiac independently of Ca2+ binding to troponin C. Am. J. PhysioZ. 268 (CeZZ Physiol. 37): C1348-C1353, 1995.-We investigated the mechanism by which influences responsiveness to Ca 2+ by measuring isometric force, Ca2+ binding, ATPase of dog cardiac proteins. (20 mM) increased submaximal depressed maximal force in skinned fiber bundles. Although the Ca2+ sensitivity of was increased by , there was no effect on Ca2+ binding to troponin C (TnC) in skinned fiber bundles. To determine if altered actin-myosin interaction or affected myosin directly, myofibrillar, actomyosin, myosin ATPase activities were measured. Maximal Ca2+activated myofibrillar Mg 2+-ATPase was depressed by 20 mM , whereas submaximal Mg2+-ATPase activities were not changed. Actomyosin Mg2+-ATPase was significantly depressed by concentrations > 15 mM. Myosin Ca 2+-ATPase was depressed by , whereas Mg 2+-ATPase K(EDTA)-ATPase activities were not affected. These data suggest that affects function via a mechanism that is independent of TnCCa2+ binding but that may involve direct effects on actin-crossbridge interaction. calcium sensitivity; myosin adenosinetriphosphatase; sin adenosinetriphosphatase; skinned fiber bundles actomyo- 1,3,7-trimethylxanthine, a pharmacological tool commonly used to release Ca2+ from the sarcoplasmic reticulum (SR) in studies of different aspects
AJP - Cell Physiology – The American Physiological Society
Published: Jun 1, 1995
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