Effect of Substitution of Troponin C in Cardiac Myofibrils with Skeletal Troponin C or Calmodulinon the Ca2+ -and Sr2+-Sensitive ATPase Activity1
- 1 July 1988
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 104 (1) , 149-154
- https://doi.org/10.1093/oxfordjournals.jbchem.a122412
Abstract
Troponin C was removed almost completely from the porcine cardiac myofibrils by the same extraction procedureusing CDTA as that previously reported for the rabbit skeletal myofibrils (Morimoto, S. & Ohtsuki, I. (1987)J. Biochem. 101, 291-301), and the effects of substitution of troponin C in cardiac myofibrils with rabbit skeletal troponin C or bovine brain calmodulin were examined. While the ATPase activity of intact cardiac myofibrils or cardiac troponin C-reconstituted cardiac myofibrils was activated at only a little higher concentration of Sr2+ than Ca2+ the skeletal troponin C-substituted cardiac myofibrils, as well as intact rabbit skeletal myofibrils, required more than 10 times higher concentration of Sr2+ than Ca2+ for activation of the myofibrillar ATPase activity. However, the concentrations of Ca2+ and Sr2+ required for the activation of the ATPase activity of the skeletal troponin C-substituted cardiac myofibrils were both about 5 times higher than those of intact skeletal myofibrils. The skeletal troponin C-substituted cardiac myofibrils, as well as intact skeletal myofibrils, also showed higher cooperativity in the Ca2+ of the ATPase activity than intact or cardiac troponinC-reconstituted cardiac myofibrils. The ATPase activity of calmodulin-substituted cardiac myofibrils was activated at a several times lower concentration of Ca2+ or Sr2+ than that of calmodulin-substituted skeletal myofibrils, while the ratios of the concentration of Sr2+ to Ca2+ required for activation were almost the same in both cases. The results indicate that, among the characteristics of divalent cation regulation in the contraction of skeletal and cardiac muscles, the higher sensitivity to Ca2+ relative to Sr2+ and the higher cooperativity in the divalent cation activation in skeletal muscle than in cardiac muscle are determined solely by the species of troponin C, but thesensitivities to the divalent cations in the contraction of skeletal and cardiac muscle are determined through the interactions between troponin C and other troponin components.Keywords
This publication has 16 references indexed in Scilit:
- A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils.Published by Elsevier ,2021
- Calmodulin-free skeletal-muscle troponin C prepared in the absence of ureaBiochemical Journal, 1981
- Re-Examination of the Apparent Binding Constant of Ethylene Glycol Bis(β-Aminoethyl Ether)-N,N,N',N'-Tetraacetic Acid with Calcium around Neutral pH12The Journal of Biochemistry, 1980
- Calmodulins from Muscles of Marine Invertebrates, Scallop and Sea AnemoneThe Journal of Biochemistry, 1980
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Physiological Significance of Ca Uptake by Mitochondria in the Heart in Comparison with that by Cardiac Sarcoplasmic Reticulum1The Journal of Biochemistry, 1976
- Calcium Binding Activity of Microsomal Fraction of Rabbit Red Muscle*The Journal of Biochemistry, 1968
- Determination of phosphate: Study of labile organic phosphate interferenceClinica Chimica Acta; International Journal of Clinical Chemistry, 1967
- The bound nucleotide of the isolated myofibrilBiochemical Journal, 1952
- DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTIONJournal of Biological Chemistry, 1949