Differential effects of pH on calcium activation of myofilaments of adult and perinatal dog hearts. Evidence for developmental differences in thin filament regulation.
- 1 May 1986
- journal article
- research article
- Published by Wolters Kluwer Health in Circulation Research
- Vol. 58 (5) , 721-729
- https://doi.org/10.1161/01.res.58.5.721
Abstract
Our results show that calcium activation of myofilament preparations of dog heart in the perinatal period is unaffected by a reduction in pH from 7.0 to 6.5, which, in adult heart myofilaments, induces a 0.4 pCa unit (-log molar free calcium concentration) rightward shift in the relation between pCa and myofibrillar adenosine triphosphatase activity. Acidic pH also had no effect on calcium binding to myofibrillar troponin C of perinatal hearts. The stoichiometry of troponin C bound calcium at full myofilament activation (about 3 mol calcium/mol troponin C) was the same for adult and perinatal heart myofibrils, as was their myofibrillar troponin C content. Moreover, there were no differences in isoelectric pH of troponin C from adult and perinatal hearts. We tested whether variants of myofilament proteins other than troponin C could account for the differential effects of acidic pH. In adult and perinatal dog heart preparations, myosin heavy chain isoenzymes appeared the same as measured, using native pyrophosphate gel electrophoresis. No evidence for thick filament-related calcium regulation in the perinatal heart myofilaments was obtained, when tested in studies in which native thin filaments were displaced with a 10-fold molar excess of pure actin. In preparations in which native thick filaments were displaced with a 10-fold molar excess of pure skeletal muscle myosin, the effects of acidic pH on calcium activation were the same as in native adult and perinatal preparations. Our major conclusion from these results in that the perinatal heart myofilaments are likely to possess variations in thin filament activity and structure.(ABSTRACT TRUNCATED AT 250 WORDS)This publication has 29 references indexed in Scilit:
- Effect of skeletal muscle myosin light chain 2 on the calcium-sensitive interaction of myosin and heavy meromyosin with regulated actinBiochemistry, 1984
- Isoforms of heavy and light chains of cardiac myosins from rat and rabbitBasic Research in Cardiology, 1982
- Polymorphic myosin as the common determinant of myofibrillar ATPase in different haemodynamic and thyroid statesBasic Research in Cardiology, 1982
- Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle.The Journal of general physiology, 1981
- Species- and age-dependent changes in the relative amounts of cardiac myosin isoenzymes in mammalsDevelopmental Biology, 1981
- The effect of calcium on the inotropy of catecholamine and paired electrical stimulation in the newborn and adult myocardiumJournal of Molecular and Cellular Cardiology, 1981
- Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom.The Journal of general physiology, 1975
- SMALL‐SCALE FRACTIONATION OF PROTEINS AND NUCLEIC ACIDS BY ISOELECTRIC FOCUSING IN POLYACRYLAMIDE GELS*Annals of the New York Academy of Sciences, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- A model for the myosin moleculeBiochimica et Biophysica Acta, 1960