The role of creatine phosphokinase in supplying energy for the calcium pump system of heart sarcoplasmic reticulum.

An investigation of isolated and purified heart sarcoplasmic reticulum performed in the current study indicates the presence of significant creatine phosphokinase (CPK) activity in this preparation. The localization of CPK on the membrane of sarcoplasmic reticulum has been revealed also by an electron microscopic histochemical method. Under the conditions of the Ca(2+)-ATPase reaction in the presence of creatine phosphate, the release of creatine into the reaction medium is observed, the rate of the latter process being dependent on the MgATP concentration in accordance with the kinetic parameters of the Ca2+-ATPase reaction. CPK localized on the reticular membrane is able to maintain the high rate of calcium consumption by the sarcoplasmic reticulum vesicles. The results obtained demonstrate the close functional coupling between CPK and Ca2+-ATPase in the membrane of sarcoplasmic reticulum and indicate the important functional role of CPK in supplying energy for the Ca(2+)-ATPase reaction and ion transport across the membrane of heart sarcoplasmic reticulum.

[1]  J. Gergely,et al.  Fractionation of solubilized sarcoplasmic reticulum. , 1971, Biochemical and biophysical research communications.

[2]  D. Maclennan Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. , 1970, The Journal of biological chemistry.

[3]  V. Saks,et al.  Studies of energy transport in heart cells. The functional coupling between mitochondrial creatine phosphokinase and ATP ADP translocase: kinetic evidence. , 1976, Archives of biochemistry and biophysics.

[4]  S. Fleischer,et al.  Isolation of sarcoplasmic reticulum by zonal centrifugation and purification of Ca 2+ -pump and Ca 2+ -binding proteins. , 1973, Biochimica et biophysica acta.

[5]  M. Aliev,et al.  Isolation of calcium pump system and purification of calcium ion-dependent ATPase from heart muscle. , 1976, Biochimica et biophysica acta.

[6]  J. H. Johnson,et al.  Continuous recording of pH and pCa during calcium binding by muscle microsomes. , 1968, Biochimica et biophysica acta.

[7]  V. Saks,et al.  The localization of the MM isozyme of creatine phosphokinase on the surface membrane of myocardial cells and its functional coupling to ouabain-inhibited (Na+, K+)-ATPase. , 1977, Biochimica et biophysica acta.

[8]  N. Baba,et al.  Histochemistry of creatine phosphokinase. , 1976, Journal of molecular and cellular cardiology.

[9]  V. Saks,et al.  Studies of energy transport in heart cells. Intracellular creatine content as a regulatory factor of frog heart energetics and force of contraction. , 1976, Biochemical medicine.

[10]  V A Saks,et al.  Kinetic properties and the functional role of particulate MM‐isoenzyme of creatine phosphokinase bound to heart muscle myofibrils , 1976, FEBS letters.

[11]  D. Deamer,et al.  A membrane-bound creatine phosphokinase in fragmented sarcoplasmic reticulum. , 1970, The Journal of biological chemistry.

[12]  A. Weber Regulatory Mechanisms of the Calcium Transport System of Fragmented Rabbit Sarcoplasmic Reticulum , 1971, The Journal of General Physiology.

[13]  V A Saks,et al.  Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: kinetic properties and regulatory action of Mg2+ ions. , 1975, European journal of biochemistry.

[14]  A. Martonosi Biochemical and Clinical Aspects of Sarcoplasmic Reticulum Function , 1972 .

[15]  D. Maclennan,et al.  Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[16]  W. Mommaerts Energetics of muscular contraction. , 1969, Physiological reviews.

[17]  S. Ebashi Molecular biology of muscular contraction , 1965 .