[A comparative study of the role of creatine phosphokinase isoenzymes in energy metabolism of skeletal and heart muscle] - PubMed

[Article in Russian]

• PMID: 870086

Comparative Study

[A comparative study of the role of creatine phosphokinase isoenzymes in energy metabolism of skeletal and heart muscle]

[Article in Russian]

V A Saks et al. Biokhimiia. 1977 Apr.

Abstract

It has been shown that the contents of mitochondria and mitochondrial isoenzyme of creatine phosphokinase are almost identical in skeletal and heart muscles. In mitochondria from both types of muscle creatine phosphokinase is functionally coupled to ATP-ADP translocase. This kind of coupling ensures complete conversion of mitochondrial ATP energy into the energy of creatine phosphate and effective control of oxidative phosphorylation by the creatine phosphokinase reaction. It has also been shown that all isoenzymes of creatine phosphokinase from heart and skeletal muscle have very similar kinetic properties. Significant differences have been found to exist between isoenzyme patterns of these muscles and also in distribution of different isoenzymes in the cells. In skeletal muscle cells creatine phosphokinase is present mainly as cytosolic MM isoenzyme; about 6% of total cellular activity is localised also in mitochondria. Due to high activity of cytosolic isoenzyme the total activity of creatine phosphokinase is about three times higher in skeletal muscle than in cardiac muscle. It has been also shown that phosphoenolpyruvate and glucose-6-phosphate do not have any inhibitory effect on creatine phosphokinase.

Similar articles

• [Functional characterization of the creatine phosphokinase reactions in heart mitochondria and myofibrils].

  Saks VA, Lipina NV, Liulina IV, Chernousova GB, Fetter R, Smirnov VI, Chazov EI. Saks VA, et al. Biokhimiia. 1976 Aug;41(8):1460-70. Biokhimiia. 1976. PMID: 1030648 Russian.

• [The functional coupling between MM isozyme of creatine phosphokinase (EC 2.7.3.2.) and MgATPase of myofibrils and (Na, K)ATPase of plasma membrane in heart cells].

  Saks VA, Lipina NV, Chernousova GB, Sharov VG, Smirnov VN, Chazov EI, Grosse R. Saks VA, et al. Biokhimiia. 1976 Dec;41(12):2099-109. Biokhimiia. 1976. PMID: 139170 Russian.

• Studies of energy transport in heart cells. Mitochondrial isoenzyme of creatine phosphokinase: kinetic properties and regulatory action of Mg2+ ions.

  Saks VA, Chernousova GB, Gukovsky DE, Smirnov VN, Chazov EI. Saks VA, et al. Eur J Biochem. 1975 Sep 1;57(1):273-90. doi: 10.1111/j.1432-1033.1975.tb02299.x. Eur J Biochem. 1975. PMID: 126157

• [Creatine kinase isoenzymes--characterization and functions in cell].

  Grzyb K, Skorkowski EF. Grzyb K, et al. Postepy Biochem. 2008;54(3):274-83. Postepy Biochem. 2008. PMID: 19112826 Review. Polish.

• Respiratory control and the integration of heart high-energy phosphate metabolism by mitochondrial creatine kinase.

  Jacobus WE. Jacobus WE. Annu Rev Physiol. 1985;47:707-25. doi: 10.1146/annurev.ph.47.030185.003423. Annu Rev Physiol. 1985. PMID: 3888084 Review.

Cited by

• Creatine kinase activity associated with the contractile proteins of the guinea-pig carotid artery.

  Clark JF, Khuchua Z, Boehm E, Ventura-Clapier R. Clark JF, et al. J Muscle Res Cell Motil. 1994 Aug;15(4):432-9. doi: 10.1007/BF00122117. J Muscle Res Cell Motil. 1994. PMID: 7806637

• Theoretical modelling of some spatial and temporal aspects of the mitochondrion/creatine kinase/myofibril system in muscle.

  Kemp GJ, Manners DN, Clark JF, Bastin ME, Radda GK. Kemp GJ, et al. Mol Cell Biochem. 1998 Jul;184(1-2):249-89. Mol Cell Biochem. 1998. PMID: 9746325

• Functional coupling as a basic mechanism of feedback regulation of cardiac energy metabolism.

  Saks VA, Kuznetsov AV, Vendelin M, Guerrero K, Kay L, Seppet EK. Saks VA, et al. Mol Cell Biochem. 2004 Jan-Feb;256-257(1-2):185-99. doi: 10.1023/b:mcbi.0000009868.92189.fb. Mol Cell Biochem. 2004. PMID: 14977180

• Myofibrillar creatine kinase and cardiac contraction.

  Ventura-Clapier R, Veksler V, Hoerter JA. Ventura-Clapier R, et al. Mol Cell Biochem. 1994 Apr-May;133-134:125-44. doi: 10.1007/BF01267952. Mol Cell Biochem. 1994. PMID: 7808450 Review.

• Metabolic compartmentation and substrate channelling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration--a synthesis.

  Saks VA, Khuchua ZA, Vasilyeva EV, Belikova OYu, Kuznetsov AV. Saks VA, et al. Mol Cell Biochem. 1994 Apr-May;133-134:155-92. doi: 10.1007/BF01267954. Mol Cell Biochem. 1994. PMID: 7808453 Review.

Publication types

MeSH terms

Substances