Advertisement

Function of Creatine Kinase Localization in Muscle Contraction

  • S. Koons
  • R. Cooke
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 194)

Abstract

The creatine phosphate shuttle hypothesis, a central theme of the Congress, suggests that mitochondrial creatine kinase (CK) produces phosphocreatine (PCr) from ATP, that CK on or near the sarcomere produces ATP from PCr, and that energy is shuttled from mitochondria to the myofibrils via PCr. According to the hypothesis the CK reaction is crucial to the control of respiration and to the control of the microenvironment of the contractile apparatus. The nucleotide concentrations in the region of the myosin ATPase are thought to depend on the localization of CK on the sarcomere (Bessman and Geiger, 1981). Many studies have addressed the issue of CK localization on the mitochondrial membrane, and of the effects of nucleotide and PCr on oxidative respiration (Jacobus and Lehninger, 1973; Saks et al., 1980). At the opposite end of the shuttle, the sarcomere, there is evidence for CK localization on the M-line structure (Turner et al., 1973). This result motivated several investigations of CK interactions with myosin and with other M-line proteins. Although some studies came to the intriguing conclusion that CK binds to the head region of myosin, others failed to confirm this observation (Houk and Putnam, 1973; Botts et al., 1975; Mani et al., 1980; Woodhead and Lowey, 1983). The possibility of a direct interaction of CK with the myosin head suggests that the contractile mechanism may depend upon CK binding, and thus upon the CK concentration. However, the functional significance of the binding of CK to either myosin or the M-line has not been previously explored by physiological measurements of fiber contraction.

Keywords

Creatine Kinase Myosin Head Creatine Kinase Activity Unstirred Layer Myosin ATPase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bessman, S.P., and Geiger, P.J., 1981, Transport of energy in muscle: the phosphorylcreatine shuttle, Science, 211: 448.PubMedCrossRefGoogle Scholar
  2. Botts, J., Stone, D.B., Wang, A.T.L., and Mendelson, R.A., 1975, Electron paramagnetic resonance and nanosecond fluorescence depolarization studies on creatine-phosphokinase interaction with myosin and its fragments, J. Supramol. Str., 3: 141.CrossRefGoogle Scholar
  3. Bradford, M., 1976, Rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72: 248.PubMedCrossRefGoogle Scholar
  4. Cande, W.Z., 1983, Creatine kinase role in anaphase chromosome movement, Nature 304: 557.PubMedCrossRefGoogle Scholar
  5. Cooke, R., and Bialek, W., 1979, The contraction of glycerinated muscle fibers as a function of the ATP concentration, Biophys J., 28: 241.PubMedCrossRefGoogle Scholar
  6. Crowder, M.C., and Cooke, R., 1984, Effects of sulfhydryl modification on the mechanics of fiber contraction, J. Mus. Res. and Cell Mot., 5: 131.CrossRefGoogle Scholar
  7. Houk, T.W., Jr., and Putnam, S.V., 1973, Location of creatine phosphokinase binding site of myosin, Biochem. Biophys. Res. Commun., 55: 1271.PubMedCrossRefGoogle Scholar
  8. Jacobus, W.E., and Lehininger, A.L., 1973, Creatine kinase of rat heart mitochondria. Coupling of creatine phosphorylation to electron transport, J. Biol. Chem., 248: 4803.PubMedGoogle Scholar
  9. Koons, S.J., Eckert, B.S., and Zobel, C.R., 1982, Immunofluorescence and inhibitor studies on creatine kinase and mitosis, Exp. Cell. Res., 140: 401.PubMedCrossRefGoogle Scholar
  10. Mani, R.S., Herasymowych, O.S., and Kay, C.M., 1980, Physical, chemical and ultrastructural studies on muscle M-line proteins, Int. J. Biochem., 12: 333.PubMedCrossRefGoogle Scholar
  11. Saks, V.A., Kupriyanov, V.V., Elizarova, G.V., and Jacobus, W.E., 1980, Studies of energy transport in heart cells. The importance of creatine kinase localization for the coupling of mitochondrial phosphorylcreatine production to oxidative phosphorylation, J. Biol. Chem., 255: 755.PubMedGoogle Scholar
  12. Savali, F., Geiger, P.J., and Bessman, S.P., 1983, Kinetic properties and functional role of creatine phosphokinase in glycerinated muscle fibers - further evidence for compartmentation, Biochem. Biophys. Res. Commun., 114: 785.CrossRefGoogle Scholar
  13. Turner, D.C., Wallimann, T., and Eppenberger, H.M., 1973, A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase, Proc. Natl. Acad. Sci. USA, 70: 702.PubMedCrossRefGoogle Scholar
  14. Wallimann, T., Schlosser, T., and Eppenberger, H.M., 1984, Function of M-line bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphorylcreatine shuttle in muscle, J. Biol. Chem., 259: 5238.PubMedGoogle Scholar
  15. Woodhead, J.C., and Lowey, S., 1983, An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments, J. Mol. Biol., 168: 831.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • S. Koons
    • 1
  • R. Cooke
    • 1
  1. 1.Dept. of Biochemistry & Biophysics and Cardiovascular Research InstituteUniversity of California, San FranciscoSan FranciscoUSA

Personalised recommendations