Contractile and metabolic effects of increased creatine kinase activity in mouse skeletal muscle

American Journal of Physiology - Cell Physiology

Volumn 270, Issue 4 39-4, 1996, Pages

  Roman, Brian B ^b   Foley, Jeanne M ^b   Meyer, Ron A ^b   Koretsky, Alan P ^b  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b NONE

Author keywords

31P nuclear magnetic resonance; isometric contraction; myosin isoform; phosphocreatine; transgenic

Indexed keywords

ADENYLATE KINASE; CONTRACTILE PROTEIN; CREATINE KINASE; LACTATE DEHYDROGENASE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBUNIT; GASTROCNEMIUS MUSCLE; HIGH ENERGY PHOSPHATE; MOUSE; MUSCLE ISOMETRIC CONTRACTION; MUSCLE METABOLISM; NONHUMAN; PRIORITY JOURNAL; SKELETAL MUSCLE; TRANSGENE;

EID: 0030003711     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1996.270.4.c1236     Document Type: Article

References (49)

1. Baldwin, K. M., W. W. Winder, and R. L. Terjung. Glycolytic enzymes in different types of skeletal muscle in adaptation to exercise. Am. J. Physiol. 225: 962-966, 1973.
2. Baskin, R. J., and C. N. Deamer. A membrane-bound creatine phosphokinase in fragmented sarcoplasmic reticulum. J. Biol. Chem. 245: 1345-1347, 1970.
3. Bessman, S. P., and C. L. Carpenter. The creatine-creatine phosphate energy shuttle. Annu. Rev. Biochem. 54: 831-862, 1985.
4. Bessman, S. P., and P. J. Geiger. Transport of energy in muscle: the phosphorylcreatine shuttle. Science Wash. DC 211: 448-452, 1983.
5. 31P NMR surface coil studies in brain, heart, and skeletal muscle of the living rat. J. Biochem. 26: 6083-6090, 1987.
6. 31P NMR magnetization-transfer measurements of ATP turnover during steady-state isometric muscle contraction in the rat hind limb in vivo. J. Biochem. 28: 4887-4893, 1989.
7. 31P NMR measurements of myocardial pH in vivo. Biochem. Biophys. Res. Commun. 151: 70-77, 1988.
8. Brosnan, M. J., S. P. Raman, L. Chen, and A. P. Koretsky. Altering creatine kinase isoenzymes in transgenic mouse muscle by overexpression of the B subunit. Am. J. Physiol. 264 (Cell Physiol. 33): C151-C160, 1993.
9. Buller, A. J., J. C. Eccles, and R. M. Eccles. Interactions between motor neurones and muscles in respect of the characteristics speeds of their responses. J. Physiol. Lond. 150: 417-439, 1960.
10. Cain, D. F., and R. E. Davies. Breakdown of adenosine triphosphate during a single contraction of working muscle. Biochem. Biophys. Res. Commun. 8: 361-366, 1962.
11. Chase, P. B., and M. J. Kushmerick. Effect of physiological ADP concentrations on contraction of single skinned fibers from rabbit fast and slow muscles. Am. J. Physiol. 268 (Cell Physiol. 37): C480-C490, 1995.
12. Cooke, R., and W. Bialek. Contraction of glycerinated muscle fibers as a function of the ATP concentration. Biophys. J. 28: 241-258, 1979.
13. Fitch, C. D., M. Jellinek, R. H. Gitts, K. M. Baldwin, and J. O. Holloszy. Phosphorylated β-guanidinopropionate as a substitute for phosphocreatine in rat muscle. Am. J. Physiol. 228: 1123-1125, 1975.
14. 31P NMR. NMR Biomed. 6: 32-38, 1993.
15. Fossel, E. T., and H. Hoefeler. Complete inhibition of creatine kinase in isolated perfused rat hearts. Am. J. Physiol. 252 (Endocrinol. Metab. 15): E124-E129, 1987.
16. Hall, N., P. Addis, and M. Deluca. Mitochondrial creatine kinase. Physical and kinetic properties of the purified enzyme from beef heart. J. Biochem. 18: 1745-1751, 1979.
17. Haugaard, N., L. Potter, A. J. Wein, and R. M. Levin. Effect of partial obstruction of the rabbit urinary bladder on malate dehydrogenase and citrate synthase activity. J. Urol. 147: 1391-1393, 1992.
18. Hogan, B., F. Constantini, and E. Lacy. Manipulating the Mouse Embryo: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor, 1986.
19. Jansson, E., B. Sjodin, and P. Tesch. Changes in muscle fibre type distribution in man after physical training. Acta Physiol. Scand. 104: 235-237, 1978.
20. Kepler, D., and K. Decker. Glycogen-determination with amyloglucosidase. In: Methods of Enzymatic Analysis, edited by H. U. Bergmeyer. New York: Academic, 1974, vol. 3, p. 1127-1131.
21. Koretsky, A. P. Investigation of cell physiology in the animal using transgenic technology. Am. J. Physiol. 262 (Cell Physiol. 31): C261-C275, 1992.
22. Koretsky, A. P., M. J. Brosnan, L. Chen, J. Chen, and T. van Dyke. NMR detection of creatine kinase expressed in liver of transgenic mice: determination of free ADP levels. Proc. Natl. Acad. Sci. USA 87: 3112-3116, 1990.
23. LaFramboise, W. A., M. J. Daood, R. D. Guthrie, P. Moretti, S. Schiaffino, and M. Ontell. Electrophoretic separation and immunological identification of type IIx myosin heavy chain in rat skeletal muscle. Biochim. Biophys. Acta 1035: 109-112, 1990.
24. eq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions. J. Biol. Chem. 254: 6528-6537.
25. McFarland, E. W., M. J., Kushmerick, and T. S. Moreland. Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type. Biophys. J. 67: 1912-1924, 1994.
26. 2+-sensitive cross- bridge state transition in mammalian single muscle fibers. J. Physiol Lond. 428: 751-764, 1990.
27. Metzger, J. M., and R. L. Moss. Phosphate and the kinetics of force generation in skinned skeletal muscle fibers (Abstract). Biophys. J. 59: 418a, 1991.
28. Meyer, R. A., T. R. Brown, B. L. Krilowicz, and M. J. Kushmerick. Phosphagen and intracellular pH changes during contraction of creatine-depleted rat muscle. Am. J. Physiol. 250 (Cell Physiol. 19): C264-C274, 1986.
29. Meyer, R. A., and J. M. Foley. Cellular processes integrating the metabolic responses to exercise. In: Handbook of Physiology. Exercise: Regulation and Integration of Multiple Systems. Bethesda, MD: Am. Physiol. Soc., sect. 12, pt. III, chapt. 18. In press.
30. Meyer, R. A., H. L. Sweeney, and M. J. Kushmerick. A simple analysis of the "phosphocreatine shuttle." Am. J. Physiol. 246 (Cell Physiol. 15): C365-C377, 1984.
31. Miller, K., J. Halow, and A. P. Koretsky. Phosphocreatine protects transgenic mouse liver expressing creatine kinase from hypoxia and ischemia. Am. J. Physiol. 265 (Cell Physiol. 34): C1544-C1551, 1994.
32. Moerland, T. S., and M. J. Kushmerick. Contractile economy and aerobic recovery metabolism in skeletal muscle adapted to creatine depletion. Am. J. Physiol. 267 (Cell Physiol. 36): C127-C137, 1994.
33. Moerland, T. S., N. G. Wolf, and M. J. Kushmerick. Administration of a creatine analogue induces isomyosin transitions in muscle. Am. J. Physiol. 257 (Cell Physiol. 26): C810-C816, 1989.
34. Passonneau, J. V., and O. H. Lowry. Phosphofructokinase. In: Enzymatic Analysis-A Practical Guide. Totowa, NJ: Human Press, 1993, p. 292-293.
35. Sambrook, J., E. F. Fritsch, and T. Maniantis. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY; Cold Spring Harbor, 1989.
36. Savabi, F. Interaction of creatine kinase and adenylate kinase systems in muscle cells. Mol. Cell. Biochem. 133/134: 145-152, 1994.
37. Savabi, F., P. J. Geiger, and S. P. Bessman. Kinetic properties and functional role of creatine phosphokinase in glycerinated muscle fibers-further evidence for compartmentation. Biochem. Biophys. Res. Commun. 114: 785-790, 1983.
38. Sharov, V. G., V. A. Saks, V. M. Smirnov, and E. I. Chazov. An electron microscopical histochemical investigation of the localization of creatine kinase in heart cells. Biochim. Biophys. Acta 468: 495-501, 1977.
39. Shoubridge, E. A., and G. K. Radda. Regulation of creatine kinase during steady-state isometric twitch contraction in rat skeletal muscle. Biochim. Biophys. Acta 805: 72-78, 1984.
40. 31P-nuclear magnetic resonance study of skeletal muscle metabolism in rats depleted of creatine with the analogue β-guanidinopropionic acid. Biochim. Biophys. Acta 805: 79-88, 1984.
41. 31P NMR study of tetanic contraction in rat muscle depleted of phosphocreatine. Am. J. Physiol. 252 (Cell Physiol. 21): C532-C542, 1987.
42. Srere, P.A. Citrate synthase. In: Methods in Enzymology, edited by J. M. Lowenstein. New York: Academic Press, 1969, vol. 13, p. 3-5.
43. Tombes, R. M., and B. M. Shapiro. Metabolite channeling: a phosphorylcreatine shuttle to mediate high energy phosphate transport between sperm mitochondrion and tail. Cell 41: 325-334, 1985.
44. Turner, D. C., T. Wallimann, and H. M. Eppenberger. 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: 702-705, 1973.
45. Van Deursen, J., A. Heerschap, F. Oerlemans, W. Ruitenbeek, P. Jap, H. ter Laak, and B. Wieringa. Skeletal muscles of mice deficient in muscle creatine kinase lack burst activity. Cell 74: 621-631, 1993.
46. Van Deursen, J., W. Ruitenbeek, A. Heerschap, P. Jap, H. ter Laak, and B. Wieringa. Creatine kinase (CK) in skeletal muscle energy metabolism: a study of mouse mutants with graded reduction in muscle CK expression. Proc. Natl. Acad. Sci. USA 91: 9091-9095, 1994.
47. Walliman, T., D. C. Turner, and H. M. Eppenberger. Localization of creatine kinase in myofibrils. J. Cell Biol. 75: 297-317, 1977.
48. Zeleznikar, R. J., P. P. Dzeja, and N. D. Goldberg. Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation bh glycolysis in intact muscle. J. Biol. Chem. 270: 7311-7319, 1995.
49. Zeleznikar, R. J., R. A. Heyman, R. M. Graeff, T. F. Walseth, S. M. Dawis, E. A. Butz, and N. D. Goldberg. Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle. J. Biol. Chem. 265: 300-311, 1990.