Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers

Biophysical Journal

Volumn 71, Issue 3, 1996, Pages 1450-1461

  Wang, Gang ^a   Kawai, Masataka ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; MAGNESIUM DERIVATIVE;

ANIMAL CELL; ARTICLE; ARTIFACT; HEART MUSCLE CELL; KINETICS; MUSCLE FATIGUE; MUSCLE ISOMETRIC CONTRACTION; MUSCLE TONE; MUSCLE TWITCH; NONHUMAN; SLOW MUSCLE FIBER; SOLEUS MUSCLE;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0029762037     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79346-3     Document Type: Article

References (53)

1. Bárany, M. 1967. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50(Suppl P2):197-218.
2. Brenner, B., M. Schoenberg, J. M. Chalovich, L. E. Greene, and E. Eissenberg. 1982. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc. Natl. Acad. Sci. USA. 79:7288-7291.
3. Cooke, R., and E. Pate. 1985. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys. J. 48:789-798.
4. Crow, M. T., and M. J. Kushmerick. 1982. Chemical energetics of slowand fast-twitch muscles of the mouse. J. Gen. Physiol. 79:147-166.
5. Dantzig, J. A., M. G. Hibberd, D. R. Trentham, and Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J. Physiol. (Lond.). 432:639-680.
6. Ferenczi, M. A., Y. E. Goldman, and R. M. Simmons. 1984. The dependence of force and shortening velocity on substrate concentration in skinned muscle fibers from Rana temporaria. J. Physiol (Lond.). 350:519-543.
7. 2+ movements and tension development in rat skinned skeletal muscle fibers. J. Physiol. (Lond.). 482:123-140.
8. Galler, S., T. L. Schmitt, and D. Pette. 1994. Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibers. J. Physiol. (Lond.). 478:513-521.
9. Geeves, M. A., R. S. Goody, and H. Gutfreund. 1984. Kinetics of acto-S1 interaction as a guide to a model for the cross-bridge cycle. J. Muscle Res. Cell Motil. 5:351-361.
10. Godt, R. E., and D. W. Maughan. 1988. On the composition of the cytosol of relaxed skeletal muscle of the frog. Am. J. Physiol. 254:C591-C604.
11. i. J. Biol. Chem. 255:543-548.
12. Hammes, G. G. 1968. Relaxation spectrometry of biological systems. Adv. Protein Chem. 23:1-57.
13. 2+ sensitivity in skinned rabbit soleus fibers. Pflugers Arch. 410:30-36.
14. Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
15. Johnson, R. E., and P. Adams. 1984. ADP binds similarly to rigor muscle myofibrils and to actomyosin subfragment one. FEBS Lett. 174:11-14.
16. Kawai, M. 1978. Head rotation or dissociation? A study of exponential rate processes in chemically skinned rabbit muscle fibers when MgATP concentration is changed. Biophys. J. 22:97-103.
17. Kawai, M., and P. W. Brandt. 1980. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J. Muscle Res. Cell Motil. 1:279-303.
18. Kawai, M., and H. R. Halvorson. 1989. Role of MgATP and MgADP in the crossbridge kinetics in chemically skinned rabbit psoas fibers, Study of a fast exponential process (C). Biophys. J. 55:595-603.
19. Kawai, M., and H. R. Halvorson. 1991. Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas muscle. Biophys. J. 59:329-342.
20. Kawai, M., Y. Saeki, and Y. Zhao. 1993. Cross-bridge scheme and kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ. Res. 73:35-50.
21. Kawai, M., and F. H. Schachat. 1984. Differences in the transient response of fast and slow skeletal muscle fibers: correlations between complex modulus and myosin light chain. Biophys. J. 45:1145-1151.
22. Kawai, M., and Y. Zhao. 1993. Cross-bridge scheme and force per crossbridge state in skinned rabbit psoas muscle fibers. Biophys. J. 65:638-651.
23. Kentish, J. C., and G. J. Stienen. 1994. Differential effects of length on maximum force production and myofibrillar ATPase activity in rat skinned cardiac muscle. J. Physiol. (Lond.). 475:175-184.
24. Kuhn, H. J., C. Bletz, K. Güth, and J. C. Rüegg. 1985. The effect of MgATP on forming and breaking actin-myosin linkages in contracted skinned insect flight muscle fibres. J. Muscle Res. Cell Motil. 6:5-27.
25. Kushmerick, M. J., R. A. Meyer, and T. R. Brown. 1992a. Regulation of oxygen consumption in fast- and slow-twitch muscle. Am. J. Physiol. 263:C598-C606.
26. i. Proc. Natl. Acad. Sci. USA. 89:7521-7525.
27. Luo, Y., R. Cooke, and E. Pate. 1993. A model of stress relaxation in cross-bridge systems: effect of a series elastic element. Am. J. Physiol. 265:C279-C288.
28. MacKinnon, R., J. K. Gwathmey, P. D. Allen, G. M. Briggs, and J. P. Morgan. 1988. Modulation by the thyroid state of intracellular calcium and contractility in ferret ventricular muscle. Circ. Res. 63:1080-1089.
29. Marston, S. B., and E. W. Taylor. 1980. Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrates muscles. J. Mol. Biol. 139:573-600.
30. McFarland, E. W., M. J. Kushmerick, and T. S. Moerland. 1994. Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type. Biophys. J. 67:1912-1924.
31. Metzger, J. M., and R. L. Moss. 1990. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science. 247:1088-1090.
32. Meyer, R. A., T. R. Brown, and M. J. Kushmerick. 1985. Phosphorus nuclear magnetic resonance of fast- and slow-twitch muscle. Am. J. Physiol. 248:C279-C287.
33. Millar, N. C., and E. Homsher. 1992. Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers. Am. J. Physiol. 252:C1239-C1245.
34. Moore, G. E., M. M. Briggs, and F. H. Schachat. 1987. Patterns of troponin T expression in mammalian fast, slow and promiscuous muscle fibers. J. Muscle Res. Cell Motil. 8:13-22.
35. Nagesser, A. S., W. J. van der Lararse, and G. Elzinga. 1992. Metabolic changes with fatigue in different types of single muscle fibers of Xenopus laevis. J. Physiol. (Lond.). 448:511-523.
36. Pate, E., M, Lin, K. Franks-Skiba, and R. Cooke. 1992. Contraction of glycerinated rabbit slow-twitch muscle fibers as a function of MgATP concentration. Am. J. Physiol, 262:C1039-C1046.
37. Pette, D., and R. S. Staron. 1990. Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev. Physiol. Biochem. Pharmacol. 116:2-47.
38. Potma, E. J., I. A. van Graas, and G. J. M. Stienen. 1994. Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit. Biophys. J. 67:2404-2410.
39. Reiser, P. J., R. L. Moss, G. G. Giulian, and M. L. Greaser. 1985. Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J. Biol. Chem. 260: 9077-9080.
40. Salviati, G., R. Betto, and D. Daniell-Betto. 1982. Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibers. Biochem. J. 207:261-272.
41. Shibata, T., W. C, Hunter, A. Yang, and K. Sagawa. 1987. Dynamic stiffness measured in central segment of excised rabbit papillary muscles during barium contracture. Circ. Res. 60:756-769.
42. Siemankowski, R. F., M. O. Wiseman, and H. D. White. 1985. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc. Natl. Acad. Sci. USA. 82:658-662.
43. Sinha, A. M., D. J. Friedman, J. M. Nigro, S. Jakovcic, M. Rabinowitz, and P. K. Umeda. 1984. Expression of rabbit ventricular α-myosin heavy chain messanger RNA sequences in atrial muscle. J. Biol. Chem. 259: 6674-6680.
44. Sleep, J., and H. Glyn. 1986. Inhibition of myofibrillar and actomyosin subfragment 1 adenosinetriphosphatase by adenosine 5′-diphosphate, pyrophosphate, and adenyl-5′-yl imdodiphosphate. Biochemistry. 25: 1149-1154.
45. Staron, R. S., and D. Pette. 1987. The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibers (rabbit soleus muscle). Biochem. J. 243:687-693.
46. Stienen, G. J. M., W. J. van der Laarse, and G. Elzinga. 1988. Dependence of the force-velocity relationship on MgATP in different types of muscle fibers from Xenopus laevis. Biophys. J. 53:849-855.
47. Wang, G., and M. Kawai. 1995. Temperature effect on elementary steps of the cross-bridge cycle in rabbit soleus muscle fibers. Biophys. J. 68:A17. (Abstr.)
48. Wang, G., Y. Zhao, and M. Kawai. 1994. Elementary steps of the cross-bridge cycle in rabbit soleus muscle fibers. Biophys. J. 66:A304. (Abstr.)
49. White, H. D., and E. W. Taylor. 1976. Energetics and mechanism of actomyosin adenosin triphosphate. Biochemistry. 15:5818-5826.
50. Wolff, M. R., K. S. McDonald, and R. L. Moss. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154-160.
51. Zhao, Y., and M. Kawai. 1993. The effect of the lattice spacing on cross-bridge kinetics in chemically skinned psoas fibers. II. Elementary steps affected by the spacing change. Biophys. J. 64:197-210.
52. Zhao, Y., and M. Kawai. 1994a. BDM affects nucleotide binding and force generation steps of the cross-bridge cycle in rabbit psoas muscle fibers. Am. J. Physiol. 266:C437-C447.
53. Zhao, Y., and M. Kawai. 1994b. The kinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. Biophys. J. 67:1655-1668.