Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle

Biophysical Journal

Volumn 74, Issue 4, 1998, Pages 2005-2015

  Regnier, M ^a,c   Martyn, D A ^a   Chase, P B ^b,c  

^a University of Washington   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; DEOXYADENOSINE TRIPHOSPHATE; MYOSIN ADENOSINE TRIPHOSPHATASE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; KINETICS; MUSCLE CONTRACTION; MUSCLE TONE; NONHUMAN; PSOAS MUSCLE; RABBIT;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0031920485     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77907-X     Document Type: Article

References (58)

1. Araujo, A., and J. W. Walker. 1996. Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium. Biophys. J. 70:2316-2326.
2. Brenner, B. 1983. Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers. Biophys. J. 41: 99-102.
3. 1) and curvature (b). Basic Res. Cardiol 81:54-69.
4. 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA. 85:3265-3269.
5. Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
6. Brozovich, F. V., L. D. Yates, and A. M. Gordon. 1988. Muscle force and stiffness during activation and relaxation. Implications for the actomyosin ATPase. J. Gen. Physiol. 91:399-420.
7. Caceci, M. S., and W. P. Cacheris. 1984. Fitting curves to data. In Byte. 340-362.
8. Chalovich, J. M. 1992. Actin mediated regulation of muscle contraction. Pharmacol. Ther. 55:95-148.
9. Chase, P. B., and M. J. Kushmerick. 1988. Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys. J. 53:935-946.
10. Chase, P. B., and M. J. Kushmerick. 1995. Effect of physiological ADP levels on contraction of single skinned fibers from rabbit fast and slow muscles. Am. J. Physiol. 268:C480-C489.
11. 2+. Biophys. J. 67:1994-2001.
12. Chase, P. B., D. A. Martyn, M. J, Kushmerick, and A. M. Gordon. 1993. Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit. J. Physiol. (Lond.). 460:231-246.
13. Dantzig, J. A., Y. E. Goldman, N. C. Millar. J. Lacktis, and E. Homsher. 1992. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J. Physiol. (Lond.). 451:247-278.
14. Dantzig, J. A., M. G. Hibberd, D. R. Trentham, and Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by pho- tolysis of caged ATP in rabbit psoas muscle fibres. J. Physiol. (Lond.). 432:639-680.
15. Edman, K. A. P. 1979. The velocity of unloaded shortening and its relation to sarcomerc length and isometric force in vertebrate muscle fibres. J. Physiol. (Lond.). 291:143-159.
16. El-Saleh, S. C., and R. J. Solaro. 1987. Calmidazolium, a calmodulin antagonist, stimulates calcium-troponin C and calcium-calmodulin- dependent activation of striated muscle myofilaments. J. Biol. Chem. 262:17240-17246.
17. Farah, C. S., and F. C. Reinach. 1995. The troponin complex and regulation of muscle contraction. FASEB J. 9:755-767.
18. Farrow, A. J., G. H. Rossmanith, and J. Unsworth. 1988. The role of calcium ions in the activation of rabbit psoas muscle. J. Muscle Res. Cell Motil. 9:261-274.
19. Ferenczi, M. A., Y. E. Goldman, and R. M. Simmons. 1984a. The dependence of force and shortening velocity on substrate concentration in skinned muscle fibres from Rana temporaria. J. Physiol. (Lond.). 350: 519-543.
20. Ferenzi, M. A., E. Homsher, and D. R. Trentham. 1984b. The kinetics of magnesium adenosine triphosphate cleavage in skinned muscle fibres of the rabbit. J. Physiol. (Lond.). 352:575-599.
21. Fortune, N. S., M, A. Geeves, and K. W. Ranatunga. 1994. Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure. J. Physiol. (Lond.). 474:283-290.
22. Geeves, M. A., and P. B. Conibear. 1995. The role of three-state docking of myosin SI with actin in force generation. Biophys. J. 68:194s-201s.
23. Godt, R. E. 1974. Calcium-activated tension of skinned muscle fibers of the frog: dependence on magnesium adenosine triphosphate concentration. J. Gen. Physiol. 63:722-739.
24. Goldman, Y. E., M. G. Hibberd, and D. R. Trentham. 1984. Initiation of active contraction by photogeneration of adenosine-5'-triphosphate in rabbit psoas muscle fibres. J. Physiol. (Lond.). 354:605-624.
25. Grabarek, Z., T. Tao, and J. Gergely. 1992. Molecular mechanism of troponin-C function. J. Muscle Res. Cell Motil. 13:383-393.
26. Hancock, W. O., L. L. Huntsman, and A. M. Gordon. 1997. Models of calcium activation account for differences between skeletal and cardiac force redevelopment kinetics. J. Muscle Res. Cell Motil. (in press).
27. Homsher, E., J. Lacktis, and M. Regnier. 1997. Strain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers. Biophys. J. 72:1780-1791.
28. 2+-specific regulatory sites of troponin C. J. Biol. Chem. 269:8919-8923.
29. Julian, F. J. 1971. The effect of calcium on the force-velocity relation of briefly glycerinated frog muscle fibres. J. Physiol. (Lond.). 218: 117-145.
30. Julian, F. J., and R. L. Moss. 1981. Effects of calcium and ionic strength on shortening velocity and tension development in frog skinned muscle fibres. J. Physiol. (Lond.). 311:179-199.
31. Julian, F. J., L. C. Rome, D. G. Stephenson, and S. Stritz. 1986. The influence of free calcium on the maximum speed of shortening in skinned frog muscle fibres. J. Physiol. (Lond.). 380:257-273.
32. Landesberg, A., and S. Sideman. 1994. Coupling calcium binding to troponin C and cross-bridge cycling in skinned cardiac cells. Am. J. Physiol. 266:H1260-H1271.
33. 2+. Biophys. J. 67:1984-1993.
34. Martyn, D. A., and A. M. Gordon. 1988. Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: effects of pH and ionic strength. J. Muscle Res. Cell Motil. 9:428-445.
35. Matsubara, I., Y. Umazume, and N. Yagi. 1985. Lateral filamentary spacing in chemically skinned murine muscles during contraction. J. Physiol. (Lond.). 360:135-148.
36. McKillop, D. F. A., and M. A. Geeves. 1993. Regulation of the interaction between actin and myosin subfragment 1 : evidence for three states of the Thin filament. Biophys. J. 65:693-701.
37. Metzger, J. M. 1996. Effects of phosphate and ADP on shortening velocity during maximal and submaximal calcium activation of the thin filament in skeletal muscle fibers. Biophys. J. 70:409-417.
38. Metzger, J. M., M. L. Greaser, and R. L. Moss. 1989. Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers: implications for twitch potentiation in intact muscle. J. Gen. Physiol. 93:855-883.
39. Metzger, J. M., and R. L. Moss. 1988. Thin filament regulation of shortening velocity in rat skinned skeletal muscle: effects of osmotic compression. J. Physiol. (Lond.). 398:165-175.
40. 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.
41. 2+-sensitive cross-bridge state transition in skeletal muscle fibers: effects due to variations in thin filament activation by extraction of troponin C. J. Gen. Physiol. 98:233-248.
42. Metzger, J. M., and R. L. Moss. 1992. Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys. J. 63:460-468.
43. Millar, N. C., and E. Homsher. 1990. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. J. Biol. Chem. 265:20234-20240.
44. Moss, R. L. 1986. Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation. J. Physiol. (Lond.). 377:487-505.
45. Moss, R. L., and R. A. Haworth. 1984. Contraction of rabbit skinned skeletal muscle fibers at low levels of magnesium adenosine triphosphate. Biophys. J. 45:733-742.
46. Regnier, M., P. B. Chase, and D. A. Martyn. 1997. Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] substrate in skinned fibers from rabbit psoas muscle. Biophys. J. 72:A379.
47. Regnier, M., and E. Homsher. 1998. The effect of ATP analogues on post-hydrolytic and force development steps in skinned skeletal muscle fibers, Biophys. J. (in press).
48. Regnier, M., D. M. Lee, and E. Homsher. 1998. ATP analogues and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis. Biophys. J. (in press).
49. 2+ regulation of tension redevelopment rate in skinned skeletal muscle. Biophys. J. 71:2786-2794.
50. Regnier, M., C. Morris, and E. Homsher. 1995. Regulation of the crossbridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers. Am. J. Physiol. 269:C1532-C1539.
51. 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.
52. Swartz, D. R., and R. L. Moss. 1992. Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers. J. Biol. Chem. 267:20497-20506.
53. Sweeney, H. L., and J. T. Stull. 1990. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc. Natl. Acad. Sci. USA. 87:414-418.
54. Tobacman, L. S. 1996. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58:447-481.
55. 2+-activated fast and slow skeletal muscle fibers. Biophys. J. 72:822-834.
56. Wahr, P. A., J. D. Johnson, and J. A. Rail. 1993. Calmidazolium binding to troponin (Tn) decreases relaxation rates in skinned frog muscle fibers. Biophys. J. 64:A24.
57. 2+ on the kinetics of phosphate release in skeletal muscle. J. Biol. Chem. 267:2459-2466.
58. Wise, R. M., J. F. Rondinone, and F. N. Briggs. 1971. Effect of calcium on force-velocity characteristics of glycerinated skeletal muscle. Am. J. Physiol. 221:973-979.