Calcium regulation of skeletal muscle thin filament motility in vitro

Biophysical Journal

Volumn 72, Issue 3, 1997, Pages 1295-1307

  Gordon, Albert M ^a,b   LaMadrid, Marissa A ^a   Chen, Ying ^b   Luo, Zhaoxiong ^a   Chase, P Bryant ^a,b  

^a UNIVERSITY OF WASHINGTON   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM ION; PHALLOIDIN; RHODAMINE; TROPOMYOSIN; TROPONIN;

ACTIN MYOSIN INTERACTION; ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; CELL MOTILITY; CONTROLLED STUDY; FAST MUSCLE FIBER; IONIC STRENGTH; MUSCLE CONTRACTION; MUSCLE FORCE; MYOFILAMENT; NONHUMAN; PSOAS MUSCLE; RABBIT; SKELETAL MUSCLE; SKINNED MUSCLE FIBER; THIN FILAMENT;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0031055303     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78776-9     Document Type: Article

References (63)

1. Brandt, P. W., M. S. Diamond, J. S. Rutchik, and F. H. Schachat. 1987. Cooperative interations between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle. J. Mol. Biol. 195:885-896.
2. Brandt, P. W., M. S. Diamond, and F. H. Schachat. 1984. The thin filament of vertebrate skeletal muscle co-operatively activates as a unit. J. Mol. Biol. 180:379-384.
3. Bremel, R. D., J. M. Murray, and A. Weber. 1972. Manifestations of cooperative behavior in the regulated actin filament during actin-activated ATP hydrolysis in the presence of calcium. Cold Spring Harb. Symp. Quant. Biol. 37:267-275.
4. Bremel, R. D., and A. Weber. 1972. Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol. 238:91-101.
5. 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.
6. i solution. Biophys. J. 50:685-691.
7. Bukatina, A. E., and F. Fuchs. 1994. Effect of phalloidin on the ATPase activity of striated muscle myofibrils. J. Muscle Res. Cell Motil. 15: 29-36.
8. Bukatina, A. E., F. Fuchs, and P. W. Brandt. 1995. Thin filament activation by phalloidin in skinned cardiac muscle. J. Mol. Cell. Cardiol. 27: 1311-1315.
9. Butters, C. A., K. A. Willadsen, and L. S. Tobacman. 1993. Cooperative interactions between adjacent troponin-tropomyosin complexes may be transmitted through the actin filament. J. Biol. Chem. 268: 15565-15570.
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. Cooke, R., and E. Pate. 1985. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys. J. 48:789-798.
12. Ebashi, S., and M. Endo. 1968. Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18:123-183.
13. Fink, R. H. A., D. G. Stephenson, and D. A. Williams. 1986. Potassium and ionic strength effects on the isometric force of skinned twitch muscle fibres of the rat and toad. J. Physiol. (Lond.). 370:317-337.
14. Fraser, I. D. C., and S. B. Marston. 1995. In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium: the thin filament is switched as a single cooperative unit. J. Biol. Chem. 270:7836-7841.
15. Godt, R. E., and T. M. Nosek. 1989. Changes in intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J. Physiol. (Lond.). 412:155-180.
16. Gordon, A. M., R. E. Godt, S. K. B. Donaldson, and C. E. Harris. 1973. Tension in skinned frog muscle fibers in solutions of varying ionic strength and neutral salt composition. J. Gen. Physiol. 62:550-574.
17. Gordon, A. M., M. LaMadrid, Y. Chen, and P. B. Chase. 1996. Calcium regulation of skeletal thin filament sliding in vitro. FASEB J. 10:A129.
18. Grabarek, Z., T. Tao, and J. Gergely. 1992. Molecular mechanism of troponin-C function. J. Muscle Res. Cell Motil. 13:383-393.
19. Gulati, J., and A. Babu. 1984. Intrinsic shortening speed of temperature-jump-activated intact muscle fibers: effects of varying osmotic pressure with sucrose and KCl. Biophys. J. 45:431-445.
20. Gulati, J., and R. J. Podolsky. 1981. Isotonic contraction of skinned muscle fibers on a slow time base: effects of ionic strength and calcium. J. Gen. Physiol. 78:233-257.
21. Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49-68.
22. Harris, D. E., and D. M. Warshaw. 1993. Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J. Biol. Chem. 268:14764-14768.
23. Head, J. G., M. D. Ritchie, and M. A. Geeves. 1995. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur. J. Biochem. 227:694-699.
24. Heeley, D. H., M. H. Watson, A. S. Mak, P. Dubord, and L. B. Smillie. 1989. Effect of phosphorylation on the interaction and functional properties of rabbit striated muscle αα-tropomyosin. J. Biol. Chem. 264: 2424-2430.
25. Hill, L. E., J. P. Mehegan, C. A. Butters, and L. S. Tobacman. 1992. Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem. 267:16106-16113.
26. Homsher, E., B. Kim, A. Bobkova, and L. S. Tobacman. 1996. Calcium regulation of thin filament movement in an in vitro motility assay. Biophys. J. 70:1881-1892.
27. Homsher, E., F. Wang, and J. R. Sellers. 1992. Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am. J. Physiol. 262:C714-C723.
28. Honda, H., and S. Asakura. 1989. Calcium-triggered movement of regulated actin in vitro. A fluorescence microscopy study. J. Mol. Biol. 205:677-683.
29. Howard, J., A. J. Hunt, and S. Baek. 1993. Assay of microtubule movement driven by single kinesin molecules. Methods Cell Biol. 39:137-147.
30. Hunt, A. J., F. Gittes, and J. Howard. 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67:766-781.
31. Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. 7:255-318.
32. 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.
33. Kellermayer, M. S., and H. L. Granzier. 1996. Calcium-dependent inhibition of in vitro thin-filament motility by native titin. FEBS Lett. 380: 281-286.
34. Kron, S. J., Y. Y. Toyoshima, T. Q. P. Uyeda, and J. A. Spudich. 1991. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol. 196:399-416.
35. Leavis, P. C., and J. Gergeley. 1984. Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16:235-305.
36. 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature. 368:65-67.
37. Lehrer, S. S., and E. P. Morris. 1982. Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase. J. Biol. Chem. 257:8073-8080.
38. Margossian, S. S., and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:55-71.
39. 2+. Biophys. J. 67:1984-1993.
40. Martyn, D. A., R. Coby, L. L. Huntsman, and A. M. Gordon. 1993. Force-calcium relations in skinned twitch and slow-tonic frog muscle fibers have similar sarcomere length dependencies. J. Muscle Res. Cell Motil. 14:65-75.
41. 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.
42. Martyn, D. A., and A. M. Gordon. 1992. Force and stiffness in glycerinated rabbit psoas fibers. Effects of calcium and elevated phosphate. J. Gen. Physiol. 99:795-816.
43. 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.
44. 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.
45. 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.
46. Moss, R. L., G. M. Diffee, and M. L. Greaser. 1995. Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms. Rev. Physiol. Biochem. Pharmacol. 126:1-63.
47. Pan, B.-S., A. M. Gordon, and Z. Luo. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495.
48. Pardee, J. D., and J. A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85:164-181.
49. Pate, E., M. Bhimani, K. Franks-Skiba, and R. Cooke. 1995. Reduced effect of pH on skinned rabbit psoas muscle mechanics at high temperatures: implications for fatigue. J. Physiol. (Lond). 486:689-694.
50. Pate, E., G. J. Wilson, M. Bhimani, and R. Cooke. 1994. Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle. Biophys. J. 66:1554-1562.
51. Potter, J. D. 1982. Preparation of troponin and its subunits. Methods Enzymol. 85:241-263.
52. 2+ regulation of tension redevelopment rate in skinned skeletal muscle. Biophys. J. 71:2786-2794.
53. 2+ sensitivity of reconstituted thin filament. A study using a novel in vitro motility assay technique. Circ. Res. 76:626-633.
54. Sata, M., S. Sugiura, H. Yamashita, S. Momomura, and T. Serizawa. 1996. Coupling between myosin ATPase cycle and creatinine kinase cycle facilitates cardiac actomyosin sliding in vitro. A clue to mechanical dysfunction during myocardial ischemia. Circulation. 93:310-317.
55. Sata, M., H. Yamashita, S. Sugiura, H. Fujita, S. Momomura, and T. Serizawa. 1995b. A new in vitro motility assay technique to evaluate calcium sensitivity of the cardiac contractile proteins. Pflugers Arch. 429:443-445.
56. Schoenberg, M. 1991. Effect of ionic strength on skinned rabbit psoas fibers in the presence of magnesium pyrophosphate. Biophys. J. 60: 690-696.
57. Sellers, J. R., G. Cuda, F. Wang, and E. Homsher. 1993. Myosin-specific adaptations of the motility assay. Methods Cell Biol. 39:23-49.
58. Smillie, L. B. 1982. Preparation and identification of α-and β-tropomyosins. Methods Enzymol. 85:234-241.
59. Tobacman, L. S. 1996. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58:447-481.
60. Toyoshima, Y. Y., S. J. Kron, and J. A. Spudich. 1990. The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay. Proc. Natl Acad. Sci. USA. 87:7130-7134.
61. Uveda, T. Q. P., S. J. Kron, and J. A. Spudich. 1990. Myosin step size estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214:699-710.
62. Wang, F., B. M. Martin, and J. R. Seller. 1993. Regulation of actomyosin interactions in Limulus muscle proteins. J. Biol. Chem. 268:3776-3780.
63. Warrick, H. M., R. M. Simmons, J. T. Finer, T. Q. P. Uyeda, S. Chu, and J. A. Spudich. 1993. In vitro methods for measuring force and velocity of the actin-myosin interaction using purified proteins. In Motility Assays for Motor Proteins. Academic Press, San Diego, CA. 1-21.