Regulation of force and unloaded sliding speed in single thin filaments: Effects of regulatory proteins and calcium

Journal of Physiology

Volumn 524, Issue 1, 2000, Pages 233-243

  Homsher, Earl ^a   Lee, David M ^a   Morris, Carl ^a   Pavlov, Dmitry ^a   Tobacman, Larry S ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ASPARAGINE; CALCIUM ION; F ACTIN; ISOLEUCINE; MYOSIN; MYOSIN HEAVY CHAIN; REGULATOR PROTEIN; TROPONIN; TROPOMYOSIN;

ACTIN FILAMENT; ANIMAL TISSUE; ARTICLE; CATTLE; MUSCLE FORCE; MUSCLE ISOMETRIC CONTRACTION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; RABBIT; THIN FILAMENT; ALLOSTERISM; ANIMAL CELL; CALCIUM BINDING; CELL ACTIVATION; CONTROLLED STUDY; FORCE; IONIC STRENGTH; ISOMETRIC FORCE; PROTEIN FUNCTION; PROTEIN INTERACTION; REGULATORY MECHANISM; SLIDING SPEED; VELOCITY;

EID: 0034177712     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.2000.00233.x     Document Type: Article

References (47)

1. BARANY, M. (1967). ATPase activity of myosin correlated with speed of muscle shortening. Journal of General Physiology 50, 197-218.
2. 2+-dependent effects on actin-tropomyosin filament motility. Biochemical Journal 327, 335-340.
3. 2+ regulation of thin filament motility. Biochemical and Biophysical Research Communications 236, 760-764.
4. 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction. Proceedings of the National Academy of Sciences of the USA 85, 3265-3269.
5. BRENNER, H., SCHOENBERG, M., CHALOVICH, J. M., GREENE, L. K. & EISNBERG, K. (1982). Evidence for crossbridge attachment in relaxed muscle at low ionic strength. Proceedings of the National Academy of Sciences of the USA 79, 88-91.
6. CHALOVICH, J. M., CHOCK, B. & EISENBERG, K. (1981). Mechanism of action of troponin-tropomyosin: inhibition of actomyosin ATPase without inhibition of myosin binding to actin. Journal of Biological Chemistry 256, 575-578.
7. CHALOVICH, J. M. & EISENBERG, E. (1982). Mechanism of action of troponin-tropomyosin: Inhibition of actomyosin ATPase activity without blocking the binding of myosin to actin. Journal of Biological Chemistry 257, 2432-2437.
8. EDMAN, K. A. P. (1979). The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. Journal of Physiology 291, 143-159.
9. FINK, R. H., STEPHENSON, D. G. & WILLIAMS, D. A. (1986). Potassium and ionic strength effects on the isometric force of skinned twitch muscle fibres of the rat and toad. Journal of Physiology 370, 317-337.
10. FRASER, I. D. C. & MARSTON, S. B. (1995). In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. Journal of Biological Chemistry 270, 7836-7841.
11. GORDON, A. M., HUXLEY, A. V. & JULIAN, F. J. (1966). Tension development in highly stretched vertebrate muscle fibres. Journal of Physiology 184, 143-169.
12. GORDON, A. M., LAMADRID, M. A., CHEN, Y., LUO, Z. & CHASE, P. B. (1997). Calcium regulation of skeletal muscle thin filament motility in vitro. Biophysical Journal 72, 1295-1307.
13. 2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers. Journal of General Physiology 97, 1141-1163.
14. HOMSHER, E., KIM, B., BOBKOVA, K. & TOBACMAN, L. S. (1996). Calcium regulation of thin filament movement in an in vitro motility assay. Biophysical Journal 70, 1881-1892.
15. HOWARD, J. & HUDSPETH, A. J. (1988). Compliance of the hair bundle associated with gating of mechanoelectrical transduction channels in the bullfrog's saccular hair cell. Neuron 1, 189-199.
16. HUXLEY, A. K. (1957). Muscle, structure and theories of contraction. Progress in Biophysical Chemistry 7, 255-318.
17. HUXLEY, H. E. (1972). Structural changes in the actin-and myosin-containing filaments during contraction. Cold Spring Harbor Symposium on Quantitative Biology 37, 361-376.
18. 2+: Statistical mechanical analysis of a troponin C site II mutant. Biophysical Journal 70, 1447-1455.
19. ISAMBERT, H., VENIER, P., MAIKIS, A. C., FATTOUM, A., KASSAB, R., PANTALONI, D. & CARLIER, M. F. (1995). Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. Journal of Biological Chemistry 270, 11437-11444.
20. JULIAN, F. J. (1971). The effect of calcium on the force-velocity relation of briefly glycerinated frog muscle fibres. Journal of Physiology 218, 117-145.
21. KRON, S. J., TOYOSHIMA, Y. Y., UYEDA, T. Q. P. & SPUDICH, J. A. (1991). Assays for actin sliding movement over myosin-coated surfaces. Methods in Enzymology 196, 399-416.
22. LEHRER, S. & MORRIS, K. P. (1982). Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase. Journal of Biological Chemistry 257, 8073-8080.
23. LIN, D., BOBKOVA, A., HOMSHER, E. & TOBACMAN, L. H. (1996). Altered cardiac troponin T in vitro function in the presence of a mutation implicated in familial hypertrophic cardiomyopathy. Journal of Clinical Investigation 97, 2842-2848.
24. MA, Y. & TAYLOR, E. W. (1994). Kinetic mechanism of myofibril ATPase. Biophysical Journal 66, 1542-1553.
25. MARGOSSIAN, S. S. & LOWEY, S. (1982). Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods in Enzymology 85, 55-71.
26. MILLAR, N. C. & HOMSHER, E. (1990). The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. Journal of Biological Chemistry 265, 20234-20240.
27. MILLER, C. J. & REISLER, K. (1995). Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin. Biochemistry 34, 2694-2700.
28. MOSS, R. L. (1986). Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin filament activation. Journal of Physiology 377, 487-505.
29. 2+ regulation of mechanical properties of striated muscle: mechanistic studies using extraction and replacement of regulatory proteins. Circulation Research 70, 865-884.
30. PARDEE, J. D. & SPUDICH, J. A. (1982). Purification of muscle actin. Methods in Cell Biology 24, 271-289.
31. PATE, E. & COOKE, H. (1989). A model of crossbridge action: the effects of ATP, ADP, and Pi. Journal of Muscle Research and Cell Motility 10, 181-196.
32. PODOLSKY, R. J. & TEICHHOLZ, L. K. (1970). The relation between calcium and contraction kinetics in skinned muscle fibres. Journal of Physiology 211, 19-35.
33. 2+ regulation of muscle contraction. Journal of Biological Chemistry 270, 2557-2562.
34. PUTKEY, J. A., SWEENEY, H. L. & CAMPBELL, S. T. (1989). Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C. Journal of Biological Chemistry 264, 12370-12378.
35. REGNIER, M., LEE, D. M. & HOMSHER, K. (1998). ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis. Biophysical Journal 74, 3044-3058.
36. SIEMANKOWSKI, R. V., WISEMAN, M. O. & WHITE, H. D. (1985). ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscles. Proceedings of the National Academy of Sciences of the USA 82, 658-662.
37. SWARTZ, D. R. & MOSS, R. L. (1992). Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers. Journal of Biological Chemistry 267, 20497-20506.
38. SWEENEY, H. L., FENG, H. H., YANG, Z. & WATKINS, H. (1998). Functional analyses of troponin T mutations that cause hypertrophic cardiomyopathy: insights into disease pathogenesis and troponin function. Proceedings of the National Academy of Sciences of the USA 95, 14406-14410.
39. TOBACMAN, L. S. & ADELSTEIN, R. S. (1986). Mechanism of regulation of cardiac actin-myosin subfragment 1 by troponin-tropomyosin. Biochemistry 25, 798-802.
40. TOBACMAN, L. S., LIN, D., BUTTERS, C., LANDIS, C., BACK, N. & HOMSHER, K. (1999). Functional consequences of troponin T mutations found in hypertrophic cardiomyopathy. Journal of Biological Chemistry 274, 28363-28370.
41. UYEDA, T. Q. P., KRONS, S. J. & SPUDICH, J. A. (1990). Myosin step size: estimation from slow sliding movement of actin over low densities of heavy meromyosin. Journal of Molecular Biology 214, 699-710.
42. VANBUREN, P., GUILFORD, W. H., KENNEDY, G., WU, J. & WARSHAW, D. M. (1994). Enhanced force generation by smooth muscle myosin in vitro. Proceedings nf the National Academy of Sciences of the USA 91, 202-205.
43. 2+ on the kinetics of phosphate release in skeletal muscle. Journal of Biological Chemistry 276, 2459-2460.
44. WANG, Y. P. & FUCHS, F. (1994). Length, force, and Ca(2+)-troponin C affinity in cardiac and slow skeletal muscle. American Journal of Physiology 266, C1077-1082.
45. WILLIAMS, D. L., GREENE, L. E. & EISENBERG, E. (1988). Cooperative turning on of myosin subfragment 1 adenosinetriphosphatase activity by the troponin-tropomyosin-actin complex. Biochemistry 27, 6987-6993.
46. WOLEDGE, R. C., CURTIN, X. A. & HOMSHER, E. (1985). Energetic Aspects of Muscle Contraction, pp. 1-329. Academic Press, San Diego.
47. XU, C., CRAIG, H., TOBACMAN, L., HOROWICZ, K. & LEHMAN, W. (1999). Tropomyosin positions in regulated thin filaments revealed by eryoelectron microscopy. Biophysical Journal 77, 985-992.