Force responses following stepwise length changes of rat skeletal muscle fibre types

Journal of Physiology

Volumn 493, Issue 1, 1996, Pages 219-227

  Galler, Stefan ^a   Hilber, Karlheinz ^a   Pette, Dirk ^b  

^a UNIVERSITY OF SALZBURG   (Austria)

^b UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; MYOSIN HEAVY CHAIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BIOMECHANICS; CONTROLLED STUDY; KINETICS; MUSCLE FORCE; MUSCLE ISOMETRIC CONTRACTION; MUSCLE LENGTH; NONHUMAN; PRIORITY JOURNAL; RAT; SKELETAL MUSCLE; THIN FILAMENT; TIME;

EID: 0029968751     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.1996.sp021377     Document Type: Article

References (29)

1. BOTTINELLI, R., BETTO, R., SCHIAFFINO, S. & REGGIANI, C. (1994a). Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. Journal of Physiology 478, 341-349.
2. BOTTINELLI, R., CANEPARI, M., REGGIANI, C. & STIENEN, G. J. M. (19944). Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres. Journal of Physiology 481, 663-675.
3. BRENNER, B. (1991). Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: A newly observed facet of cross-bridge action in muscle. Proceedings of the National Academy of Sciences of the USA 88, 10490-10494.
4. EDMAN, K. A. P. (1979). The velocity of unloaded shortening and its relations to sarcomere length and isometric force in vertebrate muscle fibres. Journal of Physiology 291, 143-159.
5. EDMAN, K. A. P., REGGIANI, C., SCHIAFFINO, S. & TE KRONNIE, G. (1988). Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres. Journal of Physiology 395, 679-694.
6. EISENBERG, E., HILL, T. L. & CHEN, Y. (1980), Cross-bridge model of muscle contraction. Quantitative analysis. Biophysical Journal 29, 195-227.
7. FORD, L. E., HUXLEY, A. F. & SIMMONS, R. M. (1977). Tension responses to sudden length change in stimulated frog muscle fibres near slack length. Journal of Physiology 269, 441-515.
8. FORD, L. E., HUXLEY, A. F. & SIMMONS, R. M. (1981). The relation between stiffness and filament overlap in stimulated frog fibres. Journal of Physiology 311, 219-249.
9. FORD, L. E., NAKAGAWA, K., DESPER, J. & SEOW, C. Y. (1991). Effect of osmotic compression on the force-velocity properties of glycerinated rabbit skeletal muscle cells. Journal of General Physiology 97, 73-88.
10. GALLER, S. (1994). Stretch activation of skeletal muscle fibre types. Pflügers Archiv 427, 384-386.
11. GALLER, S. & HILBER, K. (1994). Unloaded shortening of skinned mammalian skeletal muscle fibres: effects of the experimental approach and passive force. Journal of Muscle Research and Cell Motility 15, 400-412.
12. 2+-dependent force development of skinned muscle fibre preparations. Journal of Experimental Biology 152, 255-264.
13. GALLER, S., SCHMITT, T. L. & PETTE, D. (1994), Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibres. Journal of Physiology 478, 513-521.
14. HEINL, P., KUHN, H. J. & RÜEGG, J. C. (1974). Tension responses to quick length changes of glycerinated skeletal muscle fibres from the frog and tortoise. Journal of Physiology 237, 243-258.
15. HUXLEY, A. F. & SIMMONS, R. M. (1971). Proposed mechanism of force generation in striated muscle. Nature 233, 533-538.
16. HUXLEY, H. E. (1969). The mechanism of muscular contraction. Science 164, 1356-1366.
17. IRVING, M., ALLEN T. S. C., SABIDO-DAVID, C., CRAIK, J. S., BRANDMEIER, B., KENDRICK-JONES, J., CORRIE, J. E. T., TRENTHAM, D. R. & GOLDMAN, Y. E. (1995). Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature 375, 688-691.
18. IRVING, M., LOMBARDI, V., PIAZZESI, G. & FERENCZI, M. A. (1992). Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature 357, 156-158.
19. LOMBARDI, V., PIAZZESI, G. & LINARI, M. (1992). Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature 355, 638-641.
20. MCNALLY, E. M., KRAFT, R., BRAVO-ZEHNDER, M., TAYLOR, D. A. & LEINWAND, L. A. (1989). Full-length rat alpha and beta cardiac myosin heavy chain sequences. Journal of Molecular Biology 210, 665-671.
21. MARTYN, D. A. & GORDON, A. M. (1992). Force and stiffness in glycerinated rabbit psoas fibers: Effects of calcium and elevated phosphate. Journal of General Physiology 99, 795-816.
22. METZGER, J. M. & Moss, R. L. (1990). Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibres. Science 247, 1088-1090.
23. MOISESCU, D. G. & THIELECZEK, R. (1978). Calcium and strontium concentration changes within skinned muscle preparations following a change in the external bathing solution. Journal of Physiology 275, 241-262.
24. OAKLEY, B. R., KIRSCH, D. R. & MORRIS, N. R. (1980). A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Analytical Biochemistry 105, 361-363.
25. PETTE, D. & STARON, R. S. (1990). Cellular and molecular diversities of mammalian skeletal muscle fibres. Reviews of Physiology, Biochemistry and Pharmacology 116, 1-76.
26. RAYMENT, I., HOLDEN, H. M., WHITTAKER, M., YOHN, C. B., LORENZ, M., HOLMES, K. C. & MILLIGAN, R. A. (1993). Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65.
27. SAITO, K., AOKI, T. & YANAGIDA, T. (1994). Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. Biophysical Journal 66, 769-777.
28. SCHIAFFINO, S., GORZA, L., SARTORE, S., SAGGIN, L., AUSONI, S., VIANELLO, M., GUNDERSEN, K. & LÔMO, T. (1989). Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. Journal of Muscle Research and Cell Motility 10, 197-205.
29. TERMIN, A., STARON, R. S. & PETTE, D. (1989). Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 92, 453-457.