Temperature dependence of speed of actin filaments propelled by slow and fast skeletal myosin isoforms

Journal of Applied Physiology

Volumn 99, Issue 6, 2005, Pages 2239-2245

  Rossi, R ^a   Maffei, M ^a   Bottinelli, R ^a,b   Canepari, M ^a,b  

^a UNIVERSITY OF PAVIA   (Italy)

^b Interuniversity Institute of Myology   (Italy)

Author keywords

In vitro motility; Temperature sensitivity

Indexed keywords

ADENOSINE TRIPHOSPHATE; MYOSIN; MYOSIN HEAVY CHAIN;

ACTIN FILAMENT; ANIMAL TISSUE; ARTICLE; ENERGY; FAST MUSCLE; KINETICS; MALE; NONHUMAN; PRIORITY JOURNAL; RABBIT; RAT; SKELETAL MUSCLE; SLOW MUSCLE; TEMPERATURE DEPENDENCE; TEMPERATURE SENSITIVITY; VELOCITY;

ANIMALS; KINETICS; MALE; MICROFILAMENTS; MOLECULAR MOTOR PROTEINS; MOTION; MUSCLE FIBERS, FAST-TWITCH; MUSCLE FIBERS, SLOW-TWITCH; MUSCLE, SKELETAL; MYOSINS; PROTEIN BINDING; PROTEIN ISOFORMS; RABBITS; RATS; RATS, WISTAR; TEMPERATURE;

EID: 28044446951     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/japplphysiol.00543.2005     Document Type: Article

References (43)

1. Anson M. Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin. J Mol Biol 224: 1029-1038, 1992.
2. Anson M and Canepari M. Studies of the temperature dependency of the velocity of regulated actin filaments moving in vitro on rabbit HMM. Molecular Interactions of Actin Conference, Maui, Hawaii, 1997.
3. Anson M, Drummond DR, Geeves MA, Hennessey ES, Ritchie MD, and Sparrow JC. Actomyosin kinetics and in vitro motility of wild-type Drosophila actin and the effects of two mutations in the Act88F gene. Biophys J 68: 1991-2003, 1995.
4. Barany M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol 50, Suppl: 197-218, 1967.
5. Bennett AF. Thermal dependence of muscle function. Am J Physiol Regul Integr Comp Physiol 247: R217-R229, 1984.
6. Bottinelli R, Betto R, Schiaffino S, and Reggiani C. Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. J Physiol 478: 341-349, 1994.
7. Bottinelli R, Canepari M, Pellegrino MA, and Reggiani C. Force-velocity properties of human skeletal muscle fibres: myosin heavy chain isoform and temperature dependence. J Physiol 495: 573-586, 1996.
8. Bottinelli R, Canepari M, Reggiani C, and Stienen GJ. Myofibrillar ATPase activity during isometric contraction and isomyosin composition in rat single skinned muscle fibres. J Physiol 481: 663-675, 1994.
9. Bottinelli R, Schiaffino S, and Reggiani C. Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle. J Physiol 437: 655-672, 1991.
10. Candau R, Iorga B, Travers F, Barman T, and Lionne C. At physiological temperatures the ATPase rates of shortening soleus and psoas myofibrils are similar. Biophys J 85: 3132-3141, 2003.
11. Canepari M, Rossi R, Pellegrino MA, Bottinelli R, Schiaffino S, and Reggiani C. Functional diversity between orthologous myosins with minimal sequence diversity. J Muscle Res Cell Motil 21: 375-382, 2000.
12. Canepari M, Rossi R, Pellegrino MA, Orrell RW, Cobbold M, Harridge S, and Bottinelli R. Effects of resistance training on myosin function studied using the in vitro motility assay in young and older men. J Appl Physiol 98: 2390-2395, 2005.
13. Canepari M, Rossi R, Pellegrino MA, Reggiani C, and Bottinelli R. Speeds of actin translocation in vitro by myosins extracted from single rat muscle fibres of different types. Exp Physiol 84: 803-806, 1999.
14. Debold EP, Dave H, and Fitts RH. Fiber type and temperature dependence of inorganic phosphate: implications for fatigue. Am J Physiol Cell Physiol 287: C673-C681, 2004.
15. Gibbs CL. Cardiac energetics. Physiol Rev 58: 174-254, 1978.
16. Guo B and Guilford WH. The tail of myosin reduces actin filament velocity in the in vitro motility assay. Cell Motil Cytoskeleton 59: 264-272, 2004.
17. Harrison SM and Bers DM. Modification of temperature dependence of myofilament Ca sensitivity by troponin C replacement. Am J Physiol Cell Physiol 258: C282-C288, 1990.
18. He ZH, Bottinelli R, Pellegrino MA, Ferenczi MA, and Reggiani C. ATP consumption and efficiency of human single muscle fibers with different myosin isoform composition. Biophys J 79: 945-961, 2000.
19. Homsher E, Nili M, Chen IY, and Tobacman LS. Regulatory proteins alter nucleotide binding to acto-myosin of sliding filaments in motility assays. Biophys J 85: 1046-1052, 2003.
20. Homsher E, Wang F, and Sellers JR. Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am J Physiol Cell Physiol 262: C714-C723, 1992.
21. Honda H and Asakura S. Calcium-triggered movement of regulated actin in vitro. A fluorescence microscopy study. J Mol Biol 205: 677-683, 1989.
22. Hook P and Larsson L. Actomyosin interactions in a novel single muscle fiber in vitro motility assay. J Muscle Res Cell Motil 21: 357-365, 1999.
23. Janmot C and d' Albis A. Electrophoretic separation of developmental and adult rabbit skeletal muscle myosin heavy chain isoforms: example of application to muscle denervation study. FEBS Lett 353: 13-15, 1994.
24. Johnston IA and Sidell BD. Differences in temperature dependence of muscle contractile properties and myofibrillar ATPase activity in a cold-temperature fish. J Exp Biol 111: 179-189, 1984.
25. Kawai M, Kawaguchi K, Saito M, and Ishiwata S. Temperature change does not affect force between single actin filaments and HMM from rabbit muscles. Biophys J 78: 3112-3119, 2000.
26. Kron SJ, Toyoshima YY, Uyeda TQ, and Spudich JA. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol 196: 399-416, 1991.
27. Margossian SS and Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol 85: 55-71, 1982.
28. Mutungi G and Ranatunga KW. Temperature-dependent changes in the viscoelasticity of intact resting mammalian (rat) fast- and slow-twitch muscle fibres. J Physiol 508: 253-265, 1998.
29. Pardee JD and Spudich JA. Purification of muscle actin. Methods Enzymol 85: 164-181, 1982.
30. Pate E, Wilson GJ, Bhimani M, and Cooke R. Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle. Biophys J 66: 1554-1562, 1994.
31. Pellegrino MA, Canepari M, Rossi R, D'Antona G, Reggiani C, and Bottinelli R. Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles. J Physiol 546: 677-689, 2003.
32. Ranatunga KW. Endothermic force generation in fast and slow mammalian (rabbit) muscle fibers. Biophys J 71: 1905-1913, 1996.
33. Ranatunga KW. The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures. J Physiol 351: 517-529, 1984.
34. Ranatunga KW. Temperature-dependence of shortening velocity and rate of isometric tension development in rat skeletal muscle. J Physiol 329: 465-483, 1982.
35. Ranatunga KW. Temperature dependence of mechanical power output in mammalian (rat) skeletal muscle. Exp Physiol 83: 371-376, 1998.
36. Schiaffino S and Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev 76: 371-423, 1996.
37. Stienen GJ, Kiers JL, Bottinelli R, and Reggiani C. Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence. J Physiol 493: 299-307, 1996.
38. Ter Keurs HE, Deis N, Landesberg A, Nguyen TT, Livshitz L, Stuyvers B, and Zhang ML. Force, sarcomere shortening velocity and ATPase activity. Adv Exp Med Biol 538: 583-602; discussion 602, 2003.
39. Thedinga E, Karim N, Kraft T, and Brenner B. A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers. J Muscle Res Cell Motil 20: 785-796, 1999.
40. Tikunov BA, Sweeney HL, and Rome LC. Quantitative electrophoretic analysis of myosin heavy chains in single muscle fibers. J Appl Physiol 90: 1927-1935, 2001.
41. Toyoshima YY, Kron SJ, McNally EM, Niebling KR, Toyoshima C, and Spudich JA. Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature 328: 536-539, 1987.
42. Wang G and Kawai M. Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibres. J Physiol 531:219-234, 2001.
43. Zar J. Biostatistical Analysis (4th ed.). Englewood Cliffs, NJ: Prentice-Hall, 1999.