Abstract
This chapter describes how perturbation analysis methods are used to characterize chemical reactions taking place in muscle fibers. The perturbations include the changes in concentrations of small ligands (ATP and phosphate), length (step and sinusoidal), force, pressure, and temperature. It further discusses the details of sinusoidal analysis, and its correlation with step analysis. It also discusses how series compliance affects the kinetic measurements.
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Abbott RH, Steiger GJ (1977) Temperature and amplitude dependence of tension transients in glycerinated skeletal and insect fibrillar muscle. J Physiol 266:13–42
Bershitsky SY, Tsaturyan AK (2002) The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit. J Physiol 540:971–988
Buchthal F (1951) The rheology of the cross striated muscle fibre and its minute structural interpretation. Pubbl Staz Zool Napoli 23:115–146
Buchthal F, Rosenfalck P (1957) Elastic properties of striated muscle. In: Tissue Elasticity (Am Physiol Soc) 73–97.
Dantzig J, Goldman Y, Millar NC, Lacktis J, Homsher E (1992) Reversal of the cross-bridge force-generating transition by the photogeneration of phosphate in rabbit psoas muscle fibers. J Physiol 451:247–278
Fortune NS, Geeves MA, Ranatunga KW (1991) Tension responses to rapid pressure release in glycerinated rabbit muscle fibers. Proc Natl Acad Sci (USA) 88:7323–7327
Galler S, Wang BG, Kawai M (2005) Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles. Biophys J 89:3248–3260
Goldman YE, Hibberd MG, Trentham DR (1984a) Initiation of active contraction by photogeneration of adenosine-5’-triphosphate in rabbit psoas muscle fibres. J Physiol 354:605–624
Goldman YE, Hibberd MG, Trentham DR (1984b) Relaxation of rabbit psoas muscle fibres from rigor by photochemical generation of adenosine-5’-triphosphate. J Physiol 354:577–604
Heinl P, Kuhn HJ, Ruegg JC (1974) Tension responses to quick length changes of glycerinated skeletal muscle fibres from the frog and tortoise. J Physiol 237:243–258
Hill AV (1949) The abrupt transition from rest to activity in muscle. Proc R Soc Lond B Biol Sci 136:399–420
Huxley AF (1957) Muscle structure and theories of contraction. Prog Biophys Chem 7:255–318
Huxley AF (1974) Muscular contraction. J Physiol 243:1–43
Huxley AF, Simmons RM (1971) Proposed mechanism of force generation in striated muscle. Nature 233:533–538
Huxley AF, Simmons RM (1972) Mechanical transients and the origin of muscular force. Cold Spring Hbr Symp on Quant Biol 37:669–680
Huxley HE, Stewart A, Sosa H, Irving T (1994) X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys J 67:2411–2421
Kawai M (1978) Head rotation or dissociation? A study of exponential rate processes in chemically skinned rabbit muscle fibers when MgATP concentration is changed. Biophys J 22:97–103
Kawai M (2003) What do we learn by studying the temperature effect on isometric tension and tension transients in mammalian striated muscle fibres?. J Muscle Res Cell Motil 24:127–138
Kawai M, Brandt PW (1980) Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J Muscle Res Cell Mot 1:279–303
Kawai M, Halvorson H (1989) Role of MgATP and MgADP in the crossbridge kinetics in chemically skinned rabbit psoas fibers. Study of a fast exponential process C. Biophys J 55:595–603
Kawai M, Halvorson HR (1991) Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned fibers of rabbit psoas. Biophys J 59:329–342
Kawai M, Saeki Y, Zhao Y (1993) Cross-bridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ Res 73:35–50
Kawai M, Zhao Y (1993) Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers. Biophys J 65:638–651
Lu X, Tobacman LS, Kawai M (2006) Temperature-dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant. Biophys J 91:4230–4240
Machin KE, Pringle JW (1960) The physiology of insect fibrillar muscle. III. The effect of sinusoidal changes of length on a beetle flight muscle. Proc R Soc Lond B Biol Sci 152:311–330
Piazzesi G, Lucii L, Lombardi V (2002) The size and the speed of the working stroke of muscle myosin and its dependence on the force. J Physiol 545:145–151
Podolsky RJ (1960) Kinetics of muscular contraction: the approach to the steady state. Nature 188:666–668
Pringle JW (1967) The contractile mechanism of insect fibrillar muscle. Prog Biophys Mol Biol 17:1–60
Thirlwell H, Corrie JE, Reid GP, Trentham DR, Ferenczi MA (1994) Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase. Biophys J 67:2436–2447
Thorson J, White DC (1969) Distributed representations for actin-myosin interaction in the oscillatory contraction of muscle. Biophys J 9:360–390
Wakabayashi K, Sugimoto Y, Tanaka H, Ueno Y, Takezawa Y, Amemiya Y (1994) X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J 67:2422–2435
Wang G, Ding W, Kawai M (1999) Does thin filament compliance diminish the cross-bridge kinetics? A study in rabbit psoas fibers. Biophys J 76:978–984
Wang G, Kawai M (2001) Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibres. J Physiol 531:219–234
Wang L, Kawai M (2013) A re-interpretation of the rate of tension redevelopment (kTR) in active muscle. J Muscle Res Cell Motil 34:407–415
White DC, Thorson J (1972) Phosphate starvation and the nonlinear dynamics of insect fibrillar flight muscle. J Gen Physiol 60:307–336
Zhao Y, Kawai M (1994) Kinetic and Thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. Biophys J 67:1655–1668
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Kawai, M. (2018). How to Characterize Chemical Reactions Occurring in Muscle Fibers?. In: Biomechanics, Muscle Fibers, and How to Interface Experimental Apparatus to a Computer. Springer, Cham. https://doi.org/10.1007/978-3-319-72036-4_3
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DOI: https://doi.org/10.1007/978-3-319-72036-4_3
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