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Volumn 82, Issue 4, 1997, Pages 1297-1304

Response of compressed skinned skeletal muscle fibers to conditions that simulate fatigue

Author keywords

force; inosine 5' monophosphate; lattice compression; mechanics; pH; phosphate; phosphorylation; velocity

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; INOSINE PHOSPHATE; MYOSIN SUBFRAGMENT;

EID: 0030901192     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1997.82.4.1297     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0025759975 scopus 로고
    • 4 concentration does not decrease force in cat skeletal muscle
    • Cell Physiol. 29
    • 4 concentration does not decrease force in cat skeletal muscle. Am. J. Physiol. 260 (Cell Physiol. 29): C805-C812, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Adams, G.R.1    Fisher, M.J.2    Meyer, R.A.3
  • 2
  • 3
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • Barany, M. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 58: 197-216, 1967.
    • (1967) J. Gen. Physiol. , vol.58 , pp. 197-216
    • Barany, M.1
  • 4
    • 0021363761 scopus 로고
    • Chemical energy usage and myosin light chain phosphorylation in mammalian skeletal muscle
    • Barsotti, R. J., and T. J. Butler. Chemical energy usage and myosin light chain phosphorylation in mammalian skeletal muscle. J. Muscle Res. Cell Motil. 5: 45-64, 1984.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 45-64
    • Barsotti, R.J.1    Butler, T.J.2
  • 5
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 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, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 6
    • 0024439203 scopus 로고
    • Changes in force and intracellular metabolites during fatigue in human skeletal muscle
    • Cady, E. B., D. A. Jones, J. Lynn, and D. J. Newham. Changes in force and intracellular metabolites during fatigue in human skeletal muscle. J. Physiol. (Lond.) 418: 311-325, 1989.
    • (1989) J. Physiol. (Lond.) , vol.418 , pp. 311-325
    • Cady, E.B.1    Jones, D.A.2    Lynn, J.3    Newham, D.J.4
  • 7
    • 0023218334 scopus 로고
    • ATP utilization during intermittent and continuous muscle contractions
    • Chasiotis, D., M. Bergstrom, and E. Hultman. ATP utilization during intermittent and continuous muscle contractions. Am. J. Physiol. 63: 167-174, 1987.
    • (1987) Am. J. Physiol. , vol.63 , pp. 167-174
    • Chasiotis, D.1    Bergstrom, M.2    Hultman, E.3
  • 9
    • 0017873220 scopus 로고
    • Generation of force by single-headed myosin
    • Cooke, R., and K. Franks. Generation of force by single-headed myosin. J. Mol. Biol. 120: 361-373, 1978.
    • (1978) J. Mol. Biol. , vol.120 , pp. 361-373
    • Cooke, R.1    Franks, K.2
  • 10
    • 0023839774 scopus 로고
    • The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate
    • Cooke, R., K. Franks, G. Luciani, and E. Pate. The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate. J. Physiol. (Lond.) 395: 77-97, 1988.
    • (1988) J. Physiol. (Lond.) , vol.395 , pp. 77-97
    • Cooke, R.1    Franks, K.2    Luciani, G.3    Pate, E.4
  • 11
    • 0020040724 scopus 로고
    • Chemical energetics of slow and fast twitch muscle of the mouse
    • Crow, M. T., and M. J. Kushmerick. Chemical energetics of slow and fast twitch muscle of the mouse. J. Gen. Physiol. 79: 147-166, 1982.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 147-166
    • Crow, M.T.1    Kushmerick, M.J.2
  • 12
    • 0020972752 scopus 로고
    • Correlated reduction of velocity of shortening and the rate of energy utilization in mouse fast-twitch muscle during a continuous tetanus
    • Crow, M. T., and M. J. Kushmerick. Correlated reduction of velocity of shortening and the rate of energy utilization in mouse fast-twitch muscle during a continuous tetanus. J. Gen. Physiol. 82: 703-720, 1983.
    • (1983) J. Gen. Physiol. , vol.82 , pp. 703-720
    • Crow, M.T.1    Kushmerick, M.J.2
  • 13
    • 0023684409 scopus 로고
    • Efficiency of work performance and contraction velocity in isotonic tetani of frog sartorius
    • Di Prampero, P. E., U. Boutellier, and A. Marguearat. Efficiency of work performance and contraction velocity in isotonic tetani of frog sartorius. Pflügers Arch. 412: 455-461, 1988.
    • (1988) Pflügers Arch. , vol.412 , pp. 455-461
    • Di Prampero, P.E.1    Boutellier, U.2    Marguearat, A.3
  • 14
    • 0021901742 scopus 로고
    • Influence of aerobic metabolism on IMP accumulation in fast-twitch muscle
    • Cell Physiol. 17
    • Dudley, G. A., and R. J. Terjung. Influence of aerobic metabolism on IMP accumulation in fast-twitch muscle. Am. J. Physiol. 248 (Cell Physiol. 17): C37-C42, 1985.
    • (1985) Am. J. Physiol. , vol.248
    • Dudley, G.A.1    Terjung, R.J.2
  • 15
    • 0016757376 scopus 로고
    • Heat production and chemical changes during isometric contractions of the human quadriceps muscle
    • Edwards, R. H. T., D. K. Hill, and D. A. Jones. Heat production and chemical changes during isometric contractions of the human quadriceps muscle. J. Physiol. (Lond.) 251: 303-315, 1975.
    • (1975) J. Physiol. (Lond.) , vol.251 , pp. 303-315
    • Edwards, R.H.T.1    Hill, D.K.2    Jones, D.A.3
  • 16
    • 0021213941 scopus 로고
    • Oxygen uptake of frog skeletal muscle fibres following tetanic contractions at 18°C
    • Elzinga, G., G. J. Langewaters, N. Westerhof, and A. Weichman. Oxygen uptake of frog skeletal muscle fibres following tetanic contractions at 18°C. J. Physiol. (Lond.) 346: 365-377, 1984.
    • (1984) J. Physiol. (Lond.) , vol.346 , pp. 365-377
    • Elzinga, G.1    Langewaters, G.J.2    Westerhof, N.3    Weichman, A.4
  • 17
    • 0028107645 scopus 로고
    • Cellular mechanisms of muscle fatigue
    • Fitts, R. H. Cellular mechanisms of muscle fatigue. Physiol. Rev. 74: 49-94, 1994.
    • (1994) Physiol. Rev. , vol.74 , pp. 49-94
    • Fitts, R.H.1
  • 18
    • 0026354162 scopus 로고
    • Decreased ATP cost of isometric contractions in ATP-depleted rat fast-twitch muscle
    • Cell Physiol, 30
    • Foley, J. M., S. J. Harkema, and R. A. Meyer. Decreased ATP cost of isometric contractions in ATP-depleted rat fast-twitch muscle. Am. J. Physiol. 261 (Cell Physiol, 30): C872-C881, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Foley, J.M.1    Harkema, S.J.2    Meyer, R.A.3
  • 19
    • 0019820645 scopus 로고
    • Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit
    • Godt, R. E., and D. W. Maughan. Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbit. Pflügers Arch. 391: 334-337, 1981.
    • (1981) Pflügers Arch. , vol.391 , pp. 334-337
    • Godt, R.E.1    Maughan, D.W.2
  • 20
    • 0024661091 scopus 로고
    • Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle
    • Godt, R. E., and T. M. Nosek. Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J. Physiol. (Lond.) 412: 155-180, 1989.
    • (1989) J. Physiol. (Lond.) , vol.412 , pp. 155-180
    • Godt, R.E.1    Nosek, T.M.2
  • 21
    • 0025974702 scopus 로고
    • Torque potentiation and myosin light-chain phosphorylation in human muscle following a fatiguing contraction
    • Houston, M. E., and R. W. Grange. Torque potentiation and myosin light-chain phosphorylation in human muscle following a fatiguing contraction. Can. J. Physiol. Pharmacol. 69: 269-273, 1991.
    • (1991) Can. J. Physiol. Pharmacol. , vol.69 , pp. 269-273
    • Houston, M.E.1    Grange, R.W.2
  • 22
    • 0021367101 scopus 로고
    • The relationship between ATP hydrolysis and active force in compressed and swollen skinned muscle fibers of the rabbit
    • Krasner, B., and D. W. Maughan. The relationship between ATP hydrolysis and active force in compressed and swollen skinned muscle fibers of the rabbit. Pflügers Arch. 400: 160-165, 1984.
    • (1984) Pflügers Arch. , vol.400 , pp. 160-165
    • Krasner, B.1    Maughan, D.W.2
  • 23
    • 0028108096 scopus 로고
    • 2+] on excitation-contraction coupling in skeletal muscle fibres of the rat
    • 2+] on excitation-contraction coupling in skeletal muscle fibres of the rat. J. Physiol. (Lond.) 478: 331-339, 1994.
    • (1994) J. Physiol. (Lond.) , vol.478 , pp. 331-339
    • Lamb, G.D.1    Stephenson, D.G.2
  • 24
    • 0026029850 scopus 로고
    • Force decline due to fatigue and intracellular acidification in isolated fibres from mouse skeletal muscle
    • Lannergen, J., and H. Westerblad. Force decline due to fatigue and intracellular acidification in isolated fibres from mouse skeletal muscle. J. Physiol. (Lond.) 434: 307-322, 1991.
    • (1991) J. Physiol. (Lond.) , vol.434 , pp. 307-322
    • Lannergen, J.1    Westerblad, H.2
  • 25
    • 0024157190 scopus 로고
    • Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibers: Effects of pH and ionic strength
    • Martyn, D. A., and A. M. Gordon. Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibers: effects of pH and ionic strength. J. Muscle Res. Cell Motil. 9: 428-445, 1988.
    • (1988) J. Muscle Res. Cell Motil. , vol.9 , pp. 428-445
    • Martyn, D.A.1    Gordon, A.M.2
  • 26
    • 0009521888 scopus 로고
    • Mechanism of chemomechanical coupling in skeletal muscle during work
    • edited by D. R. Lamb and C. V. Gisolfi. Dubuque, IA: Brown and Benchmark
    • Metzger, J. M. Mechanism of chemomechanical coupling in skeletal muscle during work. In: Perspectives in Exercise Science and Sports Medicine, edited by D. R. Lamb and C. V. Gisolfi. Dubuque, IA: Brown and Benchmark, 1992, vol. 5, p. 1-50.
    • (1992) Perspectives in Exercise Science and Sports Medicine , vol.5 , pp. 1-50
    • Metzger, J.M.1
  • 27
    • 0028065226 scopus 로고
    • Fatigue and recovery of phosphorous metabolites and pH during stimulation of rat skeletal muscle: An evoked electromyography and in vivo 31-P nuclear magnetic resonance spectroscopy study
    • Mizuno, T., Y. Takanashi, K. Yoshizaki, and M. Kondo. Fatigue and recovery of phosphorous metabolites and pH during stimulation of rat skeletal muscle: an evoked electromyography and in vivo 31-P nuclear magnetic resonance spectroscopy study. Eur. J. Appl. Physiol. Occup. Physiol. 69: 102-109, 1994.
    • (1994) Eur. J. Appl. Physiol. Occup. Physiol. , vol.69 , pp. 102-109
    • Mizuno, T.1    Takanashi, Y.2    Yoshizaki, K.3    Kondo, M.4
  • 28
    • 0021961219 scopus 로고
    • The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers
    • Persechini, A., J. T. Stull, and R. Cooke. The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers. J. Biol. Chem. 260: 7951-7954, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7951-7954
    • Persechini, A.1    Stull, J.T.2    Cooke, R.3
  • 29
    • 0028789904 scopus 로고
    • Influence of inorganic phosphate and pH on ATP utilization in fast and slow skeletal muscle fibers
    • Potma, E. J., I. A. van Graas, and G. J. Stienen. Influence of inorganic phosphate and pH on ATP utilization in fast and slow skeletal muscle fibers. Biophys. J. 69: 2580-2589, 1995.
    • (1995) Biophys. J. , vol.69 , pp. 2580-2589
    • Potma, E.J.1    Van Graas, I.A.2    Stienen, G.J.3
  • 30
    • 0027291841 scopus 로고
    • The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformation
    • Roulet, A., J. M. Burgat, and R. Cardinaud. The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformation. Eur. J. Biochem. 216: 89-101, 1993.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 89-101
    • Roulet, A.1    Burgat, J.M.2    Cardinaud, R.3
  • 31
    • 0017736664 scopus 로고
    • Myosin phosphorylation in skeletal muscle fibers
    • Stull, J. T., and C. T. High. Myosin phosphorylation in skeletal muscle fibers. Biochem. Biophys. Res. Commun. 77: 1078-1082, 1977.
    • (1977) Biochem. Biophys. Res. Commun. , vol.77 , pp. 1078-1082
    • Stull, J.T.1    High, C.T.2
  • 32
    • 0020481579 scopus 로고
    • Calcium-independent myosin light chain kinase of smooth muscle. Preparation by limited chymotryptic digestion of the calcium ion dependent enzyme, purification, and characterization
    • Walsh, M. P., R. Dabrowska, S. Hinkins, and D. J. Hartshorne. Calcium-independent myosin light chain kinase of smooth muscle. Preparation by limited chymotryptic digestion of the calcium ion dependent enzyme, purification, and characterization. Biochemistry 21: 1919-1925, 1982.
    • (1982) Biochemistry , vol.21 , pp. 1919-1925
    • Walsh, M.P.1    Dabrowska, R.2    Hinkins, S.3    Hartshorne, D.J.4
  • 33
    • 0022858316 scopus 로고
    • IMP production and energy metabolism during exercise in rats in relation to age
    • Westra, H. G., A. de Haan, J. E. van Doorn, and E. J. de Haan. IMP production and energy metabolism during exercise in rats in relation to age. Biochem. J. 239: 751-755, 1986.
    • (1986) Biochem. J. , vol.239 , pp. 751-755
    • Westra, H.G.1    De Haan, A.2    Van Doorn, J.E.3    De Haan, E.J.4
  • 34
    • 0028835997 scopus 로고
    • Inhibition of muscle force by vanadate
    • Wilson, G. J., S. E. Shull, and R. Cooke. Inhibition of muscle force by vanadate. Biophys. J. 68: 216-226, 1995.
    • (1995) Biophys. J. , vol.68 , pp. 216-226
    • Wilson, G.J.1    Shull, S.E.2    Cooke, R.3
  • 35
    • 0027402667 scopus 로고
    • The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers
    • Zhao, Y., and M. Kawai. The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. Biophys. J. 64: 197-210, 1993.
    • (1993) Biophys. J. , vol.64 , pp. 197-210
    • Zhao, Y.1    Kawai, M.2
  • 36
    • 0027933737 scopus 로고
    • Kinetics and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers
    • Zhao, Y., and M. Kawai. Kinetics and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. Biophys. J. 67: 1655-1668, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 1655-1668
    • Zhao, Y.1    Kawai, M.2


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