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Volumn 70, Issue 5, 1996, Pages 2316-2326

Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; PHOSPHATE;

EID: 0029924005     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79797-7     Document Type: Article
Times cited : (36)

References (34)
  • 2
    • 0023738191 scopus 로고
    • Kinetics of ATP hydrolysis and tension production in skinned cardiac muscle of the guinea pig
    • Barsotti, R. J., and M. A. Ferenczi. 1988. Kinetics of ATP hydrolysis and tension production in skinned cardiac muscle of the guinea pig. J. Biol. Chem. 263:16750-16756.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16750-16756
    • Barsotti, R.J.1    Ferenczi, M.A.2
  • 3
    • 0023783575 scopus 로고
    • Demembranated muscle fibers catalyze a more rapid exchange between phosphate and ATP than actomyosin subfragment 1
    • Bowater, R., and J. Sleep. 1988. Demembranated muscle fibers catalyze a more rapid exchange between phosphate and ATP than actomyosin subfragment 1. Biochemistry. 27:5314-5323.
    • (1988) Biochemistry , vol.27 , pp. 5314-5323
    • Bowater, R.1    Sleep, J.2
  • 4
    • 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) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 5
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers
    • Dantzig, J. A., Y. E. Goldman, N. C. Millar, J. Laktis, and E. Homsher 1992. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers. J. Physiol. 451:247-278.
    • (1992) J. Physiol. , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Laktis, J.4    Homsher, E.5
  • 8
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total0 ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. 1988. Computer programs for calculating total from specified free or free from specified total0 ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol. 157: 378-417.
    • (1988) Methods Enzymol. , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 10
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd, M. G., J. A. Dantzig, D. R., Trentham, and Y. E. Goldman. 1985. Phosphate release and force generation in skeletal muscle fibers. Science. 228:1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Trentham, D.R.3    Goldman, Y.E.4
  • 11
    • 0022463569 scopus 로고
    • Relationships between chemical and mechanical events during muscular contraction
    • Hibberd, M. G., and D. R. Trentham. 1986. Relationships between chemical and mechanical events during muscular contraction. Annu. Rev. Biophys. Biophys. Chem. 15:119-161.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 119-161
    • Hibberd, M.G.1    Trentham, D.R.2
  • 12
    • 0025366578 scopus 로고
    • Caged compounds and striated muscle contraction
    • Homsher, E., and N. C. Millar. 1990. Caged compounds and striated muscle contraction. Annu. Rev. Physiol. 52:875-896.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 875-896
    • Homsher, E.1    Millar, N.C.2
  • 13
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Stimmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Stimmons, R.M.2
  • 14
    • 0026073088 scopus 로고
    • Two step mechanism of phosphate release and mechanism of force generation in chemically skinned fibers of rabbit psoas muscle
    • Kawai, M., and H R. Halvorson. 1991. Two step mechanism of phosphate release and mechanism of force generation in chemically skinned fibers of rabbit psoas muscle. Biophys. J. 59:329-342.
    • (1991) Biophys. J. , vol.59 , pp. 329-342
    • Kawai, M.1    Halvorson, H.R.2
  • 15
    • 0027216259 scopus 로고
    • Cross-bridge scheme and kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret
    • Kawai, M., Y. Saeki, and Y. Zhao. 1993. Cross-bridge scheme and kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ. Res. 73:35-50.
    • (1993) Circ. Res. , vol.73 , pp. 35-50
    • Kawai, M.1    Saeki, Y.2    Zhao, Y.3
  • 16
    • 0022560216 scopus 로고
    • The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle
    • Kentish, J A. 1986. The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle. J. Physiol. 370:585-604.
    • (1986) J. Physiol. , vol.370 , pp. 585-604
    • Kentish, J.A.1
  • 18
    • 0027315793 scopus 로고
    • Tension transients initiated by photorelease of MgADP in skinned skeletal muscle fibers
    • Lu. Z., R. L. Moss, and J. W. Walker. 1993. Tension transients initiated by photorelease of MgADP in skinned skeletal muscle fibers. J. Gen. Physiol. 101:867-888.
    • (1993) J. Gen. Physiol. , vol.101 , pp. 867-888
    • Lu, Z.1    Moss, R.L.2    Walker, J.W.3
  • 19
    • 0023664578 scopus 로고
    • Changes in the ATPase activity of insect fibrillar flight muscle during calcium and strain activation probed by phosphate-water oxygen exchange
    • Lund, J , M. R. Webb, and D. S. C. White. 1987. Changes in the ATPase activity of insect fibrillar flight muscle during calcium and strain activation probed by phosphate-water oxygen exchange. J. Biol. Chem. 362:8584-8590.
    • (1987) J. Biol. Chem. , vol.362 , pp. 8584-8590
    • Lund, J.1    Webb, M.R.2    White, D.S.C.3
  • 20
    • 85030197692 scopus 로고
    • A model of stress relaxation in cross-bridge systems: Effect of a series elastic element
    • Luo, Y., R. Cooke, and E. Pate. 1993. A model of stress relaxation in cross-bridge systems: effect of a series elastic element. Am. J. Physiol. 267:C1598-C1606.
    • (1993) Am. J. Physiol. , vol.267
    • Luo, Y.1    Cooke, R.2    Pate, E.3
  • 21
    • 0028294216 scopus 로고
    • Relaxation from rigor of skinned trabeculae of the guinea pig by laser flash photolysis of caged ATP
    • Martin, H., and R. J. Barsotti 1994. Relaxation from rigor of skinned trabeculae of the guinea pig by laser flash photolysis of caged ATP. Biophys. J. 66:1115-1128.
    • (1994) Biophys. J. , vol.66 , pp. 1115-1128
    • Martin, H.1    Barsotti, R.J.2
  • 22
    • 0024417752 scopus 로고
    • Cross-bridge movement in rat cardiac muscle as a function of calcium concentration
    • Matsubara, I., D. W. Maughan, Y. Saeki, and N. Yagi. 1989. Cross-bridge movement in rat cardiac muscle as a function of calcium concentration. J. Physiol (Lond.). 417:555-565.
    • (1989) J. Physiol (Lond.) , vol.417 , pp. 555-565
    • Matsubara, I.1    Maughan, D.W.2    Saeki, Y.3    Yagi, N.4
  • 23
    • 0024312136 scopus 로고
    • Variation in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • Metzger, J. M., M. L. Greaser, and R. L. Moss. 1989. Variation in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. J. Gen. Physiol 98:855-883.
    • (1989) J. Gen. Physiol , vol.98 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 24
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycennated rabbit skeletal muscle fibers
    • Millar, N. C., and E. Homsher. 1990. The effect of phosphate and calcium on force generation in glycennated rabbit skeletal muscle fibers. J. Biol. Chem. 265:20234-20240.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 25
    • 0026735649 scopus 로고
    • Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers
    • Millar, N. C., and E. Homsher. 1992. Kinetics of force generation and phosphate release in skinned rabbit soleus muscle fibers. Am. J. Physiol. 262:C1239-C1245.
    • (1992) Am. J. Physiol. , vol.262
    • Millar, N.C.1    Homsher, E.2
  • 26
    • 0022931542 scopus 로고
    • 2- dependence of tension development in skinned skeletal muscle fibers following modification of troponin by partial substitution with cardiac troponin C
    • 2- dependence of tension development in skinned skeletal muscle fibers following modification of troponin by partial substitution with cardiac troponin C. J. Biol. Chem. 261:6096-6099.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6096-6099
    • Moss, R.L.1    Lauer, M.R.2    Giullian, G.G.3    Greaser, M.L.4
  • 27
    • 0028170185 scopus 로고
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibers
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibers. J. Physiol. 480:45-60.
    • (1994) J. Physiol. , vol.480 , pp. 45-60
    • Palmer, S.1    Kentish, J.C.2
  • 28
    • 0024392532 scopus 로고
    • Addition of phosphate to active muscle probes actomyosin states within the power stroke
    • Pate, E. and R. Cooke. 1989. Addition of phosphate to active muscle probes actomyosin states within the power stroke. Pflugers Arch. 414:73-81.
    • (1989) Pflugers Arch. , vol.414 , pp. 73-81
    • Pate, E.1    Cooke, R.2
  • 30
    • 0028053976 scopus 로고
    • Kinetics of relaxation from rigor of permeabilized fast-twitch skeletal fibers from the rabbit using a novel caged ATP and apyrase
    • Thirlwell, H., J. E. T. Corrie, G. P. Reid, D. R. Trentham, and M. A. Ferenczi. 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.
    • (1994) Biophys. J. , vol.67 , pp. 2436-2447
    • Thirlwell, H.1    Corrie, J.E.T.2    Reid, G.P.3    Trentham, D.R.4    Ferenczi, M.A.5
  • 31
    • 0026609631 scopus 로고
    • 2+ on the kinetics of phosphate release in skeletal muscle
    • 2+ on the kinetics of phosphate release in skeletal muscle. J. Biol. Chem. 267:2459-2466.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2459-2466
    • Walker, J.W.1    Lu, Z.2    Moss, R.L.3
  • 33
    • 0017044811 scopus 로고
    • Energetics and mechanism of actomyosin adenosine triphosphatase
    • White, H. D., and E. Taylor. 1976. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry. 15:5818-5826.
    • (1976) Biochemistry , vol.15 , pp. 5818-5826
    • White, H.D.1    Taylor, E.2
  • 34
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff, M., K. MacDonald, and R. L. Moss. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154-160.
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.1    MacDonald, K.2    Moss, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.