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Volumn 70, Issue 5, 1996, Pages 2333-2340

Myosin regulatory light chain modulates the Ca2+ dependence of the kinetics of tension development in skeletal muscle fibers

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN LIGHT CHAIN; TROPONIN C;

EID: 0030002797     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79799-0     Document Type: Article
Times cited : (42)

References (30)
  • 3
    • 0017666938 scopus 로고
    • The significance of the slow dissociation of divalent metal ions from myosin "regulatory" light chains
    • Bagshaw, C. R., and G. H. Reed. 1977. The significance of the slow dissociation of divalent metal ions from myosin "regulatory" light chains. FEBS Lett. 81:386-390
    • (1977) FEBS Lett. , vol.81 , pp. 386-390
    • Bagshaw, C.R.1    Reed, G.H.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
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 7
    • 0028913990 scopus 로고
    • Effects of a non-divalent cation binding mutant of myosin regulatory light chain on tension generation in skinned skeletal muscle fibers
    • Diffee, G. M., M. L. Greaser, F. Reinach, and R. L. Moss. 1995. Effects of a non-divalent cation binding mutant of myosin regulatory light chain on tension generation in skinned skeletal muscle fibers. Biophys. J. 68: 1443-1452.
    • (1995) Biophys. J. , vol.68 , pp. 1443-1452
    • Diffee, G.M.1    Greaser, M.L.2    Reinach, F.3    Moss, R.L.4
  • 8
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free and free from specified total ionic concentrations in aqueous solutions containing multiple metals or ligands
    • Fabiato, A. 1988. Computer programs for calculating total from specified free and free from specified total ionic concentrations in aqueous solutions containing multiple metals or ligands. Methods Enzymol. 157: 378-417.
    • (1988) Methods Enzymol. , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 9
    • 0019974315 scopus 로고
    • Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog
    • Godt, R. E., and B. D. Lindley. 1982. Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J. Gen. Physiol. 80:279-297.
    • (1982) J. Gen. Physiol. , vol.80 , pp. 279-297
    • Godt, R.E.1    Lindley, B.D.2
  • 10
    • 0025130921 scopus 로고
    • Regulation of scallop myosin by mutant regulatory light chains
    • Goodwin, E. B., L. A. Leinwand, and A. G. Szent-Gyorgi. 1990. Regulation of scallop myosin by mutant regulatory light chains. J. Mol. Biol. 216:85-93.
    • (1990) J. Mol. Biol. , vol.216 , pp. 85-93
    • Goodwin, E.B.1    Leinwand, L.A.2    Szent-Gyorgi, A.G.3
  • 11
    • 0015218120 scopus 로고
    • Reconstitution of troponia activity from three protein components
    • Greaser, M. L., and J. Gergely. 1971. Reconstitution of troponia activity from three protein components. J. Biol. Chem. 246:4226-4233.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 12
    • 0025268166 scopus 로고
    • 2+ sensitivities of isometric tension, stiffness, and velocity of shortening in skinned skeletal muscle fibers
    • 2+ sensitivities of isometric tension, stiffness, and velocity of shortening in skinned skeletal muscle fibers. J. Gen. Physiol. 95:477-498.
    • (1990) J. Gen. Physiol. , vol.95 , pp. 477-498
    • Hofmann, P.A.1    Metzger, J.M.2    Greaser, M.L.3    Moss, R.L.4
  • 13
    • 0018625835 scopus 로고
    • The calcium binding properties of phosphorylated and unphosphorylated cardiac and skeletal myosins
    • Holroyde, M. J., J. D. Potter, and R. J. Solaro. 1979. The calcium binding properties of phosphorylated and unphosphorylated cardiac and skeletal myosins. J. Biol. Chem. 254:6478-6482.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6478-6482
    • Holroyde, M.J.1    Potter, J.D.2    Solaro, R.J.3
  • 14
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm, K. E., and J. T. Stull. 1985. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25.593-620.
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 15
    • 0024075828 scopus 로고
    • Photolabile chelators for the rapid photorelease of divalent cations
    • Kaplan, J. H., and G. C. R. Ellis-Davies. 1988. Photolabile chelators for the rapid photorelease of divalent cations. Proc. Natl. Acad. Sci. USA. 85:6571-6575
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6571-6575
    • Kaplan, J.H.1    Ellis-Davies, G.C.R.2
  • 18
    • 0015221317 scopus 로고
    • Light chains from fast and slow myosins
    • Lowey, S., and D. Risby. 1971. Light chains from fast and slow myosins. Nature. 234:81-85.
    • (1971) Nature , vol.234 , pp. 81-85
    • Lowey, S.1    Risby, D.2
  • 19
    • 0027426228 scopus 로고
    • Skeletal muscle light chains are essential for physiological speeds of shortening
    • Lowey, S., G. S. Waller, and K. M. Trybus. 1993. Skeletal muscle light chains are essential for physiological speeds of shortening. Nature. 365:454-456.
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 20
    • 0025824168 scopus 로고
    • 2+ sensitive cross-bridge state transition in skeletal muscle fibers: Effects due to variations in thin filament activation by extraction of troponin C
    • 2+ sensitive cross-bridge state transition in skeletal muscle fibers: effects due to variations in thin filament activation by extraction of troponin C. J. Gen. Physiol. 98:233-248.
    • (1991) J. Gen. Physiol. , vol.98 , pp. 233-248
    • Metzger, J.M.1    Moss, R.L.2
  • 21
    • 0026646783 scopus 로고
    • Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle
    • Metzger, J. M., and R. L. Moss. 1992. Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys. J. 63:460-468.
    • (1992) Biophys. J. , vol.63 , pp. 460-468
    • Metzger, J.M.1    Moss, R.L.2
  • 23
    • 0020615741 scopus 로고
    • Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian single skeletal muscle fibers
    • Moss, R. L., G. G. Giulian, and M. L. Greaser. 1983. Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian single skeletal muscle fibers. J. Cell Biol. 96: 970-978.
    • (1983) J. Cell Biol. , vol.96 , pp. 970-978
    • Moss, R.L.1    Giulian, G.G.2    Greaser, M.L.3
  • 25
    • 0017869701 scopus 로고
    • Reversible loss of calcium control of tension in scallop striated muscle associated with the removal of regulatory light chain
    • Simmons, R. M., and A. G. Szeni-Gyorgi. 1978. Reversible loss of calcium control of tension in scallop striated muscle associated with the removal of regulatory light chain. Nature. 273:62-64.
    • (1978) Nature , vol.273 , pp. 62-64
    • Simmons, R.M.1    Szeni-Gyorgi, A.G.2
  • 26
    • 0026774946 scopus 로고
    • Influence of a strong-binding myosin analogue on calcium-sensitive properties of skinned skeletal muscle fibers
    • Swartz, D. R., and R. L. Moss. 1992. Influence of a strong-binding myosin analogue on calcium-sensitive properties of skinned skeletal muscle fibers. J. Biol. Chem. 267:20497-20506.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20497-20506
    • Swartz, D.R.1    Moss, R.L.2
  • 28
    • 0020020860 scopus 로고
    • Preparation and fractionation of myosin light chains and exchange of the essential light chain
    • Wagner, P. D. 1982. Preparation and fractionation of myosin light chains and exchange of the essential light chain. Methods Enzymol. 85:72-81.
    • (1982) Methods Enzymol. , vol.85 , pp. 72-81
    • Wagner, P.D.1
  • 29
    • 0015223540 scopus 로고
    • Substructure of the myosin molecule. II. The light chains of myosin
    • Weeds, A. G., and S. Lowey. 1971. Substructure of the myosin molecule. II. The light chains of myosin. J. Mol. Biol. 61:701-725.
    • (1971) J. Mol. Biol. , vol.61 , pp. 701-725
    • Weeds, A.G.1    Lowey, S.2
  • 30
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with the level of activator calcium
    • Wolff, M. W., K. S. McDonald, R. L. Moss. 1995. Rate of tension development in cardiac muscle varies with the level of activator calcium. Circ. Res. 76:154-160.
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.W.1    McDonald, K.S.2    Moss, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.