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Volumn 30, Issue 9, 2011, Pages 653-659

Interaction between troponin and myosin enhances contractile activity of myosin in cardiac muscle

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; F ACTIN; MYOSIN; MYOSIN HEAVY CHAIN; TROPONIN;

EID: 80053555254     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2010.1163     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 0028555863 scopus 로고
    • Development of stiffness precedes cross-bridge attachment during the early tension rise in single frog muscle fibres
    • Bagni, M.A., Cecchi, G., et al. (1994). Development of stiffness precedes cross-bridge attachment during the early tension rise in single frog muscle fibres. J Physiol 481 (Pt 2), 273-278.
    • (1994) J Physiol , vol.481 , Issue.PART 2 , pp. 273-278
    • Bagni, M.A.1    Cecchi, G.2
  • 2
    • 0030721473 scopus 로고    scopus 로고
    • Troponin i and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility
    • Bing, W., Fraser, I.D., et al. (1997). Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility. Biochem J 327 (Pt 2), 335-340.
    • (1997) Biochem J , vol.327 , Issue.PART 2 , pp. 335-340
    • Bing, W.1    Fraser, I.D.2
  • 3
    • 33646203967 scopus 로고    scopus 로고
    • Dynamics of the C- terminal region of Tnl in the troponin complex in solution
    • Blumenschein, T.M., Stone, D.B., et al. (2006). Dynamics of the C- terminal region of Tnl in the troponin complex in solution. Biophys J 90, 2436-2444.
    • (2006) Biophys J , vol.90 , pp. 2436-2444
    • Blumenschein, T.M.1    Stone, D.B.2
  • 4
    • 67349094896 scopus 로고    scopus 로고
    • Modulation of the effects of tropomyosin on actin and myosin conforma- tional changes by troponin and Ca2+
    • Borovikov, Y.S., Karpicheva, O.E., et al. (2009). Modulation of the effects of tropomyosin on actin and myosin conforma- tional changes by troponin and Ca2+. Biochim Biophys Acta 1794, 985-994.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 985-994
    • Borovikov, Y.S.1    Karpicheva, O.E.2
  • 8
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg, E., and Greene, L.E. (1980). The relation of muscle biochemistry to muscle physiology. Annu Rev Physio 42, 293-309.
    • (1980) Annu Rev Physio , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 10
    • 0036156643 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins
    • Fujita, H., Sasaki, D., et al. (2002). Elementary steps of the cross- bridge cycle in bovine myocardium with and without regulatory proteins. Biophys J 82, 915-928. (Pubitemid 34111232)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 915-928
    • Fujita, H.1    Sasaki, D.2    Ishiwata, S.3    Kawai, M.4
  • 11
    • 4544291412 scopus 로고    scopus 로고
    • Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene
    • DOI 10.1023/B:MCBI.0000041852.42291.aa
    • Gomes, A.V., and Potter, J.D. (2004). Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene. Mol Cell Biochem 263, 99-114. (Pubitemid 39256149)
    • (2004) Molecular and Cellular Biochemistry , vol.263 , Issue.1 , pp. 99-114
    • Gomes, A.V.1    Potter, J.D.2
  • 12
    • 0032437487 scopus 로고    scopus 로고
    • Skeletal muscle regulatory proteins enhance F-actin in vitro motility
    • discussion 196-197
    • Gordon, A.M., Chen, Y., et al. (1998). Skeletal muscle regulatory proteins enhance F-actin in vitro motility. Adv Exp Med Biol 453, 187-196; discussion 196-197.
    • (1998) Adv Exp Med Biol , vol.453 , pp. 187-196
    • Gordon, A.M.1    Chen, Y.2
  • 13
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A.M., Homsher, E., et al. (2000). Regulation of contraction in striated muscle. Physiol Rev 80, 853-924. (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 14
    • 0031055303 scopus 로고    scopus 로고
    • Calcium regulation of skeletal muscle thin filament motility in vitro
    • Gordon, A.M., LaMadrid, M.A., et al. (1997). Calcium regulation of skeletal muscle thin filament motility in vitro. Biophys J 72, 1295-1307. (Pubitemid 27113652)
    • (1997) Biophysical Journal , vol.72 , Issue.3 , pp. 1295-1307
    • Gordon, A.M.1    LaMadrid, M.A.2    Chen, Y.3    Luo, Z.4    Chase, P.B.5
  • 15
    • 0017917498 scopus 로고
    • Skeletal muscle energetics and metabolism
    • Homsher, E., and Kean, C.J. (1978). Skeletal muscle energetics and metabolism. Annu Rev Physiol 40, 93-131.
    • (1978) Annu Rev Physiol , vol.40 , pp. 93-131
    • Homsher, E.1    Kean, C.J.2
  • 16
    • 0029924132 scopus 로고    scopus 로고
    • Calcium regulation of thin filament movement in an in vitro motility assay
    • Homsher, E., Kim, B., et al. (1996). Calcium regulation of thin filament movement in an in vitro motility assay. Biophys J 70, 1881-1892. (Pubitemid 26103961)
    • (1996) Biophysical Journal , vol.70 , Issue.4 , pp. 1881-1892
    • Homsher, E.1    Kim, B.2    Bobkova, A.3    Tobacman, L.S.4
  • 17
    • 0034177712 scopus 로고    scopus 로고
    • Regulation of force and unloaded sliding speed in single thin filaments: Effects of regulatory proteins and calcium
    • Homsher, E., Lee, D.M., et al. (2000). Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calcium. J Physiol 524 Pt 1, 233-243. (Pubitemid 30195317)
    • (2000) Journal of Physiology , vol.524 , Issue.1 , pp. 233-243
    • Homsher, E.1    Lee, D.M.2    Morris, C.3    Pavlov, D.4    Tobacman, L.S.5
  • 18
    • 0020653743 scopus 로고
    • Time-resolved X-ray diffraction studies on vertebrate striated muscle
    • Huxley, H.E., and Faruqi, A.R. (1983). Time-resolved X-ray diffraction studies on vertebrate striated muscle. Annu Rev Bio- phys Bioeng 12, 381-417.
    • (1983) Annu Rev Bio- Phys Bioeng , vol.12 , pp. 381-417
    • Huxley, H.E.1    Faruqi, A.R.2
  • 20
    • 0142024741 scopus 로고    scopus 로고
    • Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C
    • DOI 10.1161/01.RES.0000096363.85588.9A
    • Korte, F.S., McDonald, K.S., et al. (2003). Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C. Circ Res 93, 752-758. (Pubitemid 37288670)
    • (2003) Circulation Research , vol.93 , Issue.8 , pp. 752-758
    • Korte, F.S.1    McDonald, K.S.2    Harris, S.P.3    Moss, R.L.4
  • 21
    • 0025782977 scopus 로고
    • Assays for actin sliding movement over myosin-coated surfaces
    • Kron, S.J., Toyoshima, Y.Y., et al. (1991). Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol 196, 399-16.
    • (1991) Methods Enzymol , vol.196 , pp. 399-16
    • Kron, S.J.1    Toyoshima, Y.Y.2
  • 22
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • DOI 10.1006/jmbi.1998.1654
    • Lehrer, S.S., and Geeves, M.A. (1998). The muscle thin filament as a classical cooperative/allosteric regulatory system. J Mol Biol 277, 1081-1089. (Pubitemid 28190848)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 23
    • 0020490904 scopus 로고
    • Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
    • Lehrer, S.S., and Morris, E.P. (1982). Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase. J Biol Chem 257, 8073-8080.
    • (1982) J Biol Chem , vol.257 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 25
    • 4344700649 scopus 로고    scopus 로고
    • All-electrical switching and control mechanism for actomyosin-powered nanoactua-tors
    • Mihajlovic, G., Brunet, N.M., et al. (2004). All-electrical switching and control mechanism for actomyosin-powered nanoactua-tors. Appl Phys Lett 85, 1060-1062.
    • (2004) Appl Phys Lett , vol.85 , pp. 1060-1062
    • Mihajlovic, G.1    Brunet, N.M.2
  • 26
    • 23944457539 scopus 로고    scopus 로고
    • 2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin
    • DOI 10.1016/j.jmb.2005.06.067, PII S0022283605007527
    • Murakami, K., Yumoto, F., et al. (2005). Structural basis for Ca2+- regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. J Mol Biol 352, 178-201. (Pubitemid 41207448)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.1 , pp. 178-201
    • Murakami, K.1    Yumoto, F.2    Ohki, S.-Y.3    Yasunaga, T.4    Tanokura, M.5    Wakabayashi, T.6
  • 27
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J.D., and Spudich, J.A. (1982). Purification of muscle actin. Methods Enzymol 85 Pt B, 164-181.
    • (1982) Methods Enzymol , vol.85 , Issue.PART B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 28
    • 33644941942 scopus 로고    scopus 로고
    • An atomic model of the thin filament in the relaxed and Ca2+-activated states
    • Pirani, A., Vinogradova, M.V., et al. (2006). An atomic model of the thin filament in the relaxed and Ca2+-activated states. J Mol Biol 357, 707-717.
    • (2006) J Mol Biol , vol.357 , pp. 707-717
    • Pirani, A.1    Vinogradova, M.V.2
  • 29
    • 0016213363 scopus 로고
    • Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction
    • Potter, J.D., and Gergely, J. (1974). Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction. Biochemistry 13, 2697-2703.
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 30
    • 0028858949 scopus 로고
    • A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction
    • Potter, J.D., Sheng, Z., et al. (1995). A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction. J Biol Chem 270, 2557-2562.
    • (1995) J Biol Chem , vol.270 , pp. 2557-2562
    • Potter, J.D.1    Sheng, Z.2
  • 31
    • 1242320058 scopus 로고    scopus 로고
    • At the crossroads of myo- cardial signaling: The role of Z-discs in intracellular signaling and cardiac function
    • DOI 10.1161/01.RES.0000116143.74830.A9
    • Pyle, W.G., and Solaro, R.J. (2004). At the crossroads of myo- cardial signaling: the role of Z-discs in intracellular signaling and cardiac function. Circ Res 94, 296-305. (Pubitemid 38240720)
    • (2004) Circulation Research , vol.94 , Issue.3 , pp. 296-305
    • Pyle, W.G.1    Solaro, R.J.2
  • 34
    • 33748452105 scopus 로고    scopus 로고
    • Positive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscle
    • DOI 10.1529/biophysj.105.079061
    • Schoffstall, B., Clark, A., et al. (2006b). Positive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscle. Biophys J 91, 2216-2226. (Pubitemid 44352404)
    • (2006) Biophysical Journal , vol.91 , Issue.6 , pp. 2216-2226
    • Schoffstall, B.1    Clark, A.2    Chase, P.B.3
  • 36
    • 31744435681 scopus 로고    scopus 로고
    • Activation dependence of stretch activation in mouse skinned myocardium: Implications for ventricular function
    • DOI 10.1085/jgp.200509432
    • Stelzer, J. E., Larsson, L., et al. (2006). Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular function. J Gen Physiol 127, 95-107. (Pubitemid 43177133)
    • (2006) Journal of General Physiology , vol.127 , Issue.2 , pp. 95-107
    • Stelzer, J.E.1    Larsson, L.2    Fitzsimons, D.P.3    Moss, R.L.4
  • 37
    • 34548356872 scopus 로고    scopus 로고
    • Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphorylation
    • DOI 10.1161/CIRCRESAHA.107.153650
    • Stelzer, J.E., Patel, J.R., et al. (2007). Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase A phosphory- lation. Circ Res 101, 503-511. (Pubitemid 47347881)
    • (2007) Circulation Research , vol.101 , Issue.5 , pp. 503-511
    • Stelzer, J.E.1    Patel, J.R.2    Walker, J.W.3    Moss, R.L.4
  • 38
    • 0034614419 scopus 로고    scopus 로고
    • Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy
    • Szczesna, D., Zhang, R., et al. (2000). Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy. J Biol Chem 275, 624630.
    • (2000) J Biol Chem , vol.275 , pp. 624630
    • Szczesna, D.1    Zhang, R.2
  • 39
    • 0018368483 scopus 로고
    • Mechanism of actomyosin ATPase and the problem of muscle contraction
    • Taylor, E.W. (1979). Mechanism of actomyosin ATPase and the problem of muscle contraction. CRC Crit Rev Biochem 6, 103164.
    • (1979) CRC Crit Rev Biochem , vol.6 , pp. 103164
    • Taylor, E.W.1
  • 40
    • 0017113027 scopus 로고
    • Kinetic analysis of ATPase mechanisms
    • Trentham, D.R., Eccleston, J.F., et al. (1976). Kinetic analysis of ATPase mechanisms. Q Rev Biophys 9, 217-281.
    • (1976) Q Rev Biophys , vol.9 , pp. 217-281
    • Trentham, D.R.1    Eccleston, J.F.2
  • 42
    • 0030935378 scopus 로고    scopus 로고
    • 2+ sensitivity of the acto-S1-TM ATPase activity of the thin filament
    • 2+ sensitivity of the acto-S1-TM ATPase activity of the thin filament. J Biol Chem 272, 10529-10537.
    • (1997) J Biol Chem , vol.272 , pp. 10529-10537
    • Van Eyk, J.E.1    Thomas, L.T.2
  • 43
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White, H.D. (1982). Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol 85 Pt B, 698-708.
    • (1982) Methods Enzymol , vol.85 PART B , pp. 698-708
    • White, H.D.1
  • 44
    • 70350238351 scopus 로고    scopus 로고
    • Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle
    • Wu, S., Liu, J., et al. (2009). Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle. J Struct Biol 168, 485502.
    • (2009) J Struct Biol , vol.168 , pp. 485502
    • Wu, S.1    Liu, J.2


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