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Driving Filament Sliding: Weak binding cross-bridge states, strong binding cross-bridge states, and the power stroke

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Book cover Sliding Filament Mechanism in Muscle Contraction

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 565))

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References

  • Bagshaw CR, Eccleston JF, Trentham DR, and Yates DW. Transient kinetic studies of the Mg++-dependent ATPase of myosin and its proteolytic fragments. Cold Spring Harb Symp Quant Biol 37: 127–135, 1973.

    CAS  Google Scholar 

  • Brenner B, Schoenberg M, Chalovich JM, Greene LC, and Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc Natl Acad Sci USA 79: 7288–7291, 1982.

    Article  PubMed  CAS  Google Scholar 

  • Brenner B, Yu LC, and Podolsky R.J. X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys J 46: 299–306, 1984.

    PubMed  CAS  Google Scholar 

  • Brenner B, and Yu LC. Equatorial X-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing. Biophys J 48:829–834, 1985.

    PubMed  CAS  Google Scholar 

  • Brenner B, Chalovich JM, Greene LC, Eisenberg E, and Schoenberg M. Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solutions. Biophys J 50: 685–691, 1986.

    PubMed  CAS  Google Scholar 

  • Brenner B, Yu LC, Greene LC, Eisenberg E, and Schoenberg M. Ca2+-sensitive cross-bridge dissociation in the presence of MgPPi in skinned rabbit psoas fibers. Biophys J 50: 1101–1108, 1986(b).

    PubMed  CAS  Google Scholar 

  • Brenner B. Muscle mechanics and biochemical kinetics, in: Molecular Mechanism of Muscular Contraction, John Squire, ed, Macmillan Press Ltd., London, pp. 77–149, 1990.

    Google Scholar 

  • Brenner B, Yu LC, and Chalovich JM. Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon. Implications for the pathway to force generation. Proc Natl Acad Sci USA 88: 5739–5743, 1991.

    Article  PubMed  CAS  Google Scholar 

  • Brenner B, Chalovich JM, and Yu LC. Distinct molecular processes associated with isometric force generation and with rapid tension recovery after quick release. Biophys J 68:106s–111s, 1995.

    PubMed  CAS  Google Scholar 

  • Brenner B, Kraft T, and Chalovich JM. Fluorescence of NBD-labeled troponin-I as a probe for the kinetics of thin filament activation. Adv Exp Med Mol Biol 453:177–185, 1998.

    CAS  Google Scholar 

  • Brenner B, and Chalovich JM. Kinetics of thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-l,3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Implications for regulation of muscle contraction. Biophys J 77:2692–2708, 1999.

    PubMed  CAS  Google Scholar 

  • Brenner B, Kraft T, Yu LC, and Chalovich JM. Thin filament activation probed by fluorescence of N-((2-Iodoacetoxy)ethyi)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labelled troponin I incorporated in skinned fibers of rabbit psoas muscle. Biophys J 77:2677–2691, 1999.

    PubMed  CAS  Google Scholar 

  • Chase PB, Martyn DA, Kushmerick MJ, and Gordon AM. Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit. J Physiol Lond 460:231–46, 1993.

    PubMed  CAS  Google Scholar 

  • Dantzig JA, Goldman YE, Millar NC, Lacktis J, and Homsher E. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol Lond 451:247–278, 1992.

    PubMed  CAS  Google Scholar 

  • Frisbie SM, Chalovich JM, Brenner B, and Yu LC Modulation of cross-bridge affinity for MgGTP by Ca++ in skinned fibers of rabbit psoas muscle. Biophys J 72:2255–2261, 1997.

    PubMed  CAS  Google Scholar 

  • Geeves MA, Goody RS, and Gutfreund H. Kinetics of acto.Sl interaction. J Muscle Res Cell Motil 5:351–361, 1984.

    Article  PubMed  CAS  Google Scholar 

  • Geeves MA, and Conibear PB. The role of three state docking of myosin S1 with actin in force generation. Biophys J 68:l94s–201s, 1995.

    Google Scholar 

  • Goody RS, and Hofmann F. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides J Muscle Res Cell Motil 1:101–115, 1980.

    Article  PubMed  CAS  Google Scholar 

  • Greene LE, and Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci USA: 77:2616–2620, 1980.

    Article  PubMed  CAS  Google Scholar 

  • Greene LE, Sellers JR, Eisenberg E, and Adelstein RS. Binding of gizzard smooth muscle myosin subfragment-one to actin in the presence and absence of ATP. Biochemistry 22:530–535, 1983.

    Article  PubMed  CAS  Google Scholar 

  • Gu J, Xu S, and Yu LC. A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle. Biophys J 82:2123–33, 2002.

    PubMed  CAS  Google Scholar 

  • Head JG, Ritchie MD, and Geeves MA. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur J Biochem 227:694–699, 1995.

    Article  PubMed  CAS  Google Scholar 

  • Holmes KC. The actomyosin interaction and its control by tropomyosin. Biophys J 68:2s–5s, 1995.

    PubMed  CAS  Google Scholar 

  • Kraft T, Yu LC, Kuhn HJ, and Brenner B. Effect of Ca++ on weak cross-bridge interaction with actin in the presence of the nucleotide analog ATPyS. Proc Natl Acad Sci USA 89: 11362–11366, 1992.

    Article  PubMed  CAS  Google Scholar 

  • Kraft T, Chalovich JM, Yu LC, and Brenner B. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys J 68:2404–2418, 1995.

    PubMed  CAS  Google Scholar 

  • Kraft T, Xu S, Brenner B, and Yu LC. The effect of thin filament activation on the attachment of weak binding cross-bridges: A 2D-Xray-diffraction study on single muscle fibers. Biophys J 76:1494–1513, 1999.

    PubMed  CAS  Google Scholar 

  • Kraft T, Mattel T, Radocaj A, Piep B, Nocula Ch, Furch M, and Brenner B. Structural features of cross-bridges in isometrically contracting skeletal muscle Biophys J 82:2536–2547, 2002.

    PubMed  CAS  Google Scholar 

  • Kraft T, Mählmann E, Mattei T, and Brenner B. Effects of myosin binding to actin on structural and functional properties of the myosin head domain. Biophys J 86:266a, 2004

    Google Scholar 

  • Lehman W, Craig R, and Vibert P. Ca2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368:65–67, 1994.

    Article  PubMed  CAS  Google Scholar 

  • Lehman W, Vibert P, Uman P, and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J Mol Biol 251:191–196, 1995.

    Article  PubMed  CAS  Google Scholar 

  • Mattel T, Mählmann E, Piep B, Kraft T, and Brenner B. MgADP.AlF4-binding to cross-bridges under rigor conditions: mechanical and structural properties of the resulting cross-bridge state. Biophys J 86:266a, 2004.

    Google Scholar 

  • McKillop DFA, and Geeves MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65:693–701, 1993.

    PubMed  CAS  Google Scholar 

  • Millar NC, and Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. A steady state and transient kinetic study. J Biol Chem 265:20234–20240, 1990.

    PubMed  CAS  Google Scholar 

  • Schoenberg M. Equilibrium muscle cross-bridge behavior. Theoretical considerations. Biophys J 48:467–475, 1985.

    Article  PubMed  CAS  Google Scholar 

  • Stein LA, Schwartz RP, Chock PB, and Eisenberg E. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5′-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry 18, 3895–3909, 1979.

    Article  PubMed  CAS  Google Scholar 

  • Stein LE, Chock PB, and Eisenberg E. The rate-limiting step in the actomyosin adenosintriphosphatase cycle. Biochemistry 23:1555–1563, 1984.

    Article  PubMed  CAS  Google Scholar 

  • White HD, and Taylor EW. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15:5818–5826, 1976.

    Article  PubMed  CAS  Google Scholar 

  • Xu S, Malinchik S, Gllroy D, Kraft T, Brenner B, and Yu LC. X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys J 72:2292–2303, 1997.

    Google Scholar 

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Author information

Authors and Affiliations

  1. Dept. Molecular and Cell Physiology, Medical School Hannover, D-30625, Hannover, Germany

    Bernhard Brenner, Enke Mählmann, Thomas Mattei & Theresia Kraft

Authors
  1. Bernhard Brenner
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  2. Enke Mählmann
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  3. Thomas Mattei
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  4. Theresia Kraft
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Editor information

Editors and Affiliations

  1. Teiko University, Tokyo, Japan

    Haruo Sugi

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© 2005 Springer Science+Business Media, Inc.

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Brenner, B., Mählmann, E., Mattei, T., Kraft, T. (2005). Driving Filament Sliding: Weak binding cross-bridge states, strong binding cross-bridge states, and the power stroke. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_7

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  • DOI: https://doi.org/10.1007/0-387-24990-7_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-387-24989-6

  • Online ISBN: 978-0-387-24990-2

  • eBook Packages: MedicineMedicine (R0)

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