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. 1986 Nov;50(5):875–884. doi: 10.1016/S0006-3495(86)83528-7

The effect of cross-bridge clustering and head-head competition on the mechanical response of skeletal muscle under equilibrium conditions.

A Tözeren, M Schoenberg
PMCID: PMC1329812  PMID: 3790690

Abstract

The effect of cross-bridge clustering and head-head competition on the mechanical response of skeletal muscle under equilibrium conditions is considered. For this purpose, the recent multiple site equilibrium cross-bridge model of Schoenberg (Schoenberg, M., 1985, Biophys. J., 48:467-475) is extended in accordance with the formalism of T.L. Hill (1974, Prog. Biophys, Mol. Biol., 28:267-340) to consider the case where groups of independent cross-bridge heads compete with each other for binding to multiple actin sites. Cooperative behavior between heads is not allowed. Computations indicate that for the double-headed cross-bridge with two independent equivalent heads, the time course of force decay after a stretch is similar to that for the single-headed cross-bridge; that is, the rate constant for force decay is approximately equal to the cross-bridge head detachment rate constant. The results also show that the force decay after a stretch becomes slower than the detachment rate constant of a single head when cross-bridge heads bind adjacently in clusters so that competition between heads for binding to the available actin sites increases. However, if one assumes that the detachment rate constant of an unstrained head in a fiber is comparable to that of an S1 molecule in solution, this effect is not large enough to explain why some of the rate constants for force decay after a stretch in rigor, or in the presence of ATP analogues such as adenyl-5'-yl imidodiphosphate, appear to be significantly slower than the detachment rate constant of S1 from actin in solution.

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Selected References

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  1. Brenner B., Chalovich J. M., Greene L. E., Eisenberg E., Schoenberg M. Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solution. Biophys J. 1986 Oct;50(4):685–691. doi: 10.1016/S0006-3495(86)83509-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brenner B., Schoenberg M., Chalovich J. M., Greene L. E., Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7288–7291. doi: 10.1073/pnas.79.23.7288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. HUXLEY A. F. Muscle structure and theories of contraction. Prog Biophys Biophys Chem. 1957;7:255–318. [PubMed] [Google Scholar]
  4. Haselgrove J. C., Reedy M. K. Modeling rigor cross-bridge patterns in muscle I. Initial studies of the rigor lattice of insect flight muscle. Biophys J. 1978 Dec;24(3):713–728. doi: 10.1016/S0006-3495(78)85415-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hill T. L. Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. Prog Biophys Mol Biol. 1974;28:267–340. doi: 10.1016/0079-6107(74)90020-0. [DOI] [PubMed] [Google Scholar]
  6. Hill T. L. Theoretical formalism for the sliding filament model of contraction of striated muscle. Part II. Prog Biophys Mol Biol. 1975;29(2):105–159. doi: 10.1016/0079-6107(76)90021-3. [DOI] [PubMed] [Google Scholar]
  7. Konrad M., Goody R. S. Kinetic and thermodynamic properties of the ternary complex between F-actin, myosin subfragment 1 and adenosine 5'-[beta, gamma-imido]triphosphate. Eur J Biochem. 1982 Nov 15;128(2-3):547–555. doi: 10.1111/j.1432-1033.1982.tb07000.x. [DOI] [PubMed] [Google Scholar]
  8. Kuhn H. J. Cross bridge slippage induced by the ATP analogue AMP-PNP and stretch in glycerol-extracted fibrillar muscle fibres. Biophys Struct Mech. 1978 Apr 13;4(2):159–168. doi: 10.1007/BF00539229. [DOI] [PubMed] [Google Scholar]
  9. Lymn R. W., Taylor E. W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 1971 Dec 7;10(25):4617–4624. doi: 10.1021/bi00801a004. [DOI] [PubMed] [Google Scholar]
  10. Marston S. B. The rates of formation and dissociation of actin-myosin complexes. Effects of solvent, temperature, nucleotide binding and head-head interactions. Biochem J. 1982 May 1;203(2):453–460. doi: 10.1042/bj2030453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pate E. F., Brokaw C. J. Cross-bridge behavior in rigor muscle. Biophys Struct Mech. 1980;7(1):51–63. doi: 10.1007/BF00538158. [DOI] [PubMed] [Google Scholar]
  12. Schoenberg M., Brenner B., Chalovich J. M., Greene L. E., Eisenberg E. Cross-bridge attachment in relaxed muscle. Adv Exp Med Biol. 1984;170:269–284. doi: 10.1007/978-1-4684-4703-3_24. [DOI] [PubMed] [Google Scholar]
  13. Schoenberg M., Eisenberg E. Muscle cross-bridge kinetics in rigor and in the presence of ATP analogues. Biophys J. 1985 Dec;48(6):863–871. doi: 10.1016/S0006-3495(85)83847-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Schoenberg M. Equilibrium muscle cross-bridge behavior. Theoretical considerations. Biophys J. 1985 Sep;48(3):467–475. doi: 10.1016/S0006-3495(85)83802-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Trybus K. M., Taylor E. W. Transient kinetics of adenosine 5'-diphosphate and adenosine 5'-(beta, gamma-imidotriphosphate) binding to subfragment 1 and actosubfragment 1. Biochemistry. 1982 Mar 16;21(6):1284–1294. doi: 10.1021/bi00535a028. [DOI] [PubMed] [Google Scholar]

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