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Literature DB >> 6455168

Cross-bridge model of muscle contraction. Quantitative analysis.

Abstract

We recently presented, in a qualitative manner, a cross-bridge model of muscle contraction which was based on a biochemical kinetic cycle for the actomyosin ATPase activity. This cross-bridge model consisted of two cross-bridge states detached from actin and two cross-bridge states attached to actin. In the present paper, we attempt to fit this model quantitatively to both biochemical and physiological data. We find that the resulting complete cross-bridge model is able to account reasonably well for both the isometric transient data observed when a muscle is subjected to a sudden change in length and for the relationship between the velocity of muscle contraction in vivo and the actomyosin ATPase activity in vitro. This model also illustrates the interrelationship between biochemical and physiological data necessary for the development of a complete cross-bridge model of muscle contraction.

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Year: 1980 PMID： 6455168 PMCID： PMC1328691 DOI： 10.1016/S0006-3495(80)85126-5

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

33 in total

1. The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation.

Authors: E Eisenberg; C Moos
Journal: Biochemistry Date: 1968-04 Impact factor: 3.162

2. The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Appendix. Free energy and enthalpy of atp hydrolysis in the sarcoplasm.

Authors: M J Kushmerick; R E Davies
Journal: Proc R Soc Lond B Biol Sci Date: 1969-12-23

3. Effect of temperature on actin activation of heavy meromyosin ATPase.

Authors: W W Barouch; C Moos
Journal: Biochim Biophys Acta Date: 1971-05-11

4. Proposed mechanism of force generation in striated muscle.

Authors: A F Huxley; R M Simmons
Journal: Nature Date: 1971-10-22 Impact factor: 49.962

5. Effect of pH and metal ion concentration on the equilibrium hydrolysis of adenosine triphosphate to adenosine diphosphate.

Authors: R A Alberty
Journal: J Biol Chem Date: 1968-04-10 Impact factor: 5.157

6. Actin-heavy meromyosin biding. Determination of binding stoichiometry from adenosine triphosphatase kinetic measurements.

Authors: A A Rizzino; W W Barouch; E Eisenberg; C Moos
Journal: Biochemistry Date: 1970-06-09 Impact factor: 3.162

7. A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stages.

Authors: A F Huxley
Journal: Proc R Soc Lond B Biol Sci Date: 1973-02-27

8. Equilibrium binding of adenosine diphosphate to myosin.

Authors: S Lowey; S M Luck
Journal: Biochemistry Date: 1969-08 Impact factor: 3.162

9. The variation in isometric tension with sarcomere length in vertebrate muscle fibres.

Authors: A M Gordon; A F Huxley; F J Julian
Journal: J Physiol Date: 1966-05 Impact factor: 5.182

10. The reversibility of adenosine triphosphate cleavage by myosin.

Authors: C R Bagshaw; D R Trentham
Journal: Biochem J Date: 1973-06 Impact factor: 3.857

167 in total

1. A weakly coupled version of the Huxley crossbridge model can simulate energetics of amphibian and mammalian skeletal muscle.

Authors: C J Barclay
Journal: J Muscle Res Cell Motil Date: 1999-02 Impact factor: 2.698

2. Shortening properties of two biochemically defined muscle fibre types of the Norway lobster Nephrops norvegicus L.

Authors: J M Holmes; K Hilber; S Galler; D M Neil
Journal: J Muscle Res Cell Motil Date: 1999-04 Impact factor: 2.698

3. Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.

Authors: R Stehle; B Brenner
Journal: Biophys J Date: 2000-03 Impact factor: 4.033

Cross-bridge model of muscle contraction. Quantitative analysis.

1. The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation.

2. The chemical energetics of muscle contraction. II. The chemistry, efficiency and power of maximally working sartorius muscles. Appendix. Free energy and enthalpy of atp hydrolysis in the sarcoplasm.

3. Effect of temperature on actin activation of heavy meromyosin ATPase.

4. Proposed mechanism of force generation in striated muscle.

5. Effect of pH and metal ion concentration on the equilibrium hydrolysis of adenosine triphosphate to adenosine diphosphate.

6. Actin-heavy meromyosin biding. Determination of binding stoichiometry from adenosine triphosphatase kinetic measurements.

7. A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stages.

8. Equilibrium binding of adenosine diphosphate to myosin.

9. The variation in isometric tension with sarcomere length in vertebrate muscle fibres.

10. The reversibility of adenosine triphosphate cleavage by myosin.

1. A weakly coupled version of the Huxley crossbridge model can simulate energetics of amphibian and mammalian skeletal muscle.

2. Shortening properties of two biochemically defined muscle fibre types of the Norway lobster Nephrops norvegicus L.

3. Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.

Review 4. Cooperativity of myosin molecules through strain-dependent chemistry.

5. Theoretical formalism for kinesin motility I. Bead movement powered by single one-headed kinesins.

6. Molecular model of muscle contraction.

7. Two heads of myosin are better than one for generating force and motion.

8. Stretch activation and myosin heavy chain isoforms of rat, rabbit and human skeletal muscle fibres.

9. Dependency of the force-velocity relationships on Mg ATP in different types of muscle fibers from Xenopus laevis.

10. Stretch activation, unloaded shortening velocity, and myosin heavy chain isoforms of rat skeletal muscle fibres.