Literature DB >> 8519955

Compliance of thin filaments in skinned fibers of rabbit skeletal muscle.

H Higuchi1, T Yanagida, Y E Goldman.   

Abstract

The mechanical compliance (reciprocal of stiffness) of thin filaments was estimated from the relative compliance of single, skinned muscle fibers in rigor at sarcomere lengths between 1.8 and 2.4 micron. The compliance of the fibers was calculated as the ratio of sarcomere length change to tension change during imposition of repetitive cycles of small stretches and releases. Fiber compliance decreased as the sarcomere length was decreased below 2.4 micron. The compliance of the thin filaments could be estimated from this decrement because in this range of lengths overlap between the thick and thin filaments is complete and all of the myosin heads bind to the thin filament in rigor. Thus, the compliance of the overlap region of the sarcomere is constant as length is changed and the decrease in fiber compliance is due to decrease of the nonoverlap length of the thin filaments (the I band). The compliance value obtained for the thin filaments implies that at 2.4-microns sarcomere length, the thin filaments contribute approximately 55% of the total sarcomere compliance. Considering that the sarcomeres are approximately 1.25-fold more compliant in active isometric contractions than in rigor, the thin filaments contribute approximately 44% to sarcomere compliance during isometric contraction.

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Year:  1995        PMID: 8519955      PMCID: PMC1236329          DOI: 10.1016/S0006-3495(95)79975-1

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


  45 in total

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Journal:  Prog Biophys Biophys Chem       Date:  1957

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Journal:  Nature       Date:  1975-06-26       Impact factor: 49.962

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Authors:  Y E Goldman; R M Simmons
Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

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Authors:  R Craig
Journal:  J Mol Biol       Date:  1977-01-05       Impact factor: 5.469

5.  Tension responses to sudden length change in stimulated frog muscle fibres near slack length.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

6.  X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle.

Authors:  J C Haselgrove; H E Huxley
Journal:  J Mol Biol       Date:  1973-07-15       Impact factor: 5.469

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Authors:  I Otsuki
Journal:  J Biochem       Date:  1974-04       Impact factor: 3.387

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

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Authors:  R Cooke; K Franks
Journal:  Biochemistry       Date:  1980-05-13       Impact factor: 3.162

10.  Sizes of components in frog skeletal muscle measured by methods of stereology.

Authors:  B A Mobley; B R Eisenberg
Journal:  J Gen Physiol       Date:  1975-07       Impact factor: 4.086

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  109 in total

1.  Effect of stretching on undamped elasticity in muscle fibres from Rana temporaria.

Authors:  M Mantovani; G A Cavagna; N C Heglund
Journal:  J Muscle Res Cell Motil       Date:  1999-01       Impact factor: 2.698

2.  Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers.

Authors:  A K Tsaturyan; S Y Bershitsky; R Burns; M A Ferenczi
Journal:  Biophys J       Date:  1999-07       Impact factor: 4.033

3.  Detection of fluorescently labeled actin-bound cross-bridges in actively contracting myofibrils.

Authors:  W C Cooper; L R Chrin; C L Berger
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

4.  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

5.  Influence of ionic strength on the actomyosin reaction steps in contracting skeletal muscle fibers.

Authors:  H Iwamoto
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

Review 6.  Cooperativity of myosin molecules through strain-dependent chemistry.

Authors:  T Duke
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

7.  High-resolution structure of hair-cell tip links.

Authors:  B Kachar; M Parakkal; M Kurc; Y Zhao; P G Gillespie
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

8.  Clamped-filament elongation model for actin-based motors.

Authors:  Richard B Dickinson; Daniel L Purich
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

9.  Synchronous oscillations of length and stiffness during loaded shortening of frog muscle fibres.

Authors:  K A Edman; N A Curtin
Journal:  J Physiol       Date:  2001-07-15       Impact factor: 5.182

10.  The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit.

Authors:  Sergey Y Bershitsky; Andrey K Tsaturyan
Journal:  J Physiol       Date:  2002-05-01       Impact factor: 5.182

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