Literature DB >> 1491070

Unloaded shortening after a quick release of a contracting, single fibre from crayfish slow muscle.

T Tameyasu1.   

Abstract

The time course of shortening at zero load was studied by the slack test method during tetanic contractions in isolated, single, slow muscle fibres of the crayfish. In 28 of 32 shortenings (from 14 different fibres) a biphasic shortening was seen, which consisted of an initial high-velocity phase lasting 3.3-20.8 ms and a following slow-velocity phase lasting for the entire time examined (up to 89.2 ms). Provided that the shortening occurred uniformly along the fibre length, velocity in the initial phase, V1, of the biphasic shortening was 14.4 +/- 3.4 (mean +/- SD, n = 10) microns s-1 per half sarcomere at Lo, the slack length, at 20 degrees C, while that in the second phase, V2, was 7.4 +/- 1.4 microns s-1 per half sarcomere. Lowering temperature decreased both V1 and V2 with Q10 = 1.4 for V1 and 2.0 for V2. Lowering the external Ca concentration from 15 mM, the standard, to 2 mM resulted in a tetanic tension below one-third of that at 15 mM Ca and decreased both V1 (t test; p < 0.01) and V2 (p < 0.001). Prestretching the fibre to 1.5 Lo had no significant effect on V2 (p < 0.3) but increased V1 (p < 0.001). The distance shortened during the initial high-velocity phase, LV1, was 4.0 +/- 1.8% Lo (mean +/- SD, n = 10) at 20 degrees C or about 0.14 microns per half sarcomere on average. LV1 was independent of the tetanic tension level when it was changed by lowering the external Ca concentration or temperature in the same fibre. Prestretching the fibre to 1.5 Lo, at which the sum of the active and the resting tension was lower than Po at Lo in two of three fibres, increased LV1 significantly (p < 0.001). The independency of LV1 from the tension level indicates that the initial high-velocity phase was not from shortening of some inert components in the fibre. One possibility is that the initial high-velocity phase was brought about by an acceleration of shortening by a compressive force, the origin of which has been discussed. The slow-velocity phase seemed to result from the crossbridge turnover with little exogeneous stress on myofilaments. Four different fibres exhibited an unloaded shortening with a constant velocity during the entire time examined (29.9-61.8 ms). This type of shortening had a velocity between the usual V1 and V2 values, suggesting that a compressive force accelerated the shortening during the entire time.

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Year:  1992        PMID: 1491070     DOI: 10.1007/bf01738251

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  27 in total

1.  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

2.  Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres.

Authors:  Y E Goldman; J A McCray; K W Ranatunga
Journal:  J Physiol       Date:  1987-11       Impact factor: 5.182

3.  Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation.

Authors:  R L Moss
Journal:  J Physiol       Date:  1986-08       Impact factor: 5.182

4.  The effect of external calcium ions on the excitation-contraction coupling in single muscle fibres of the crayfish.

Authors:  D Zacharová; J Zachar
Journal:  Physiol Bohemoslov       Date:  1967

Review 5.  Sarcomere-associated cytoskeletal lattices in striated muscle. Review and hypothesis.

Authors:  K Wang
Journal:  Cell Muscle Motil       Date:  1985

6.  Isotonic velocity transients in frog muscle fibres following quick changes in load.

Authors:  H Sugi; T Tsuchiya
Journal:  J Physiol       Date:  1981       Impact factor: 5.182

7.  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

8.  The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres.

Authors:  K A Edman
Journal:  J Physiol       Date:  1979-06       Impact factor: 5.182

9.  The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments.

Authors:  R Horowits; R J Podolsky
Journal:  J Cell Biol       Date:  1987-11       Impact factor: 10.539

10.  ATPase activity of myosin correlated with speed of muscle shortening.

Authors:  M Bárány
Journal:  J Gen Physiol       Date:  1967-07       Impact factor: 4.086

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  3 in total

1.  Effects of myofibrillar bundle diameter on the unloaded shortening velocity of skinned skeletal muscle fibres.

Authors:  K Hilber; S Galler
Journal:  J Muscle Res Cell Motil       Date:  1998-02       Impact factor: 2.698

2.  Unloaded shortening of skinned mammalian skeletal muscle fibres: effects of the experimental approach and passive force.

Authors:  S Galler; K Hilber
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

3.  Force per cross-sectional area from molecules to muscles: a general property of biological motors.

Authors:  Jean-Pierre Rospars; Nicole Meyer-Vernet
Journal:  R Soc Open Sci       Date:  2016-07-20       Impact factor: 2.963

  3 in total

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