Literature DB >> 302331

The force-velocity relationship in vertebrate muscle fibres at varied tonicity of the extracellular medium.

K A Edman, J C Hwang.   

Abstract

1. The relationship between active force and velocity of shortening was studied during tetanic contraction of isolated semitendinosus muscle fibres of the frog (0.5-2.0 degrees C). Measurements were carried out with the fibre immersed in isotonic (1.00R) Ringer solution and in solutions that were made hypotonic by reduction of NaCl (osmolality 0.62 and 0.81 of normal Ringer) and hypertonic by addition of sucrose (osmolality 1.22 and 1.44 of normal Ringer).2. The force-velocity relation was hyperbolic at loads lower than 80% of measured isometric force (P(0)) but exhibited a reversed curvature between 0.8P(0) and P(0). The maximum velocity of shortening was determined in two different ways: (i) by extrapolation to zero load from force-velocity data truncated at 0.8P(0) (computer fitting of hyperbola, leastsquares method) and (ii) by recording the time required to take up the slack of the fibre after a quick release during tetanus.3. Isometric force and maximum speed of shortening both changed inversely with the tonicity of the extracellular medium. Immersion of the fibre in 0.81R hypotonic solution caused active tension and shortening velocity to increase by 10 +/- 1% (mean +/- S.E. of mean, n = 14) and 12 +/- 1%, respectively. Conversely, force and shortening velocity decreased by 12 +/- 1% (n = 13) and 22 +/- 2% when normal Ringer was replaced by 1.22R hypertonic solution. These changes doubled when the tonicity was altered from normal Ringer to 0.62R and 1.44R, respectively.4. Changes in fibre cross-sectional area equivalent to those obtained in the 0.81R and 1.22R solutions (+11% and -13%, respectively) were produced by varying the sarcomere length within the range 2.0-2.5 mum in the normal Ringer solution. Maximum velocity of shortening remained very nearly constant under these conditions, indicating that the shortening velocity, like the isometric force, is not critically dependent on changes in myofilament lattice width over the range considered.5. The results support the view that both shortening velocity and active force are modulated by changes of the intracellular ionic strength above and below the level that normally exists in the intact muscle fibre.

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Year:  1977        PMID: 302331      PMCID: PMC1283712          DOI: 10.1113/jphysiol.1977.sp011901

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  22 in total

1.  Non-hyperbolic force-velocity relationship in single muscle fibres.

Authors:  K A Edman; L A Mulieri; B Scubon-Mulieri
Journal:  Acta Physiol Scand       Date:  1976-10

2.  SARCOPLASMIC RETICULUM. I. THE UPTAKE OF CA++ BY SARCOPLASMIC RETICULUM FRAGMENTS.

Authors:  A MARTONOSI; R FERETOS
Journal:  J Biol Chem       Date:  1964-02       Impact factor: 5.157

3.  The behaviour of frog muscle in hypertonic solutions.

Authors:  J V HOWARTH
Journal:  J Physiol       Date:  1958-11-10       Impact factor: 5.182

4.  Electron microscope studies of the organisation of the filaments in striated muscle.

Authors:  H E HUXLEY
Journal:  Biochim Biophys Acta       Date:  1953-11

5.  Mechanical deactivation induced by active shortening in isolated muscle fibres of the frog.

Authors:  K A Edman
Journal:  J Physiol       Date:  1975-03       Impact factor: 5.182

6.  Ca++ uptake in muscle microsomes. Activation by polyamines.

Authors:  L De Meis
Journal:  J Biol Chem       Date:  1968-03-25       Impact factor: 5.157

7.  Myosin adenosine triphosphatase. Convergence of activation by actin and by SH1 modification at physiological ionic strength.

Authors:  M Burke; E Reisler; S Himmelfarb; W F Harrington
Journal:  J Biol Chem       Date:  1974-10-10       Impact factor: 5.157

8.  Changes in sarcomere length during isometric tension development in frog skeletal muscle.

Authors:  D R Cleworth; K A Edman
Journal:  J Physiol       Date:  1972-12       Impact factor: 5.182

9.  On the relationships between membrane potential, calcium transient and tension in single barnacle muscle fibres.

Authors:  C C Ashley; E B Ridgway
Journal:  J Physiol       Date:  1970-07       Impact factor: 5.182

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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  52 in total

1.  An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle.

Authors:  R Elangovan; M Capitanio; L Melli; F S Pavone; V Lombardi; G Piazzesi
Journal:  J Physiol       Date:  2011-12-23       Impact factor: 5.182

2.  Mechanism of force enhancement during and after lengthening of active muscle: a temperature dependence study.

Authors:  H Roots; G J Pinniger; G W Offer; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2012-06-16       Impact factor: 2.698

3.  Effects of solution tonicity on crossbridge properties and myosin lever arm disposition in intact frog muscle fibres.

Authors:  Barbara Colombini; Maria Angela Bagni; Giovanni Cecchi; Peter John Griffiths
Journal:  J Physiol       Date:  2006-10-05       Impact factor: 5.182

4.  Effect of ionic strength on crossbridge kinetics as studied by sinusoidal analysis, ATP hydrolysis rate and X-ray diffraction techniques in chemically skinned rabbit psoas fibres.

Authors:  M Kawai; J S Wray; K Güth
Journal:  J Muscle Res Cell Motil       Date:  1990-10       Impact factor: 2.698

5.  When fibres go slack and cross bridges are free to run: a brilliant method to study kinetic properties of acto-myosin interaction.

Authors:  Carlo Reggiani
Journal:  J Physiol       Date:  2007-06-14       Impact factor: 5.182

6.  The force bearing capacity of frog muscle fibres during stretch: its relation to sarcomere length and fibre width.

Authors:  K A Edman
Journal:  J Physiol       Date:  1999-09-01       Impact factor: 5.182

7.  Metabolic changes with fatigue in different types of single muscle fibres of Xenopus laevis.

Authors:  A S Nagesser; W J van der Laarse; G Elzinga
Journal:  J Physiol       Date:  1992-03       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.  Force-velocity relation in normal and nitrate-treated frog single muscle fibres during rise of tension in an isometric tetanus.

Authors:  G Cecchi; F Colomo; V Lombardi
Journal:  J Physiol       Date:  1978-12       Impact factor: 5.182

10.  Recovery of fatigued Xenopus muscle fibres is markedly affected by the extracellular tonicity.

Authors:  H Westerblad; J Lännergren
Journal:  J Muscle Res Cell Motil       Date:  1990-04       Impact factor: 2.698

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