Literature DB >> 8057258

The effect of hypertonicity on force generation in tetanized single fibres from frog skeletal muscle.

G Piazzesi1, M Linari, V Lombardi.   

Abstract

1. We compared the tension transient that follows a step change in sarcomere length in normal Ringer solution with that in Ringer solution made hypertonic by the addition of 98 mM sucrose. Steps were applied on tetanized single muscle fibres during either the isometric plateau or the steady force response to lengthening at low speed. Sarcomere length was controlled on selected fibre segments by a striation follower. Analysis is limited to phase 1 (the tension change simultaneous with the length step, mainly due to cross-bridge elasticity) and phase 2 (the quick phase of tension recovery, a manifestation of the cross-bridge elementary force-generating process). 2. At the isometric tetanus plateau the steady force is reduced by 19% in hypertonic solution, and the stiffness is slightly increased. During slow lengthening both steady force and stiffness are similar in normal solution and in hypertonic solution. In hypertonic solution the tension-to-stiffness ratio, a measure of the mean cross-bridge extension before the step, is markedly reduced in isometric conditions (-23%), but not during lengthening (-2%). 3. The plots of instantaneous tension versus the length change during the step show that in hypertonic medium the elasticity of the fibre is almost undamped. Thus the increase in stiffness cannot be attributed to an increase in viscosity. 4. In isometric conditions (T2-T1)/(Ti-T1), the proportion of the initial tension drop recovered at the end of phase 2, is not affected by hypertonicity for releases of moderate and large size (> 2 nm) and is reduced for small releases (< 2 nm) and for stretches. The abscissa intercept of the relation (T2-T1)/(Ti-T1) versus step amplitude is the same in both media. During lengthening, for releases of small and moderate size, (T2-T1)/(Ti-T1) is 20% lower in hypertonic solution. For large releases the slope of the relation is lower so that the abscissa intercept is not changed. 5. The speed of quick tension recovery following a step length change imposed in isometric conditions is slightly depressed in hypertonic solution. The relation between speed of recovery and step amplitude maintains its shape and is shifted downwards. During lengthening, the speed of quick tension recovery in hypertonic solution is less dependent on step amplitude than in normal solution, as if a more linear viscoelasticity is responsible for a large fraction of residual recovery.(ABSTRACT TRUNCATED AT 400 WORDS)

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Year:  1994        PMID: 8057258      PMCID: PMC1160465          DOI: 10.1113/jphysiol.1994.sp020152

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


  25 in total

1.  The behaviour of frog muscle in hypertonic solutions.

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

2.  The effects of tonicity on tension and stiffness of tetanized skeletal muscle fibres of the frog.

Authors:  A Månsson
Journal:  Acta Physiol Scand       Date:  1989-06

3.  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

4.  Muscular contraction.

Authors:  A F Huxley
Journal:  J Physiol       Date:  1974-11       Impact factor: 5.182

5.  Muscle contraction: the effect of ionic strength.

Authors:  E April; P W Brandt; J P Reuben; H Grundfest
Journal:  Nature       Date:  1968-10-12       Impact factor: 49.962

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

Authors:  K A Edman; J C Hwang
Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

7.  Kinetics of regeneration of cross-bridge power stroke in shortening muscle.

Authors:  G Piazzesi; M Linari; V Lombardi
Journal:  Adv Exp Med Biol       Date:  1993       Impact factor: 2.622

8.  The relation between stiffness and filament overlap in stimulated frog muscle fibres.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1981-02       Impact factor: 5.182

9.  [Effect of calcitonin on human gastric function].

Authors:  C Trovato; A Cerciello; R Carleo
Journal:  Boll Soc Ital Biol Sper       Date:  1981-01-15

10.  Critical dependence of calcium-activated force on width in highly compressed skinned fibers of the frog.

Authors:  J Gulati; A Babu
Journal:  Biophys J       Date:  1985-11       Impact factor: 4.033

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  11 in total

1.  Temperature dependence of the force-generating process in single fibres from frog skeletal muscle.

Authors:  G Piazzesi; M Reconditi; N Koubassova; V Decostre; M Linari; L Lucii; V Lombardi
Journal:  J Physiol       Date:  2003-03-28       Impact factor: 5.182

2.  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

3.  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

4.  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

5.  The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle.

Authors:  M Linari; G Piazzesi; V Lombardi
Journal:  Biophys J       Date:  2009-01       Impact factor: 4.033

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.  The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin.

Authors:  M Linari; I Dobbie; M Reconditi; N Koubassova; M Irving; G Piazzesi; V Lombardi
Journal:  Biophys J       Date:  1998-05       Impact factor: 4.033

8.  Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas.

Authors:  Marco Linari; Marco Caremani; Claudia Piperio; Philip Brandt; Vincenzo Lombardi
Journal:  Biophys J       Date:  2007-01-19       Impact factor: 4.033

9.  The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms.

Authors:  Marco Linari; Roberto Bottinelli; Maria Antonietta Pellegrino; Massimo Reconditi; Carlo Reggiani; Vincenzo Lombardi
Journal:  J Physiol       Date:  2003-10-10       Impact factor: 5.182

10.  Cross-bridge kinetics studied with staircase shortening in single fibres from frog skeletal muscle.

Authors:  M Linari; V Lombardi; G Piazzesi
Journal:  J Muscle Res Cell Motil       Date:  1997-02       Impact factor: 2.698

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