Literature DB >> 1593453

Tension responses to joule temperature jump in skinned rabbit muscle fibres.

S Y Bershitsky1, A K Tsaturyan.   

Abstract

1. Joule temperature jumps (T-jumps) from 5-9 degrees C up to 40 degrees C were used to study the cross-bridge kinetics and thermodynamics in skinned rabbit muscle fibres. To produce a T-jump, an alternating current pulse was passed through a fibre 5 s after removing the activating solution (pCa congruent to 4.5) from the experimental trough. The pulse frequency was congruent to 30 kHz, amplitude less than or equal to 3 kV, and duration 0.2 ms. The pulse energy liberated in the fibre was calculated using a special analog circuit and then used for estimation of the T-jump amplitude. 2. The T-jump induced a tri-exponential tension transient. Phases 1 and 2 had rate constants k1 = 450-1750 s-1 and k2 = 60-250 s-1 respectively, characterizing the tension rise, whereas phase 3 had a rate constant k3 = 5-10 s-1 representing tension recovery due to the fibre cooling. 3. An increase from 13 to 40 degrees C for the final temperature achieved by the T-jump led to an increase in the amplitudes of phases 1 and 2. After T-jumps to 30-40 degrees C during phase 1, tension increased by 50-80%. During phase 2 an approximately 2-fold tension increase continued. Rate constants k1 and k2 increased with temperature and temperature coefficients (Q10) were 1.6 and 1.7, respectively. 4. To study which processes in the cross-bridges are involved in phases 1 and 2, a series of experiments were made where step length changes of -9 to +3 nm (hs)-1 (nanometres per half-sarcomere length) were applied to the fibre 4 ms before the T-jump. 5. After the step shortening, the rate constant of phase 1 increased, whereas its amplitude decreased compared to those without a length change. This indicates that phase 1 is determined by some force-generating process in the cross-bridges attached to the thin filaments. This process is, most probably, the same as that producing the early tension recovery following the length change. The enthalpy change (delta H) associated with the reaction controlling this process was estimated to be positive (15-30 kJ mol-1). 6. Both the rate constant k2 and the maximal tension achieved at the end of phase 2 were practically independent of the preceding length changes. This means that phase 2 is accompanied by the cross-bridge detachment and reattachment to new sites on the thin filaments.(ABSTRACT TRUNCATED AT 400 WORDS)

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Mesh:

Year:  1992        PMID: 1593453      PMCID: PMC1176044          DOI: 10.1113/jphysiol.1992.sp019010

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


  25 in total

1.  A Fourier method for the analysis of exponential decay curves.

Authors:  S W Provencher
Journal:  Biophys J       Date:  1976-01       Impact factor: 4.033

2.  Effect of joule temperature jump on tension and stiffness of skinned rabbit muscle fibers.

Authors:  A K Tsaturyan
Journal:  Biophys J       Date:  1989-11       Impact factor: 4.033

3.  Transmission phenomena and early tension recovery in skinned muscle fibres of the frog.

Authors:  T Blangé; G J Stienen
Journal:  Pflugers Arch       Date:  1985-09       Impact factor: 3.657

4.  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

5.  Heat changes during transient tension responses to small releases in active frog muscle.

Authors:  S H Gilbert; L E Ford
Journal:  Biophys J       Date:  1988-10       Impact factor: 4.033

6.  The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution.

Authors:  B Brenner
Journal:  Basic Res Cardiol       Date:  1986       Impact factor: 17.165

7.  Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad.

Authors:  D G Stephenson; D A Williams
Journal:  J Physiol       Date:  1985-03       Impact factor: 5.182

8.  Tension transients during steady shortening of frog muscle fibres.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1985-04       Impact factor: 5.182

9.  The stiffness of frog skinned muscle fibres at altered lateral filament spacing.

Authors:  Y E Goldman; R M Simmons
Journal:  J Physiol       Date:  1986-09       Impact factor: 5.182

10.  A model of crossbridge action: the effects of ATP, ADP and Pi.

Authors:  E Pate; R Cooke
Journal:  J Muscle Res Cell Motil       Date:  1989-06       Impact factor: 2.698

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  40 in total

1.  Imaging of thermal activation of actomyosin motors.

Authors:  H Kato; T Nishizaka; T Iga; K Kinosita; S Ishiwata
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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.  Temperature change does not affect force between single actin filaments and HMM from rabbit muscles.

Authors:  M Kawai; K Kawaguchi; M Saito; S Ishiwata
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

Review 4.  Mechanics and models of the myosin motor.

Authors:  A F Huxley
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

5.  Structural responses to the photolytic release of ATP in frog muscle fibres, observed by time-resolved X-ray diffraction.

Authors:  A K Tsaturyan; S Y Bershitsky; R Burns; Z H He; M A Ferenczi
Journal:  J Physiol       Date:  1999-11-01       Impact factor: 5.182

6.  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

7.  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

Review 8.  What do we learn by studying the temperature effect on isometric tension and tension transients in mammalian striated muscle fibres?

Authors:  Masataka Kawai
Journal:  J Muscle Res Cell Motil       Date:  2003       Impact factor: 2.698

9.  Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.

Authors:  Sergey Y Bershitsky; Natalia A Koubassova; Pauline M Bennett; Michael A Ferenczi; Dmitry A Shestakov; Andrey K Tsaturyan
Journal:  Biophys J       Date:  2010-09-22       Impact factor: 4.033

Review 10.  Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  2010-10-01       Impact factor: 5.182

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