Literature DB >> 3446791

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

Y E Goldman1, J A McCray, K W Ranatunga.   

Abstract

1. A technique was developed to generate 2-8 degrees C step temperature perturbations (T-jumps) in single muscle fibres to study the thermodynamics of muscle contraction. A solid-state pulsed holmium laser emitting at 2.065 microns heated the fibre and surrounding solution in approximately 150 mus. The signal from a 100 microns thermocouple fed back to a heating wire maintained the elevated temperature after the laser pulse. 2. Tension of glycerol-extracted muscle fibres from rabbit psoas muscle did not change significantly following T-jumps when the fibre was relaxed. 3. In rigor, tension decreased abruptly on heating indicating normal (not rubber-like) thermoelasticity. The thermoelastic coefficient (negative ratio of relative length change to relative temperature change) of the fibre was estimated to be -0.021 at sarcomere lengths of 2.5-2.8 microns. Rigor tension was constant after the temperature step and returned to the original value on recooling. 4. In maximal Ca2+ activation, tension transients initiated by T-jumps had several phases. An immediate tension decrease suggests that thermoelasticity during contraction is similar to that in rigor. Active tension then recovered to the value before the T-jump with an apparent rate constant of approximately 400 s-1 (at 10-20 degrees C). This rate constant did not have an appreciable dependence on the final temperature. Finally, tension increased exponentially to a new higher level with a rate constant of approximately 20 s-1 at 20 degrees C. This rate constant increased with temperature with a Q10 of 1.4. 5. At submaximal Ca2+ activation the tension rise was followed by a decay to below the value before the T-jump. This decline was expected from the temperature dependence of steady pCa-tension curves. The final tension decline occurred on the 1-5 s time scale. 6. The value and amplitude dependence of the rate constant for the quick recovery following T-jumps were similar to those of the quick recovery following length steps during active contractions. The enthalpy change associated with the quick tension recovery following temperature-step perturbations was estimated to be positive suggesting that the recovery process is an endothermic reaction. Slower reaction steps on the 10-30 ms timescale, as well as reactions corresponding to the quick recovery, may contribute to the cross-bridge power stroke.

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Year:  1987        PMID: 3446791      PMCID: PMC1192294          DOI: 10.1113/jphysiol.1987.sp016770

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


  36 in total

1.  Active and rigor muscle stiffness [proceedings].

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

2.  Series elastic properties of skinned muscle fibres in contraction and rigor.

Authors:  T Yamamoto; J W Herzig
Journal:  Pflugers Arch       Date:  1978-01-31       Impact factor: 3.657

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.  Temperature-dependence of local melting in the myosin subfragment-2 region of the rigor cross-bridge.

Authors:  H Ueno; W F Harrington
Journal:  J Mol Biol       Date:  1986-07-05       Impact factor: 5.469

5.  Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.

Authors:  S S Rosenfeld; E W Taylor
Journal:  J Biol Chem       Date:  1985-01-10       Impact factor: 5.157

6.  Temperature and amplitude dependence of tension transients in glycerinated skeletal and insect fibrillar muscle.

Authors:  R H Abbott; G J Steiger
Journal:  J Physiol       Date:  1977-03       Impact factor: 5.182

7.  Contractile deactivation by rapid, microwave-induced temperature jumps.

Authors:  B D Lindley; B Kuyel
Journal:  Biophys J       Date:  1978-10       Impact factor: 4.033

8.  Temperature-dependence of shortening velocity and rate of isometric tension development in rat skeletal muscle.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  1982-08       Impact factor: 5.182

9.  The kinetics of magnesium adenosine triphosphate cleavage in skinned muscle fibres of the rabbit.

Authors:  M A Ferenczi; E Homsher; D R Trentham
Journal:  J Physiol       Date:  1984-07       Impact factor: 5.182

10.  Conformational transition in the myosin hinge upon activation of muscle.

Authors:  H Ueno; W F Harrington
Journal:  Proc Natl Acad Sci U S A       Date:  1981-10       Impact factor: 11.205

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  61 in total

1.  Imaging of thermal activation of actomyosin motors.

Authors:  H Kato; T Nishizaka; T Iga; K Kinosita; S Ishiwata
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

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

4.  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

5.  Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium.

Authors:  Hideaki Fujita; Masataka Kawai
Journal:  J Physiol       Date:  2002-02-15       Impact factor: 5.182

6.  Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest.

Authors:  K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

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

Authors:  T Tameyasu
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

10.  Hydrostatic compression in glycerinated rabbit muscle fibers.

Authors:  K W Ranatunga; N S Fortune; M A Geeves
Journal:  Biophys J       Date:  1990-12       Impact factor: 4.033

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