Series elastic properties of skinned muscle fibres in contraction and rigor

Yamamoto, Tomoka; Herzig, J. W.

doi:10.1007/bf00581144

Cited by 40 publications

(32 citation statements)

References 6 publications

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“…To quantitate the thermal expansion, the tension response to imposed quick length changes of the same order was measured. Tension in a fibre in the rigor state changed in proportion to the length step and there was little tension recovery following the length step (Goldman & Simmons, 1977;Yamamoto & Herzig, 1978).…”

Section: Laser T-jumps In Skinned Muscle Fibres 79mentioning

confidence: 99%

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

Goldman

McCray

Ranatunga

1987

The Journal of Physiology

108

166

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SUMMARY1. A technique was developed to generate 2-8°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 usm heated the fibre and surrounding solution in approximately 150 /is. The signal from a 100 ,um 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 rubberlike) 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 ,um. 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°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-5 at 20 '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

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Section: Laser T-jumps In Skinned Muscle Fibres 79mentioning

confidence: 99%

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

Goldman

McCray

Ranatunga

1987

The Journal of Physiology

108

166

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“…Stress-relaxation in rigor is highly dependent on the time since the stretch was applied. In frog muscle there is a very early, small decay of tension followed by near constancy over the next 50 ms (Goldman & Simmons, 1977;Yamamoto & Herzig, 1978). In skinned rabbit muscle Schoenberg & Eisenberg, (1985) round a continuously slowing fall from 3 ms onwards, whose slope increased in AMPPNP.…”

Section: Condition Slope N (S -1 X 105)mentioning

confidence: 96%

Slip of rabbit striated muscle in rigor or AMPPNP

Somasundaram

Newport

Tregear

1989

J Muscle Res Cell Motil

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Single glycerol-extracted rabbit psoas muscle fibres have been slowly extended either in rigor or in the unhydrolysable ATP analogue, AMPPNP, and their sarcomere length, sarcomere structure and tension measured. The length of regularly arrayed sarcomeres, measured by optical diffraction, increased continuously as the muscle was stretched; the maximum sarcomere extension seen was approximately 6%. In the electron microscope sarcomeres from extended muscle fixed in rigor or AMPPNP remained regular in their internal structure, without rupture or obvious lengthening around the Z line. During steady extension at 0.024% per min the tension in the muscle fibre rose until it reached a limiting value [Tm] when the sarcomeres had stretched by 0.8-1.6% and then remained constant with continued extension, while the sarcomeres continued to stretch. Provided that a novel form of preparation of the glycerol-extracted fibres was employed, Tm in rigor was a large fraction of the tension expected from an active isometric muscle fibre. In the presence of AMPPNP Tm was reduced by a factor of 2 to 3. Step extension by 0.08% at 5-min intervals gave the same pattern of mechanical response with similar values of Tm. The isometric tension decay in the interval between the steps was very rapid at first and slowed continuously until the next step. The average speed of tension fall between 30 and 300 s after stretch was measured at each step and plotted relative to the tension in the muscle. The relationship approached linearity, although with a significant upward curvature at high tension.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The arrangement of this elasticity is classically represented using a three-component Hill muscle model [11][12][13], which comprises a contractile element (CE, muscle fibres), a series elastic element (SEE, elastic tendon/aponeurosis at either end of the muscle) and an elastic element in parallel with the contractile component (PEE, titin, perimysium). Muscle fibres also have inherent elasticity (what is represented within the SEE in the classical Hill model as Hill worked on fibre bundles [14][15][16]). Here, we focus on larger animals where the compliance of the tendon and aponeurosis will be much greater than that of the fascicles [13] and the fascicles can be approximated to be only contractile in nature.…”

Section: Muscle -Tendon Elasticitymentioning

confidence: 99%

The anatomical arrangement of muscle and tendon enhances limb versatility and locomotor performance

Wilson

Lichtwark

2011

Phil. Trans. R. Soc. B

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The arrangement of muscles and tendons has been studied in detail by anatomists, surgeons and biomechanists for over a century, and the energetics and mechanics of muscle contraction for almost as long. Investigation of how muscles function during locomotion and the relative length change in muscle fibres and the associated elastic tendon has, however, been more challenging. In recent years, novel in vivo measurement methods such as ultrasound and sonomicrometry have contributed to our understanding of the dynamics of the muscle tendon unit during locomotion. Here, we examine both published and new data to explore how muscles are arranged to deliver the wide repertoire of locomotor function and the trade-offs between performance and economy that result.

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Series elastic properties of skinned muscle fibres in contraction and rigor

Cited by 40 publications

References 6 publications

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

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

Slip of rabbit striated muscle in rigor or AMPPNP

The anatomical arrangement of muscle and tendon enhances limb versatility and locomotor performance

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