Pressure sensitivity of active tension in glycerinated rabbit psoas muscle fibres: Effects of ADP and phosphate

Fortune, N. S.; Geeves, Michael A.; Ranatunga, K. W.

doi:10.1007/bf01739967

Cited by 30 publications

(36 citation statements)

References 22 publications

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“…The steady tension in a fused tetanic contraction was typically reduced at increased hydrostatic pressure and it was comparable to the pressure-induced tension depression obtained in maximally Ca2"-activated skinned muscle fibres; this was attributed to an effect of high pressure on cycling cross-bridges (Geeves & Ranatunga, 1987;Fortune, Geeves & Ranatunga, 1989. Additionally, we argued that a small reduction in active tension in muscle fibres was expected from studies on the interaction between isolated actin and myosin subfragment-i (SI) in solution (Coates, Criddle & Geeves, 1985), which showed that high pressure inhibits a particular isomerization between two acto-Si complexes.…”

supporting

confidence: 52%

“…The basic design features of the pressure chamber were published by Geeves & Ranatunga (1987), the design of the transducer assembly by Fortune et al (1989) and the methodology used in recording transient tension responses following rapid (<1Ims) pressure release is described by Fortune et al (1991). MS 2132, pp.…”

Section: Methodsmentioning

confidence: 99%

“…The sarcomere length, as monitored by laser diffraction, was 2-2-2-6 um. Full details of the composition of experimental solutions are given elsewhere (Fortune et al 1989 It has been shown that high pressure has a negligible effect on the binding of calcium to EGTA buffers. Goldmann (1990) …”

Section: Methodsmentioning

confidence: 99%

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Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure.

Fortune

Geeves

Ranatunga

1994

The Journal of Physiology

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1. Effects of hydrostatic pressure (range 0.1-10 MPa) on the isometric tension of skinned (rabbit psoas) muscle fibres were examined at 12°C and at different levels of Ca2" activation (pCa range 4-7); the effects on both the steady tension and the tension transients induced by rapid pressure release (< 1 ms) are described. 2. The steady tension was depressed by increased pressure (-1 % MPa1) at a high level of Ca2" activation (pCa -4) whereas it was potentiated at lower Ca2" levels (pCa > 6); the effects were reversible. 3. At maximal Ca2+ activation, the tension recovery following pressure release (10 MPa to atmospheric) consisted of a fast (-30 s') and a slow (2-3 s-) phase; the rate and the normalized amplitude (normalized to the steady tension at atmospheric pressure for a particular pCa) of the fast phase were invariant with changes in Ca2+ level. 4. The effects of changing Ca2+ level on the slow phase were complex; its positive amplitude at high Ca2" levels changed to negative and the rate decreased to -1 s-I at low Ca2" levels (pCa > 6 0). 5. Results are discussed in relation to previous studies on the effect of pressure on intact muscle fibres and the actin-myosin interaction. This work supports calcium regulation of cross-bridge recruitment rather than calcium regulation of the rate of a specific step in the cross-bridge cycle.

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supporting

confidence: 52%

Section: Methodsmentioning

confidence: 99%

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Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure.

Fortune

Geeves

Ranatunga

1994

The Journal of Physiology

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“…In both fibre types, the addition of 10 mÒ BDM inhibited active contractions and abolished stretch activation seen at high temperatures (see Mutungi & Ranatunga, 1996a), but had no effect on the stretch-induced passive tension response. Experiments were also done to examine the main effects of chemical skinning on the passive tension components in fast and slow fibres: the relaxing solutions used for these experiments were similar to those described by Fortune, Geeves & Ranatunga (1989) and Ranatunga (1994) and they contained 5-10 mÒ MgATP and 15-20 mÒ EGTA (pH 7-7·1; ionic strength, 180-200 mÒ). The experiments were done at 10°C and a full set of data at a range of stretch velocities was initially collected from a preparation before skinning.…”

Section: Methodsmentioning

confidence: 99%

“…The experiments were done at 10°C and a full set of data at a range of stretch velocities was initially collected from a preparation before skinning. Then the Ringer solution was quickly replaced with skinning solution containing 0·5% Brij (Brij 58, Aldrich;Fortune et al 1989) while the preparation was still connected to the recording assembly. A preparation remained exposed to skinning solution for 1 h before a second set of passive tension responses was recorded in standard relaxing solution, for comparison with the responses from the intact preparation.…”

Section: Methodsmentioning

confidence: 99%

Temperature‐dependent changes in the viscoelasticity of intact resting mammalian (rat) fast‐ and slow‐twitch muscle fibres

Mutungi

Ranatunga

1998

The Journal of Physiology

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The tension and sarcomere length responses induced by ramp stretches (at amplitudes of 1‐3 % fibre length (Lo) and speeds of 0.01‐12 Lo s−1) were examined at different temperatures (range, 10‐35 °C) in resting intact muscle fibre bundles isolated from the soleus (a slow‐twitch muscle) and extensor digitorum longus (a fast‐twitch muscle) of the rat. Some observations are also presented on the effects of chemical skinning on passive viscoelasticity at 10 °C. As previously reported, the tension response to a ramp stretch, in different preparations and under various conditions, could be resolved into a viscous (P1), a viscoelastic (P2) and an elastic (P3) component and showed characteristic differences between slow and fast muscle fibres. Chemical skinning of the muscle fibres led to a decrease in the amplitude of all three tension components. However, the fast‐slow fibre differences remained after skinning. For example, the viscosity coefficient derived from P1 tension data decreased from 0.84 ± 0.06 before skinning to 0.44 ± 0.06 kN s m−2 after skinning in fast fibres; the corresponding values in slow fibres were 2.1 ± 0.08 and 0.87 ± 0.09 kN s m−2, respectively. Increasing the experimental temperature from 10 to 35 °C led to a decrease in all the tension components in both fast and slow muscle fibre bundles. The decrease of P1 (viscous) tension was such that the viscosity coefficient calculated using P1 data was reduced from 0.84 ± 0.1 to 0.43 ± 0.05 kN s m−2 in fast fibres and from 2.0 ± 0.1 to 1.0 ± 0.1 kN s m−2 in slow fibres (Q10 of ≈1.3 in both). In both fast and slow muscle fibre preparations, the plateau tension of the viscoelastic component (P2) decreased by 60‐80 % as the temperature was increased from 10 to 35 °C giving P2 tension a Q10 of ≈1.4 in slow fibres and ≈1.7 in the fast fibres. Additionally, the relaxation time of the viscoelasticity decreased from 11.9 ± 1 ms (fast) and 43.1 ± 1 ms (slow) at 10 °C to 3 ± 0.5 ms (fast) at 25 °C and 8.7 ± 0.6 ms (slow) at 35 °C (Q10 of ≈2.0 in slow and ≈2.5 in fast fibres). The fast‐slow fibre differences in passive viscoelasticity remained at the high physiological temperatures. The physiological significance of such fibre‐type differences and their possible underlying mechanisms are discussed.

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Vertebrate Skeletal and Cardiac Muscle

Hogan

Besch

1993

Advances in Comparative and Environmental Physiology

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Pressure sensitivity of active tension in glycerinated rabbit psoas muscle fibres: Effects of ADP and phosphate

Cited by 30 publications

References 22 publications

Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure.

Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure.

Temperature‐dependent changes in the viscoelasticity of intact resting mammalian (rat) fast‐ and slow‐twitch muscle fibres

Vertebrate Skeletal and Cardiac Muscle

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