Influence of Ionic Strength on Contractile Force and Energy Consumption of Skinned Fibers From Mammalian and Crustacean Striated Muscle

Godt, R. E.; Fogaça, R. T. H.; Andrews, Mark A.; Nosek, Thomas M.

doi:10.1007/978-1-4615-2872-2_67

Cited by 7 publications

(10 citation statements)

References 29 publications

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“…These effects of IS are much smaller than those reported for permeabilized mammalian fibres (Kawai et al 1990; Godt et al 1993; Seow & Ford, 1993; Iwamoto, 2000). Isometric force produced by rabbit fibres is diminished considerably by raising the IS with potassium propionate over a range similar to that used here; for example, Kawai et al (1990) reported a reduction of 50% in force when IS was increased from 200 to 300 mmol l −1 .…”

Section: Discussioncontrasting

confidence: 59%

“…Isometric force produced by rabbit fibres is diminished considerably by raising the IS with potassium propionate over a range similar to that used here; for example, Kawai et al (1990) reported a reduction of 50% in force when IS was increased from 200 to 300 mmol l −1 . Steady‐state ATPase of mammalian muscle is also reduced by raising the IS, but by less than the force reduction (Kawai et al 1990; Godt et al 1993).…”

Section: Discussionmentioning

confidence: 99%

“…This effect of IS is not simply due to a reduction in the number of cross‐bridges attached because stiffness and force do not remain proportional when IS is changed. Stiffness increases relative to force in studies at very low temperatures (1–5°C; Seow & Ford, 1993; Iwamoto, 2000), but decreases in proportion to force near 20°C (Kawai et al 1990; Godt et al 1993). Thus it seems that the relative importance of ionic interactions and hydrophobic interactions in determining force varies with temperature.…”

mentioning

confidence: 99%

“…Experiments with mammalian fibres have shown that at subphysiological temperatures (0–20°C) force is strongly depressed as ionic strength is increased beyond the physiological value of 200 mmol l −1 (Kawai et al 1990; Godt et al 1993; Seow & Ford, 1993; Iwamoto, 2000). This effect of IS is not simply due to a reduction in the number of cross‐bridges attached because stiffness and force do not remain proportional when IS is changed.…”

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confidence: 99%

“…Species difference in sensitivity to IS Godt et al (1993) reported results showing that isometric force in permeabilized rabbit fibres was more sensitive than permeabilized lobster fibres to IS in the range 150–315 mmol l −1 produced by increasing the concentration of either potassium chloride or potassium methanesulphonate. Lobster fibres retained close to 80% of their maximal force even when IS was raised above 500 mmol l −1 with the sulphonate solution.…”

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confidence: 99%

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Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres

West¹,

Ferenczi²,

Woledge³

et al. 2005

The Journal of Physiology

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We measured the effects of ionic strength (IS), 200 (standard) and 400 mmol l −1 (high), on force and ATP hydrolysis during isometric contractions of permeabilized white fibres from dogfish myotomal muscle at their physiological temperature, 12• C. One goal was to test the validity of our kinetic scheme that accounts for energy release, work production and ATP hydrolysis. Fibres were activated by flash photolysis of the P 3 -1-(2 nitrophenyl) ethyl ester of ATP (NPE-caged ATP), and time-resolved phosphate (P i ) release was detected with the fluorescent protein MDCC-PBP, N -(2[1-maleimidyl]ethyl)-7-diethylamino-coumarin-3-carboxamide phosphate binding protein. High IS slowed the transition from rest to contraction, but as the fibres approached the isometric force plateau they showed little IS sensitivity. By 0.5 s of contraction, the force and the rate of P i release at standard and high IS values were not significantly different. A five-step reaction mechanism was used to account for the observed time courses of force and P i release in all conditions explored here. Only the rate constants for reactions of ATP, ADP and P i with the contractile proteins varied with IS, thus suggesting that the actin-myosin interactions are largely non-ionic. Our reaction scheme also fits previous results for intact fibres.

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Section: Discussioncontrasting

confidence: 59%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres

West¹,

Ferenczi²,

Woledge³

et al. 2005

The Journal of Physiology

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Osmolytes and Cell‐Volume Regulation: Physiological and Evolutionary Principles

Somero

Yancey

1997

Comprehensive Physiology

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The sections in this article are: What Makes a Solute an Osmolyte? The Basic Osmoregulatory Response: Conservation Paired with Change Osmolyte Taxonomy: Evolutionary Convergence and Conservation The Discovery of Organic Osmolytes Polyols and Sugars Free Amino Acids and Their Derivatives Methylated Ammonium and Sulfonium Compounds Urea and Urea with Methylamines Osmolyte Effects: Perturbation, Stabilization, and Compatibility Changes in Concentrations of Inorganic Ions Are Generally Perturbing of Biochemical Systems Organic Osmolyte Compatibility with Biochemical Functions In Vitro Organic Osmolyte Compatibility with Protein Structure In Vitro Compatibility of Organic Osmolytes: In Vivo and Cell Culture Studies Organic Osmolyte Effects: Counteracting Solute Systems Counteracting Solute Effects In Vitro Urea Counteraction in Living Systems Salt Counteraction (Haloprotection) Exceptions to Counteraction Regulation of Osmolyte Concentrations Interspecific Similarities in Basic Regulatory Strategies Osmolyte Regulation in Bacteria and Plants Osmolyte Regulation in Invertebrates Osmolyte Regulation in Lower Vertebrates The Mammalian Kidney Stress Protein Induction in Hyperosmotic Stress Mechanisms of Solute Effects—and Non‐Effects The Hofmeister Series and Organic Osmolyte Structures Preferential Exclusion of Compatible Osmolytes from the Protein Surface Solute Interactions with Ligands in Solution Nonreactivity of Modified Amino Acid Osmolytes Monosaccharide Reactivity with Proteins Favorable Effects of Compatible Solutes Not Related to Osmoregulation Inorganic Ions: Perturbation and Compatibility Evolutionary Perspectives Macromolecular vs. “Micromolecular” Evolution Evolution of Osmolyte Molecules: An Overview of Principles of Selection Summary: The Adaptive Significance of Osmolyte System Evolution

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Intracellular sodium homeostasis in relation to the effective free-energy change of ATP hydrolysis: studies of crayfish muscle fibers

Combs¹,

Ellington²

1997

Journal of Comparative Physiology B: Biochemical, Systemic, and

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Influence of Ionic Strength on Contractile Force and Energy Consumption of Skinned Fibers From Mammalian and Crustacean Striated Muscle

Cited by 7 publications

References 29 publications

Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres

Influence of ionic strength on the time course of force development and phosphate release by dogfish muscle fibres

Osmolytes and Cell‐Volume Regulation: Physiological and Evolutionary Principles

Intracellular sodium homeostasis in relation to the effective free-energy change of ATP hydrolysis: studies of crayfish muscle fibers

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