Contractile responses to temperature in the locomotory musculature of striped bass <i>Morone saxatilis</i>

Moerland, Timothy S.; Sidell, Bruce D.

doi:10.1002/jez.1402400105

Cited by 8 publications

(5 citation statements)

References 21 publications

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“…T t depends not only on the experimental conditions but also on whether Ca 2+ -regulatory proteins are present. The Arrhenius plot of fish myofibrillar ATPase at saturating Ca 2+ exhibited a discontinuity [ 68 ], while this was not the case for in vitro motility sliding speed and actin-activated MgATPase activity with fish myosin and unregulated F-actin [ 69 ]. For regulated thin filaments, Homsher et al [ 16 ] reported a break in the Arrhenius plot around 12.5°C that was not observed for unregulated F-actin within the 7–25°C temperature range.…”

Section: Discussionmentioning

confidence: 99%

Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Brunet

Mihajlović

Aledealat

et al. 2012

Journal of Biomedicine and Biotechnology

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Microfabricated thermoelectric controllers can be employed to investigate mechanisms underlying myosin-driven sliding of Ca2+-regulated actin and disease-associated mutations in myofilament proteins. Specifically, we examined actin filament sliding—with or without human cardiac troponin (Tn) and α-tropomyosin (Tm)—propelled by rabbit skeletal heavy meromyosin, when temperature was varied continuously over a wide range (∼20–63°C). At the upper end of this temperature range, reversible dysregulation of thin filaments occurred at pCa 9 and 5; actomyosin function was unaffected. Tn-Tm enhanced sliding speed at pCa 5 and increased a transition temperature (Tt) between a high activation energy (Ea) but low temperature regime and a low Ea but high temperature regime. This was modulated by factors that alter cross-bridge number and kinetics. Three familial hypertrophic cardiomyopathy (FHC) mutations, cTnI R145G, cTnI K206Q, and cTnT R278C, cause dysregulation at temperatures ∼5–8°C lower; the latter two increased speed at pCa 5 at all temperatures.

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Section: Discussionmentioning

confidence: 99%

Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Brunet

Mihajlović

Aledealat

et al. 2012

Journal of Biomedicine and Biotechnology

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“…The Arrhenius plot is well fit by a single, least-squares, linear skinned, fast-twitch fibers from the bulltrout (Johnston and Sidell, 1984), but approximately 30% greater than observed Normalized Force (% o Vi) for fast-twitch fibers from a different teleost, the striped bass (Moerland and Sidell, 1986). We note that there is a downiortening velocity at varying [Vi] (10 puM-1 mM) normal-ward concavity in the present data for temperatures <150C St to that obtained in the absence of Vi versus normalized (lower temperatures to right of Fig.…”

Section: C Omentioning

confidence: 90%

Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle

Pate¹,

Wilson²,

Bhimani³

et al. 1994

Biophysical Journal

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We have investigated the effects of the orthophosphate (P(i)) analog orthovanadate (Vi) on maximum shortening velocity (Vmax) in activated, chemically skinned, vertebrate skeletal muscle fibers. Using new "temperature-jump" protocols, reproducible data can be obtained from activated fibers at high temperatures, and we have examined the effect of increased [Vi] on Vmax for temperatures in the range 5-30 degrees C. We find that for temperatures < or = 20 degrees C, increasing [Vi] inhibits Vmax; for temperatures > or = 25 degrees C, increasing [Vi] does not inhibit Vmax. Attached cross-bridges bound to Vi are thought to be an analog of the weakly bound actin-myosin.ADP-P(i) state. The data suggest that the weakly bound Vi state can inhibit velocity at low temperature, but not at high temperature, with the transition occurring over a narrow temperature range of < 5 degrees C. This suggests a highly cooperative interaction. The data also define a Q10 for Vmax of 2.1 for chemically skinned rabbit psoas fibers over the temperature range of 5-30 degrees C.

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“…Furthermore, physiologically relevant variations in viscosity likely influence motility of ectotherms. In particular, certain species of fish may experience significant changes in temperature, with concomitant changes in cytoplasmic viscosity (see above) and thus changes in the speed and energy requirements for swimming (Moerland and Sidell, 1986).…”

Section: Shortening Velocitymentioning

confidence: 99%

Effect of Viscosity on Mechanics of Single, Skinned Fibers from Rabbit Psoas Muscle

Chase

Denkinger²,

Kushmerick

1998

Biophysical Journal

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Muscle contraction is highly dynamic and thus may be influenced by viscosity of the medium surrounding the myofilaments. Single, skinned fibers from rabbit psoas muscle were used to test this hypothesis. Viscosity within the myofilament lattice was increased by adding to solutions low molecular weight sugars (disaccharides sucrose or maltose or monosaccharides glucose or fructose). At maximal Ca2+ activation, isometric force (Fi) was inhibited at the highest solute concentrations studied, but this inhibition was not directly related to viscosity. Solutes readily permeated the filament lattice, as fiber diameter was unaffected by added solutes (except for an increased diameter with Fi < 30% of control). In contrast, there was a linear dependence upon 1/viscosity for both unloaded shortening velocity and also the kinetics of isometric tension redevelopment; these effects were unrelated to either variation in solution osmolarity or inhibition of force. All effects of added solute were reversible. Inhibition of both isometric as well as isotonic kinetics demonstrates that viscous resistance to filament sliding was not the predominant factor affected by viscosity. This was corroborated by measurements in relaxed fibers, which showed no significant change in the strain-rate dependence of elastic modulus when viscosity was increased more than twofold. Our results implicate cross-bridge diffusion as a significant limiting factor in cross-bridge kinetics and, more generally, demonstrate that viscosity is a useful probe of actomyosin dynamics.

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Contractile responses to temperature in the locomotory musculature of striped bass Morone saxatilis

Cited by 8 publications

References 21 publications

Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle

Effect of Viscosity on Mechanics of Single, Skinned Fibers from Rabbit Psoas Muscle

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Contractile responses to temperature in the locomotory musculature of striped bass Morone saxatilis

Cited by 8 publications

References 21 publications

Micromechanical Thermal Assays of Ca2+-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Micromechanical Thermal Assays of Ca2+-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle

Effect of Viscosity on Mechanics of Single, Skinned Fibers from Rabbit Psoas Muscle

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Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin

Micromechanical Thermal Assays of Ca²⁺-Regulated Thin-Filament Function and Modulation by Hypertrophic Cardiomyopathy Mutants of Human Cardiac Troponin