The kinetics of muscle contraction

White, D. C. S.; Thorson, John

doi:10.1016/0079-6107(73)90007-2

Cited by 92 publications

(67 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this study we model the sarcomere using a ladder structure for the overlap zone and an additional elasticity for the non-overlap zone. This model is similar to the structures proposed by White and Thorson (1973) and Ford and colleagues (1981) (Fig. 1).…”

Section: Methodssupporting

confidence: 89%

See 1 more Smart Citation

Untitled

Blangé

Heide

Treijtel

et al. 1997

Journal of Muscle Research and Cell Motility

View full text Add to dashboard Cite

The effect of actin filament compliance on the interpretation of the elastic properties of skeletal muscle fibres Blange, T.; van der Heide, U.A.; Treijtel, B.W.; de Beer, E.L. Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. SummaryRecently, X-ray diffraction studies provided direct evidence for an appreciable length change in the actin filament upon activation. This finding has profound implications on the interpretation of the elastic properties of skeletal muscle fibre.In this study we determined the compliance of the actin filament during activation, using the data obtained previously from quick stretch and release experiments on skeletal muscle fibres of the frog. The effects of filament compliance are demonstrated clearly in the elastic properties of partially activated fibres. The low-frequency elasticity increases linearly with tension, reflecting an increase in the number of force-producing cross-bridges. At higher frequencies, this linearity is lost. In this study we describe the data consistently in terms of a cross-bridge stiffness increasing linearly with tension and a constant Young's modulus for the actin filament of 44 MN m per kN m ÿ 2 tension developed. Using this value for the actin filament Young's modulus, its contribution to the elastic properties of skeletal muscle fibre of the frog is considered in rigor and relaxation. The filament compliance hardly affects the overall elasticity of the musle fibre in relaxation. In contrast, it contributes to a large extent to the overall elasticity in rigor. Taking account of the filament compliance, we find that the Young's modulus in rigor exhibits an increase from 14 MN m ÿ 2 at frequencies below 500 Hz to 55 MN m ÿ 2 above 40 kHz.

show abstract

Section: Methodssupporting

confidence: 89%

“…Here, we analysed the data in terms of a compliance of the actin filament and cross-bridge compliance, using a ladder structure to model the overlap zone of the sarcomere (A-band) similar to the structures proposed by White and Thorson (1973) and Ford and colleagues (1981) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Untitled

Blangé

Heide

Treijtel

et al. 1997

Journal of Muscle Research and Cell Motility

View full text Add to dashboard Cite

show abstract

“…The IFM are fibrillar muscles specialized for asynchronous cycles of contractions that operate at a higher frequency than the firing rate of their motor neurons (White and Thorson, 1974). They have the property of being activated by stretch in the presence of Ca +.…”

Section: Introductionmentioning

confidence: 99%

Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation.

Prado

Canal

Barbas

et al. 1995

MBoC

View full text Add to dashboard Cite

To identify proteins that interact in vivo with muscle components we have used a genetic approach based on the isolation of suppressors of mutant alleles of known muscle components. We have applied this system to the case of troponin I (TnI) in Drosophila and its mutant allele heldup2 (hdp2). This mutation causes an alanine to valine substitution at position 116 after a single nucleotide change in a constitutive exon. Among the isolated suppressors, one of them results from a second site mutation at the TnI gene itself. Muscles endowed with TnI mutated at both sites support nearly normal myofibrillar structure, perform notably well in wing beating and flight tests, and isolated muscle fibers produce active force. We show that the structural and functional recovery in this suppressor does not result from a change in the stoichiometric ratio of TnI isoforms. The second site suppression is due to a leucine to phenylalanine change within a heptameric leucine string motif adjacent to the actin binding domain of TnI. These data evidence a structural and functional role for the heptameric leucine string that is most noticeable, if not specific, in the indirect flight muscle. INTRODUCTIONThe regulation of contraction in striated muscle occurs by mechanisms that are remarkably similar throughout the animal kingdom. Nerve input results in the

show abstract

“…We implemented the sinusoidal analysis method (Kawai and Brandt 1980), which changes the muscle length in sinewaves of varying frequency (0.13-700 Hz); historically, this method was used by Pringle's group on insect flight muscles (Pringle 1967;White and Thorson 1974). The amplitude of the length change is small (0.125% L 0 ), which corresponds to 1.25 nm per half sarcomere when the sarcomere length is 2 μm.…”

Section: Methods Of Studying Cross-bridge Kineticsmentioning

confidence: 99%

“…These methods require many cross-bridge cycles, hence the slowest step (rate limiting step) influences the measured parameters most significantly. These methods are comparable to the ATP hydrolysis rate measurement, because its rate is also limited by the slowest step in the cross-bridge cycle (Zhao and Kawai 1994a).We implemented the sinusoidal analysis method (Kawai and Brandt 1980), which changes the muscle length in sinewaves of varying frequency (0.13-700 Hz); historically, this method was used by Pringle's group on insect flight muscles (Pringle 1967;White and Thorson 1974). The amplitude of the length change is small (0.125% L 0 ), which corresponds to 1.25 nm per half sarcomere when the sarcomere length is 2 μm.…”

mentioning

confidence: 99%

Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation

Kawai

Ishiwata

2006

J Muscle Res Cell Motil

View full text Add to dashboard Cite

The technique of selective removal of the thin filament by gelsolin in bovine cardiac muscle fibres, and reconstitution of the thin filament from isolated proteins is reviewed, and papers that used reconstituted preparations are discussed. By comparing the results obtained in the absence/presence of regulatory proteins tropomyosin (Tm) and troponin (Tn), it is concluded that the role of Tm and Tn in force generation is not only to expose the binding site of actin to myosin, but also to modify actin for better stereospecific and hydrophobic interaction with myosin. This conclusion is further supported by experiments that used a truncated Tm mutant and the temperature study of reconstituted fibres. The conclusion is consistent with the hypothesis that there are three states in the thin filament: blocked state, closed state, and open state. Tm is the major player to produce these effects, with Tn playing the role of Ca 2+ sensing and signal transmission mechanism. Experiments that changed the number of negative charges at the N-terminal finger of actin demonstrates that this part of actin is essential to promote the strong interaction between actin and myosin molecules, in addition to the well-known weak interaction that positions the myosin head at the active site of actin prior to force generation. KeywordsActin; Regulatory proteins; Tropomyosin; Troponin; Myosin; Gelsolin; Cross-bridge kinetics; Sinusoidal analysis; BDM Thin filament reconstituted muscle fibre systemFor the purpose of understanding the cross-bridge interaction with actin and the role of regulatory proteins in this interaction, we reconstituted the thin filament in cardiac muscle fibres. This method is schematically represented in Fig. 1. The thin filament is first removed by gelsolin (Fig. 1A to 1B), followed by sequential reconstitution with G-actin (Fig. 1C), and regulatory proteins, tropomyosin (Tm) and troponin (Tn) (Fig. 1D). Gelsolin is an actin and thin filament severing protein, hence its action is specific and it does not disrupt other sarcomeric structure. However, overtreatment with gelsolin would disrupt the Z-line structure, because actin is one of the main constituents in the Z-line. The thin filament reconstitution method was initially developed at Ishiwata's laboratory and the key properties of the Correspondence to: Masataka Kawai, masataka-kawai@uiowa.edu. reconstituted fibres, such as the recovery of isometric tension, the tension-pCa relationship, and the function of spontaneous oscillatory contraction, were examined on skeletal fibres (Funatsu et al. 1994), followed by cardiac fibres (Fujita et al. 1996; Ishiwata 1998, 1999; for brief review see Ishiwata et al. 1998). In these works, it was demonstrated that bovine cardiac fibres were successful as the reconstituted system, in which actin, Tm and Tn can be replaced with those prepared from other muscles, for example, rabbit skeletal muscle proteins (Fujita et al. 1996;Fujita and Ishiwata 1999). The reconstitution method in cardiac fibres was successfully applied at ...

show abstract

The kinetics of muscle contraction

Cited by 92 publications

References 78 publications

Untitled

Untitled

Functional recovery of troponin I in a Drosophila heldup mutant after a second site mutation.

Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation

Contact Info

Product

Resources

About