ArticleThe Journal of physiology2004
The effect of tropomyosin on force and elementary steps of the cross-bridge cycle in reconstituted bovine myocardium.
Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- Assessing Cardiac Contractility From Single Molecules to Whole Hearts.JACC. Basic to translational science · 2024Review
- Molecular Mechanisms of the Deregulation of Muscle Contraction Induced by the R90P Mutation in Tpm3.12 and the Weakening of This Effect by BDM and W7.International journal of molecular sciences · 2021Article
- The effects of inorganic phosphate on muscle force development and energetics: challenges in modelling related to experimental uncertainties.Journal of muscle research and cell motility · 2021Article
- Molecular Mechanisms of Muscle Weakness Associated with E173A Mutation in Tpm3.12. Troponin CaInternational journal of molecular sciences · 2020Article
- The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.International journal of molecular sciences · 2018Article
- Article
- Impact of tropomyosin isoform composition on fast skeletal muscle thin filament regulation and force development.Journal of muscle research and cell motility · 2015Article
- Using baculovirus/insect cell expressed recombinant actin to study the molecular pathogenesis of HCM caused by actin mutation A331P.Journal of molecular and cellular cardiology · 2014Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Analysis of the molecular pathogenesis of cardiomyopathy-causing cTnT mutants I79N, ΔE96, and ΔK210.Biophysical journal · 2013Article
- Article
- Thin filament-reconstituted skinned muscle fibers for the study of muscle physiology.Journal of biomedicine & biotechnology · 2011Review
- The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.Journal of muscle research and cell motility · 2010Article
- Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2009Article
- Temperature change does not affect force between regulated actin filaments and heavy meromyosin in single-molecule experiments.The Journal of physiology · 2006Article
- Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation.Journal of muscle research and cell motility · 2006Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The role of tropomyosin (Tm) in the elementary steps of the cross-bridge cycle in bovine myocardium was investigated. The thin filament was selectively removed using gelsolin (thin filament severing protein), and the actin filament was reconstituted from G-actin. Tm was further reconstituted without troponin (Tn), and the kinetic constants of the elementary steps of the cross-bridge cycle were deduced using sinusoidal analysis at pCa </= 4.66, pH 7.00, and 25 degrees C. The association constant of MgATP to cross-bridges (K(1)) after reconstitution of Tm was 20.7 +/- 2.3 mm(-1), which was about 2 x the control (untreated) myocardium (9.1 +/- 1.3 mm(-1)). Following reconstitution of Tm, the equilibrium constant of the cross-bridge detachment step (K(2)), the phosphate (P(i)) association constant (K(5)) and the equilibrium constant of the force-generation step (K(4)), which significantly changed in the actin filament-reconstituted myocardium, recovered to those of the control myocardium. Active tension after reconstitution of Tm was 0.69 x the control myocardium, a value between the control (1.00 x) and the actin filament-reconstituted myocardium (0.59 x). Tm-reconstituted myocardium was further reconstituted with Tn, and the effect of MgATP on the rate constants (K(1), K(2)) was studied. Following reconstitution with Tn, the myocardium regained the Ca(2+)-sensitivity and the active tension became 0.83 x the control myocardium. In addition, K(1) recovered to the value of the control myocardium with Tn reconstitution. These results indicate that both Tm and Tn enhance the force generated by each cross-bridge, and that Tm is primarily responsible for the change in the kinetic constants of the elementary steps of the cross-bridge cycle.
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