ArticleThe Journal of physiology2003
Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils.
Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- Multi-omics insight into cardiac myofibril remodeling in post-prandial Burmese pythons.Communications biology · 2026Article
- Assessing Cardiac Contractility From Single Molecules to Whole Hearts.JACC. Basic to translational science · 2024Review
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- The relation between sarcomere energetics and the rate of isometric tension relaxation in healthy and diseased cardiac muscle.Journal of muscle research and cell motility · 2021Article
- Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers.Frontiers in physiology · 2020Article
- The homozygous K280N troponin T mutation alters cross-bridge kinetics and energetics in human HCM.The Journal of general physiology · 2019Article
- Kinetic coupling of phosphate release, force generation and rate-limiting steps in the cross-bridge cycle.Journal of muscle research and cell motility · 2017Review
- The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.American journal of physiology. Cell physiology · 2016Article
- Impact of tropomyosin isoform composition on fast skeletal muscle thin filament regulation and force development.Journal of muscle research and cell motility · 2015Article
- Altered Tnnt3 characterizes selective weakness of fast fibers in mice overexpressing FSHD region gene 1 (FRG1).American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Journal of muscle research and cell motility · 2013Article
- Residual force enhancement in skeletal muscles: one sarcomere after the other.Journal of muscle research and cell motility · 2012Review
- Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle.Journal of molecular and cellular cardiology · 2011Article
- Mechanical and kinetic effects of shortened tropomyosin reconstituted into myofibrils.Pflugers Archiv : European journal of physiology · 2009Article
- Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrils.Biophysical journal · 2009Article
- Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.Pflugers Archiv : European journal of physiology · 2009Article
- Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle.The Journal of physiology · 2008Article
- A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility.Biophysical journal · 2008Article
- Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle.The Journal of general physiology · 2008Article
- Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres.The Journal of physiology · 2007Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The effects of the removal of fast skeletal troponin C (fsTnC) and its replacement by cardiac troponin C (cTnC) and the exchange of fast skeletal troponin (fsTn) for cardiac troponin (cTn) were measured in rabbit fast skeletal myofibrils. Electrophoretic analysis of myofibril suspensions indicated that replacement of fsTnC or exchange of fsTn with cTnC or cTn was about 90% complete in the protocols used. Mechanical measurements in single myofibrils, which were maximally activated by fast solution switching, showed that replacement of fsTnC with cTnC reduced the isometric tension, the rate of tension rise following a step increase in Ca2+ (kACT), and the rate of tension redevelopment following a quick release and restretch (kTR), but had no effect on the kinetics of the fall in tension when the concentration of inorganic phosphate (Pi) was abruptly increased (kPi(+)). These data suggest that the chimeric protein produced by cTnC replacement in fsTn alters those steps controlling the weak-to-strong crossbridge attachment transition. Inefficient signalling within the chimeric troponin may cause these changes. However, replacement of fsTn by cTn had no effect on maximal isometric tension, kACT or kTR, suggesting that these mechanics are largely determined by the isoform of the myosin molecule. Replacement of fsTn by cTn, on the other hand, shifted the pCa50 of the pCa-tension relationship from 5.70 to 6.44 and reduced the Hill coefficient from 3.3 to 1.4, suggesting that regulatory protein isoforms primarily alter Ca2+ sensitivity and the cooperativity of the force-generating mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.