ArticleThe Journal of physiology2008
Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle.
Article in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Danicamtiv Increases Myosin Recruitment and Alters Cross-Bridge Cycling in Cardiac Muscle.Circulation research · 2023Article
- 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
- New insights provided by myofibril mechanics in inherited cardiomyopathies.Conditioning medicine · 2019Article
- The CaThe Journal of physiology · 2017Article
- Effects of Cardiac Troponin I Mutation P83S on Contractile Properties and the Modulation by PKA-Mediated Phosphorylation.The journal of physical chemistry. B · 2016Article
- Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016Review
- Finally, We Can Relax: A New Generation of Muscle Models that Incorporate Sarcomere Compliance.Biophysical journal · 2016Article
- Contractile properties of developing human fetal cardiac muscle.The Journal of physiology · 2016Article
- 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
- 2-Deoxyadenosine triphosphate restores the contractile function of cardiac myofibril from adult dogs with naturally occurring dilated cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2016Article
- Troponin I Mutations R146G and R21C Alter Cardiac Troponin Function, Contractile Properties, and Modulation by Protein Kinase A (PKA)-mediated Phosphorylation.The Journal of biological chemistry · 2015Article
- The embryonic myosin R672C mutation that underlies Freeman-Sheldon syndrome impairs cross-bridge detachment and cycling in adult skeletal muscle.Human molecular genetics · 2015Article
- Impact of tropomyosin isoform composition on fast skeletal muscle thin filament regulation and force development.Journal of muscle research and cell motility · 2015Article
- 2-Deoxy adenosine triphosphate improves contraction in human end-stage heart failure.Journal of molecular and cellular cardiology · 2015Article
- PKA phosphorylation of cardiac troponin I modulates activation and relaxation kinetics of ventricular myofibrils.Biophysical journal · 2014Article
- Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.Archives of biochemistry and biophysics · 2013Article
- Contractility and kinetics of human fetal and human adult skeletal muscle.The Journal of physiology · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The influence of Ca(2+) binding properties of individual troponin versus cooperative regulatory unit interactions along thin filaments on the rate tension develops and declines was examined in demembranated rabbit psoas fibres and isolated myofibrils. Native skeletal troponin C (sTnC) was replaced with sTnC mutants having altered Ca(2+) dissociation rates (k(off)) or with mixtures of sTnC and D28A, D64A sTnC, that does not bind Ca(2+) at sites I and II (xxsTnC), to reduce near-neighbour regulatory unit (RU) interactions. At saturating Ca(2+), the rate of tension redevelopment (k(TR)) was not altered for fibres containing sTnC mutants with decreased k(off) or mixtures of sTnC:xxsTnC. We examined the influence of k(off) on maximal activation and relaxation in myofibrils because they allow rapid and large changes in [Ca(2+)]. In myofibrils with M80Q sTnC(F27W) (decreased k(off)), maximal tension, activation rate (k(ACT)), k(TR) and rates of relaxation were not altered. With I60Q sTnC(F27W) (increased k(off)), maximal tension, k(ACT) and k(TR) decreased, with no change in relaxation rates. Surprisingly, the duration of the slow phase of relaxation increased or decreased with decreased or increased k(off), respectively. For all sTnC reconstitution conditions, Ca(2+) dependence of k(TR) in fibres showed Ca(2+) sensitivity of k(TR) (pCa(50)) shifted parallel to tension and low-Ca(2+) k(TR) was elevated. Together the data suggest the Ca(2+)-dependent rate of tension development and the duration (but not rate) of relaxation can be greatly influenced by k(off) of sTnC. This influence of sTnC binding kinetics occurs primarily within individual RUs, with only minor contributions of RU interactions at low Ca(2+).
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