ArticleIntegrative and comparative biology2018
A Spatially Explicit Model Shows How Titin Stiffness Modulates Muscle Mechanics and Energetics.
Article in Integrative and comparative biology, 2018. 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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17 citing papers in PubMed, 32 citations in OpenAlex.
- The E525K β-Myosin Mutation Causes Hypocontractility in Cardiomyocytes Without Altering Loaded Crossbridge Cycling.bioRxiv : the preprint server for biology · 2026Article
- Nanometer scale difference in myofilament lattice structure of muscle alters muscle function in a spatially explicit model.PLoS computational biology · 2025Article
- Bayesian estimation of muscle mechanisms and therapeutic targets using variational autoencoders.Biophysical journal · 2025Article
- Bayesian Estimation of Muscle Mechanisms and Therapeutic Targets Using Variational Autoencoders.bioRxiv : the preprint server for biology · 2024Article
- A novel kinetic model to demonstrate the independent effects of ATP and ADP/Pi concentrations on sarcomere function.PLoS computational biology · 2024Article
- Design Principles and Benefits of Spatially Explicit Models of Myofilament Function.Methods in molecular biology (Clifton, N.J.) · 2024Article
- AnBioMed research international · 2024Article
- Machine learning meets Monte Carlo methods for models of muscle's molecular machinery to classify mutations.The Journal of general physiology · 2023Article
- dATP elevation induces myocardial metabolic remodeling to support improved cardiac function.Journal of molecular and cellular cardiology · 2023Article
- Subcellular Remodeling in Filamin C Deficient Mouse Hearts Impairs Myocyte Tension Development during Progression of Dilated Cardiomyopathy.International journal of molecular sciences · 2022Article
- A mechanism for sarcomere breathing: volume change and advective flow within the myofilament lattice.Biophysical journal · 2021Article
- Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Time of Day and Muscle Strength: A Circadian Output?Physiology (Bethesda, Md.) · 2021Article
- Article
- Growing Old Too Early: Skeletal Muscle Single Fiber Biomechanics in Ageing R349P Desmin Knock-in Mice Using theInternational journal of molecular sciences · 2020Article
- Nanometer-scale structure differences in the myofilament lattice spacing of two cockroach leg muscles correspond to their different functions.The Journal of experimental biology · 2020Article
- Nebulin and titin modulate cross-bridge cycling and length-dependent calcium sensitivity.The Journal of general physiology · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In striated muscle, the giant protein titin spans the entire length of a half-sarcomere and extends from the backbone of the thick filament, reversibly attaches to the thin filaments, and anchors to the dense protein network of the z-disk capping the end of the half-sarcomere. However, little is known about the relationship between the basic mechanical properties of titin and muscle contractility. Here, we build upon our previous multi-filament, spatially explicit computational model of the half-sarcomere by incorporating the nonlinear mechanics of titin filaments in the I-band. We vary parameters of the nonlinearity to understand the effects of titin stiffness on contraction dynamics and efficiency. We do so by simulating isometric contraction for a range of sarcomere lengths (SLs; 1.6-3.25 µm). Intermediate values of titin stiffness accurately reproduce the passive force-SL relation for skeletal muscle. The maximum force-SL relation is not affected by titin for SL≤2.5 µm. However, as titin stiffness increases, maximum force for the four thick filament system at SL = 3.0 µm significantly decreases from 103.2 ± 2 to 58.8 ± 1 pN. Additionally, by monitoring ATP consumption, we measure contraction efficiency as a function of titin stiffness. We find that at SL = 3.0 µm, efficiency significantly decreases from 13.9 ± 0.4 to 7.0 ± 0.3 pN/ATP when increasing titin stiffness, with little or no effect below 2.5 µm. Taken together, our results suggest that, despite an increase in the fraction of motors bound to actin along the descending limb when titin is stiffer, the force-generating capacity of the motors is reduced. These results suggest that titin stiffness has the potential to affect contractile efficiency.
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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.