ArticleBiophysical journal2010
The role of thin filament cooperativity in cardiac length-dependent calcium activation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 52 citations in OpenAlex.
- The CabioRxiv : the preprint server for biology · 2026Article
- Piezo1 Regulates the Skeletal Muscle Length-Tension Relationship Through Channel-Independent Mechanotransduction.Biomolecules · 2026Article
- Modeling the effects of thin filament near-neighbor cooperative interactions in mammalian myocardium.The Journal of general physiology · 2025Article
- An integrated picture of the structural pathways controlling the heart performance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The carbon monoxide prodrug oCOm-21 increases CaPhysiological reports · 2024Article
- Sarcomere length affects Ca2+ sensitivity of contraction in ischemic but not non-ischemic myocardium.The Journal of general physiology · 2023Article
- Cardiac efficiency and Starling's Law of the Heart.The Journal of physiology · 2022Article
- Work-loop contractions reveal that the afterload-dependent time course of cardiac CaJournal of applied physiology (Bethesda, Md. : 1985) · 2022Article
- Mechanisms of Frank-Starling law of the heart and stretch activation in striated muscles may have a common molecular origin.Journal of muscle research and cell motility · 2021Article
- Article
- Biophysically detailed mathematical models of multiscale cardiac active mechanics.PLoS computational biology · 2020Article
- Sarcomere length-dependent effects on CaThe Journal of general physiology · 2019Article
- Functional significance of C-terminal mobile domain of cardiac troponin I.Archives of biochemistry and biophysics · 2017Article
- The contractile adaption to preload depends on the amount of afterload.ESC heart failure · 2017Article
- The Frank-Starling Law: a jigsaw of titin proportions.Biophysical reviews · 2017Review
- Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin- and thick-filament proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Historical perspective on heart function: the Frank-Starling Law.Biophysical reviews · 2015Review
- Rapid large-scale purification of myofilament proteins using a cleavable His6-tag.American journal of physiology. Heart and circulatory physiology · 2015Article
- A Spatially Detailed Model of Isometric Contraction Based on Competitive Binding of Troponin I Explains Cooperative Interactions between Tropomyosin and Crossbridges.PLoS computational biology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Length-dependent activation (LDA) is a prominent feature of cardiac muscle characterized by decreases in the Ca(2+) levels required to generate force (i.e., increases in Ca(2+) sensitivity) when muscle is stretched. Previous studies have concluded that LDA originates from the increased ability of (strong) cross-bridges to attach when muscle is lengthened, which in turn enhances Ca(2+) binding to the troponin C (TnC) subunit of the troponin complex. However, our results demonstrate that inhibition of strong cross-bridge attachment with blebbistatin had no effect on the length-dependent modulation of Ca(2+) sensitivity (i.e., EC(50)) or Ca(2+) cooperativity, suggesting that LDA originates upstream of cross-bridge attachment. To test whether LDA arises from length dependence of thin-filament activation, we replaced native cTnC with a mutant cTnC (DM-TnC) that is incapable of binding Ca(2+). Although progressive replacement of native cTnC with DM-TnC caused an expected monotonic decrease in the maximal force (F(max)), DM-TnC incorporation induced much larger increases in EC(50) and decreases in Ca(2+) cooperativity at short lengths than at long lengths. These findings support the conclusion that LDA arises primarily from the influence of length on the modulation of the Ca(2+) cooperativity arising from interaction between adjacent troponin-tropomyosin complexes on the thin filament.
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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.