ArticleBiophysical journal2009
Cooperative cross-bridge activation of thin filaments contributes to the Frank-Starling mechanism in cardiac muscle.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- CaJournal of molecular and cellular cardiology · 2025Article
- Myosin-actin crossbridge independent sarcomere length induced CaJournal of molecular and cellular cardiology · 2025Article
- Danicamtiv affected isometric force and cross-bridge kinetics similarly in skinned myocardial strips from male and female rats.Journal of muscle research and cell motility · 2024Article
- N-terminal truncated cardiac troponin I enhances Frank-Starling response by increasing myofilament sensitivity to resting tension.The Journal of general physiology · 2023Article
- 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
- The regulatory light chain mediates inactivation of myosin motors during active shortening of cardiac muscle.Nature communications · 2021Article
- The effect of variable troponin C mutation thin filament incorporation on cardiac muscle twitch contractions.Journal of molecular and cellular cardiology · 2021Article
- Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers.Frontiers in physiology · 2020Article
- Cardiac myosin activation with 2-deoxy-ATP via increased electrostatic interactions with actin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Developmental increase in β-MHC enhances sarcomere length-dependent activation in the myocardium.The Journal of general physiology · 2019Article
- Regulatory light chain phosphorylation augments length-dependent contraction in PTU-treated rats.The Journal of general physiology · 2019Article
- Sarcomere length-dependent effects on CaThe Journal of general physiology · 2019Article
- Cardiomyopathy mutation (F88L) in troponin T abolishes length dependency of myofilament CaThe Journal of general physiology · 2018Article
- Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber CaBiophysical journal · 2017Article
- Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.eLife · 2017Article
- Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.Archives of biochemistry and biophysics · 2016Article
- The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain.Archives of biochemistry and biophysics · 2016Article
- Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm (20ΔRRM) Mice.Frontiers in physiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin cross-bridges play an important role in the regulation of thin-filament activation in cardiac muscle. To test the hypothesis that sarcomere length (SL) modulation of thin-filament activation by strong-binding cross-bridges underlies the Frank-Starling mechanism, we inhibited force and strong cross-bridge binding to intermediate levels with sodium vanadate (Vi). Force and stiffness varied proportionately with [Ca(2+)] and [Vi]. Increasing [Vi] (decreased force) reduced the pCa(50) of force-[Ca(2+)] relations at 2.3 and 2.0 microm SL, with little effect on slope (n(H)). When maximum force was inhibited to approximately 40%, the effects of SL on force were diminished at lower [Ca(2+)], whereas at higher [Ca(2+)] (pCa < 5.6) the relative influence of SL on force increased. In contrast, force inhibition to approximately 20% significantly reduced the sensitivity of force-[Ca(2+)] relations to changes in both SL and myofilament lattice spacing. Strong cross-bridge binding cooperatively induced changes in cardiac troponin C structure, as measured by dichroism of 5' iodoacetamido-tetramethylrhodamine-labeled cardiac troponin C. This apparent cooperativity was reduced at shorter SL. These data emphasize that SL and/or myofilament lattice spacing modulation of the cross-bridge component of cardiac thin-filament activation contributes to the Frank-Starling mechanism.
Indexed as
Identifiers
What OpenQuestion holds
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.