ArticleThe Journal of general physiology2013
Effect of muscle length on cross-bridge kinetics in intact cardiac trabeculae at body temperature.
Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Reduced preload increases Mechanical Control (strain-rate dependence) of Relaxation by modifying myosin kinetics.Archives of biochemistry and biophysics · 2021Article
- Contraction-relaxation coupling is unaltered by exercise training and infarction in isolated canine myocardium.The Journal of general physiology · 2021Article
- Impact of etiology on force and kinetics of left ventricular end-stage failing human myocardium.Journal of molecular and cellular cardiology · 2021Article
- Myosin cross-bridge kinetics slow at longer muscle lengths during isometric contractions in intact soleus from mice.Proceedings. Biological sciences · 2021Article
- Impact of heart rate on cross-bridge cycling kinetics in failing and nonfailing human myocardium.American journal of physiology. Heart and circulatory physiology · 2019Article
- Omecamtiv Mecarbil Slows Myosin Kinetics in Skinned Rat Myocardium at Physiological Temperature.Biophysical journal · 2019Article
- Lost in translation: Interpreting cardiac muscle mechanics data in clinical practice.Archives of biochemistry and biophysics · 2019Review
- Myocardial relaxation in human heart failure: Why sarcomere kinetics should be center-stage.Archives of biochemistry and biophysics · 2019Review
- Increased cross-bridge recruitment contributes to transient increase in force generation beyond maximal capacity in human myocardium.Journal of molecular and cellular cardiology · 2018Article
- I-Wire Heart-on-a-Chip II: Biomechanical analysis of contractile, three-dimensional cardiomyocyte tissue constructs.Acta biomaterialia · 2017Article
- Length-Dependent Prolongation of Force Relaxation Is Unaltered by Delay of Intracellular Calcium Decline in Early-Stage Rabbit Right Ventricular Hypertrophy.Frontiers in physiology · 2017Article
- Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion.The Journal of physiology · 2016Article
- Insights into length-dependent regulation of cardiac cross-bridge cycling kinetics in human myocardium.Archives of biochemistry and biophysics · 2016Article
- Rabbit models of cardiac mechano-electric and mechano-mechanical coupling.Progress in biophysics and molecular biology · 2016Review
- Molecule specific effects of PKA-mediated phosphorylation on rat isolated heart and cardiac myofibrillar function.Archives of biochemistry and biophysics · 2016Article
- Influence of metabolic dysfunction on cardiac mechanics in decompensated hypertrophy and heart failure.Journal of molecular and cellular cardiology · 2016Article
- Effect of exercise training and myocardial infarction on force development and contractile kinetics in isolated canine myocardium.Journal of applied physiology (Bethesda, Md. : 1985) · 2016Article
- Cardiac muscle mechanics: Sarcomere length matters.Journal of molecular and cellular cardiology · 2016Article
- Myocardial Contractile Dysfunction Is Present without Histopathology in a Mouse Model of Limb-Girdle Muscular Dystrophy-2F and Is Prevented after Claudin-5 Virotherapy.Frontiers in physiology · 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
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5 authors.
Funding
Abstract
Dynamic force generation in cardiac muscle, which determines cardiac pumping activity, depends on both the number of sarcomeric cross-bridges and on their cycling kinetics. The Frank-Starling mechanism dictates that cardiac force development increases with increasing cardiac muscle length (corresponding to increased ventricular volume). It is, however, unclear to what extent this increase in cardiac muscle length affects the rate of cross-bridge cycling. Previous studies using permeabilized cardiac preparations, sub-physiological temperatures, or both have obtained conflicting results. Here, we developed a protocol that allowed us to reliably and reproducibly measure the rate of tension redevelopment (k(tr); which depends on the rate of cross-bridge cycling) in intact trabeculae at body temperature. Using K(+) contractures to induce a tonic level of force, we showed the k(tr) was slower in rabbit muscle (which contains predominantly β myosin) than in rat muscle (which contains predominantly α myosin). Analyses of k(tr) in rat muscle at optimal length (L(opt)) and 90% of optimal length (L(90)) revealed that k(tr) was significantly slower at L(opt) (27.7 ± 3.3 and 27.8 ± 3.0 s(-1) in duplicate analyses) than at L(90) (45.1 ± 7.6 and 47.5 ± 9.2 s(-1)). We therefore show that k(tr) can be measured in intact rat and rabbit cardiac trabeculae, and that the k(tr) decreases when muscles are stretched to their optimal length under near-physiological conditions, indicating that the Frank-Starling mechanism not only increases force but also affects cross-bridge cycling kinetics.
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