ArticleThe Journal of physiology2002
Length-dependent activation in three striated muscle types of the rat.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Finite Element Model of the Shoulder with Active Rotator Cuff Muscles: Application to Wheelchair Propulsion.Annals of biomedical engineering · 2024Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Striated muscle proteins are regulated both by mechanical deformation and by chemical post-translational modification.Biophysical reviews · 2021Review
- Frozen/thawed meat quality associated with muscle fiber characteristics of porcine longissimus thoracis et lumborum, psoas major, semimembranosus, and semitendinosus muscles.Scientific reports · 2021Article
- Myosin cross-bridge kinetics slow at longer muscle lengths during isometric contractions in intact soleus from mice.Proceedings. Biological sciences · 2021Article
- Analysis of decay kinetics of the cytosolic calcium transient induced by oxytocin in rat myometrium smooth muscle cells.Journal of muscle research and cell motility · 2021Article
- Pork Loin Chop Quality and Muscle Fiber Characteristics as Affected by the Direction of Cut.Foods (Basel, Switzerland) · 2020Article
- Article
- Strategies for targeting the cardiac sarcomere: avenues for novel drug discovery.Expert opinion on drug discovery · 2020Review
- Effect of myofibril passive elastic properties on the mechanical communication between motor proteins on adjacent sarcomeres.Scientific reports · 2019Article
- Developmental increase in β-MHC enhances sarcomere length-dependent activation in the myocardium.The Journal of general physiology · 2019Article
- Cardiac-specific knockout of Lmod2 results in a severe reduction in myofilament force production and rapid cardiac failure.Journal of molecular and cellular cardiology · 2018Article
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- Cardiomyopathy mutation (F88L) in troponin T abolishes length dependency of myofilament CaThe Journal of general physiology · 2018Article
- Altered myofilament structure and function in dogs with Duchenne muscular dystrophy cardiomyopathy.Journal of molecular and cellular cardiology · 2018Article
- Omecamtiv Mecarbil Abolishes Length-Mediated Increase in Guinea Pig Cardiac Myofiber CaBiophysical journal · 2017Article
- Titin-mediated thick filament activation, through a mechanosensing mechanism, introduces sarcomere-length dependencies in mathematical models of rat trabecula and whole ventricle.Scientific reports · 2017Article
- The Frank-Starling Law: a jigsaw of titin proportions.Biophysical reviews · 2017Review
4 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
The process whereby sarcomere length modulates the sensitivity of the myofilaments to Ca(2+) is termed length-dependent activation. Length-dependent activation is a property of all striated muscles, yet the relative extent of length-dependent activation between skeletal muscle and cardiac muscle is unclear. Although length-dependent activation may be greater in fast skeletal muscle (FSM) than in slow skeletal muscle (SSM), there has not been a well controlled comparison of length-dependent activation between skeletal muscle and cardiac muscle (CM). Accordingly, we measured sarcomere length-dependent properties in skinned soleus (SSM), psoas (FSM) and ventricular trabeculae (CM) of the rat under carefully controlled conditions. The free Ca(2+)-force relationship was determined at sarcomere lengths (SL) of 1.95 microm, 2.10 microm and 2.25 microm and fitted to a modified Hill equation. FSM and SSM were more sensitive to Ca(2+) than CM. Length-dependent activation was ordered as CM > FSM > SSM. Cooperativity as measured by the Hill coefficient of the Ca(2+)-force relationship was not significantly different between CM and FSM, both of which exhibited greater cooperativity than SSM. SL did not significantly alter this parameter in each muscle type. To establish whether the observed differences can be explained by alterations in interfilament spacing, we measured myofilament lattice spacing (LS) by synchrotron X-ray diffraction in relaxed, skinned muscle preparations. LS was inversely proportional to SL for each muscle type. The slope of the SL-LS relationship, however, was not significantly different between striated muscle types. We conclude that (1) length-dependent activation differs among the three types of striated muscle and (2) these differences in the length-dependent properties among the striated muscle types may not solely be explained by the differences in the response of interfilament spacing to changes in muscle length in relaxed, skinned isolated muscle preparations.
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