ArticleThe Journal of physiology2000
Ca2+ dependence of loaded shortening in rat skinned cardiac myocytes and skeletal muscle fibres.
Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Pulsatile Myofilament Activity in Myotrem Myopathy Associated with Myogenic Tremor.International journal of molecular sciences · 2025Article
- Myosin binding protein-C modulates loaded sarcomere shortening in rodent permeabilized cardiac myocytes.The Journal of general physiology · 2025Article
- PPP1R12C Promotes Atrial Hypocontractility in Atrial Fibrillation.Circulation research · 2023Article
- Thin filament regulation of cardiac muscle power output: Implications for targets to improve human failing hearts.The Journal of general physiology · 2023Article
- Molecular regulation of stretch activation.American journal of physiology. Cell physiology · 2022Article
- Article
- Cardiac MyBP-C phosphorylation regulates the Frank-Starling relationship in murine hearts.The Journal of general physiology · 2021Article
- CaAmerican journal of physiology. Cell physiology · 2020Article
- Regulation of Myofilament Contractile Function in Human Donor and Failing Hearts.Frontiers in physiology · 2020Article
- What a drag!: Skeletal myosin binding protein-C affects sarcomeric shortening.The Journal of general physiology · 2019Article
- Regulation of myofilament force and loaded shortening by skeletal myosin binding protein C.The Journal of general physiology · 2019Article
- Regulating myofilament power: The determinant of health.Archives of biochemistry and biophysics · 2019Review
- Lost in translation: Interpreting cardiac muscle mechanics data in clinical practice.Archives of biochemistry and biophysics · 2019Review
- Force-Clamp Rheometry for Characterizing Protein-based Hydrogels.Journal of visualized experiments : JoVE · 2018Article
- Point mutations in the tri-helix bundle of the M-domain of cardiac myosin binding protein-C influence systolic duration and delay cardiac relaxation.Journal of molecular and cellular cardiology · 2018Article
- Age-related reduction in single muscle fiber calcium sensitivity is associated with decreased muscle power in men and women.Experimental gerontology · 2018Article
- The contractile adaption to preload depends on the amount of afterload.ESC heart failure · 2017Article
- Cardiac myofibrillar contractile properties during the progression from hypertension to decompensated heart failure.American journal of physiology. Heart and circulatory physiology · 2017Article
- Molecule specific effects of PKA-mediated phosphorylation on rat isolated heart and cardiac myofibrillar function.Archives of biochemistry and biophysics · 2016Article
- Elevated Ca2+ transients and increased myofibrillar power generation cause cardiac hypercontractility in a model of Noonan syndrome with multiple lentigines.American journal of physiology. Heart and circulatory physiology · 2015Article
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1 author.
Funding
Abstract
This study examined the effects of activator Ca2+ on loaded shortening and power output in skinned rat cardiac myocyte preparations, and fast- and slow-twitch skeletal muscle fibres at 12 degrees C. Shortening velocities were slowed at nearly all relative loads when Ca2+ activation levels were reduced to approximately 70% maximal isometric force (P4.5) in cardiac myocyte preparations, as well as in fast-twitch and slow-twitch skeletal muscle fibres. Peak absolute power outputs declined significantly as Ca2+ activation levels were progressively reduced from maximal to 30% P4.5 in all three striated muscle types, with the greatest change in fast-twitch fibres. In cardiac myocyte preparations, even peak relative power output progressively fell when Ca2+ activation levels were lowered to approximately 70, 50 and 30% P4.5. Peak relative power output also progressively fell in fast-twitch fibres as Ca2+ activation levels were lowered from maximal down to 50% P4.5. However, in slow-twitch fibres, peak relative power output decreased only at 70% P4.5 and then remained unchanged with further reductions in Ca2+ activation levels. The greater Ca2+ dependence of peak relative power output in cardiac myocytes and fast-twitch fibres may arise from a shared mechanism such as cooperative inactivation of the thin filament, which is likely to be slowest in less cooperative slow-twitch fibres. During submaximal Ca2+ activations, the time course of shortening became markedly curvilinear during isotonic shortening in all three muscle types. The progressive slowdown in shortening velocity during isotonic contractions was greatest in fast-twitch fibres, consistent with the higher degree of cooperativity of Ca2+ activation in fast-twitch fibres. Additionally, fast-twitch and slow-twitch fibre stiffness decreased in concert with the curvature of length traces during loaded shortening. These results are consistent with the idea that cooperative inactivation of the thin filament occurs during loaded shortening and such a mechanism may contribute to the progressive slowing and overall Ca2+ dependence of loaded shortening velocity.
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