ArticleBiophysical journal1998
Thin filament cooperativity as a major determinant of shortening velocity in skeletal muscle fibers.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- cMyBP-C phosphorylation modulates the time-dependent slowing of unloaded shortening in murine skinned myocardium.The Journal of general physiology · 2021Article
- CaAmerican journal of physiology. Cell physiology · 2020Article
- Are Force Enhancement after Stretch and Muscle Fatigue Due to Effects of Elevated Inorganic Phosphate and Low Calcium on Cross Bridge Kinetics?Medicina (Kaunas, Lithuania) · 2020Article
- Regulating myofilament power: The determinant of health.Archives of biochemistry and biophysics · 2019Review
- The contractile adaption to preload depends on the amount of afterload.ESC heart failure · 2017Article
- Tropomyosin flexural rigidity and single ca(2+) regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy.Frontiers in physiology · 2012Article
- A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction.Biophysical journal · 2009Article
- Sarcomere length dependence of rat skinned cardiac myocyte mechanical properties: dependence on myosin heavy chain.The Journal of physiology · 2007Article
- Kinetics of force recovery following length changes in active skinned single fibres from rabbit psoas muscle: analysis and modelling of the late recovery phase.The Journal of physiology · 2006Article
- Physiological consequences of thin filament cooperativity for vertebrate striated muscle contraction: a theoretical study.Journal of muscle research and cell motility · 2006Article
- Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates.The Journal of physiology · 2005Article
- Dynamics of crossbridge-mediated activation in the heart.Journal of muscle research and cell motility · 2005Article
- Thin filament activation and unloaded shortening velocity of rabbit skinned muscle fibres.The Journal of physiology · 2003Article
- Isotonic force modulates force redevelopment rate of intact frog muscle fibres: evidence for cross-bridge induced thin filament activation.The Journal of physiology · 2002Article
- Strong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca(2+).The Journal of physiology · 2001Article
- Influence of ionic strength on the actomyosin reaction steps in contracting skeletal muscle fibers.Biophysical journal · 2000Article
- Ca2+ dependence of loaded shortening in rat skinned cardiac myocytes and skeletal muscle fibres.The Journal of physiology · 2000Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism underlying the calcium sensitivity of the velocity of shortening of skeletal muscle fibers was investigated using a multiple shortening protocol: within a single contraction, skinned rabbit psoas fibers were made to shorten repetitively under a light load by briefly stretching back to their initial length at regular intervals. At saturating [Ca2+], the initial fast shortening pattern was repeated reproducibly. At submaximal [Ca2+], the first shortening consisted of fast and slow phases, but only the slow phase was observed in later shortenings. When the fibers were held isometric after the first shortening, the velocity of the second shortening recovered with time. The recovery paralleled tension redevelopment, implying a close relationship between the velocity and the number of the preexisting force-producing cross-bridges. However, this parallelism was lost as [Ca2+] was increased. Thus, the velocity was modified in a manner consistent with the cooperative thin filament activation by strong binding cross-bridges and its modulation by calcium. The present results therefore provide evidence that the thin filament cooperativity is primarily responsible for the calcium sensitivity of velocity. The effect of inorganic phosphate to accelerate the slow phase of shortening is also explained in terms of the cooperative activation.
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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.