ArticleBiophysical journal2001
Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Understanding altered contractile properties in advanced age: insights from a systematic muscle modelling approach.Biomechanics and modeling in mechanobiology · 2023Article
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- Influence of 4 weeks of downhill running on calcium sensitivity of rat single muscle fibers.Physiological reports · 2022Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Functional and structural differences between skinned and intact muscle preparations.The Journal of general physiology · 2022Review
- The molecular basis of thin filament activation: from single molecule to muscle.Scientific reports · 2017Article
- Sex differences in stretch-dependent effects on tension and Ca(2+) transient of rat trabeculae in monocrotaline pulmonary hypertension.The journal of physiological sciences : JPS · 2015Article
- Calcium sensitivity of residual force enhancement in rabbit skinned fibers.American journal of physiology. Cell physiology · 2014Article
- In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation.Biophysical journal · 2014Article
- The constant beat: cardiomyocytes adapt their forces by equal contraction upon environmental stiffening.Biology open · 2013Article
- Article
- Residual force enhancement in skeletal muscles: one sarcomere after the other.Journal of muscle research and cell motility · 2012Review
- Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle.Journal of molecular and cellular cardiology · 2011Article
- Contribution of stretch to the change of activation properties of muscle fibers in the diaphragm at the transition from fetal to neonatal life.Frontiers in physiology · 2011Article
- Myofilament length dependent activation.Journal of molecular and cellular cardiology · 2010Review
- Cooperative cross-bridge activation of thin filaments contributes to the Frank-Starling mechanism in cardiac muscle.Biophysical journal · 2009Article
- Nonlinear force-length relationship in the ADP-induced contraction of skeletal myofibrils.Biophysical journal · 2007Article
- Influence of enhanced troponin C Ca2+-binding affinity on cooperative thin filament activation in rabbit skeletal muscle.The Journal of physiology · 2007Article
- Sarcomere lattice geometry influences cooperative myosin binding in muscle.PLoS computational biology · 2007Article
- The effects of force inhibition by sodium vanadate on cross-bridge binding, force redevelopment, and Ca2+ activation in cardiac muscle.Biophysical journal · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Linear dichroism of 5' tetramethyl-rhodamine (5'ATR) was measured to monitor the effect of sarcomere length (SL) on troponin C (TnC) structure during Ca2+ activation in single glycerinated rabbit psoas fibers and skinned right ventricular trabeculae from rats. Endogenous TnC was extracted, and the preparations were reconstituted with TnC fluorescently labeled with 5'ATR. In skinned psoas fibers reconstituted with sTnC labeled at Cys 98 with 5'ATR, dichroism was maximal during relaxation (pCa 9.2) and was minimal at pCa 4.0. In skinned cardiac trabeculae reconstituted with a mono-cysteine mutant cTnC (cTnC(C84)), dichroism of the 5'ATR probe attached to Cys 84 increased during Ca2+ activation of force. Force and dichroism-[Ca2+] relations were fit with the Hill equation to determine the pCa50 and slope (n). Increasing SL increased the Ca2+ sensitivity of force in both skinned psoas fibers and trabeculae. However, in skinned psoas fibers, neither SL changes or force inhibition had an effect on the Ca2+ sensitivity of dichroism. In contrast, increasing SL increased the Ca2+ sensitivity of both force and dichroism in skinned trabeculae. Furthermore, inhibition of force caused decreased Ca2+ sensitivity of dichroism, decreased dichroism at saturating [Ca2+], and loss of the influence of SL in cardiac muscle. The data indicate that in skeletal fibers SL-dependent shifts in the Ca2+ sensitivity of force are not caused by corresponding changes in Ca2+ binding to TnC and that strong cross-bridge binding has little effect on TnC structure at any SL or level of activation. On the other hand, in cardiac muscle, both force and activation-dependent changes in cTnC structure were influenced by SL. Additionally, the effect of SL on cardiac muscle activation was itself dependent on active, cycling cross-bridges.
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