ArticleThe Journal of physiology2007
Influence of enhanced troponin C Ca2+-binding affinity on cooperative thin filament activation in rabbit skeletal muscle.
Article in The Journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- Hypertrophic cardiomyopathy: Mutations to mechanisms to therapies.Frontiers in physiology · 2022Review
- Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016Review
- The length-tension curve in muscle depends on lattice spacing.Proceedings. Biological sciences · 2013Article
- Structural and functional consequences of cardiac troponin C L57Q and I61Q Ca(2+)-desensitizing variants.Archives of biochemistry and biophysics · 2013Article
- Contractility and kinetics of human fetal and human adult skeletal muscle.The Journal of physiology · 2013Article
- Filament compliance influences cooperative activation of thin filaments and the dynamics of force production in skeletal muscle.PLoS computational biology · 2012Article
- Assessment of contractility in intact ventricular cardiomyocytes using the dimensionless 'Frank-Starling Gain' index.Pflugers Archiv : European journal of physiology · 2011Review
- Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle.Journal of molecular and cellular cardiology · 2011Article
- Effect of Ca2+ binding properties of troponin C on rate of skeletal muscle force redevelopment.American journal of physiology. Cell physiology · 2010Article
- Myofilament length dependent activation.Journal of molecular and cellular cardiology · 2010Review
- Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C.Journal of molecular and cellular cardiology · 2008Article
- Thin filament Ca2+ binding properties and regulatory unit interactions alter kinetics of tension development and relaxation in rabbit skeletal muscle.The Journal of physiology · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We studied how enhanced skeletal troponin C (sTnC) Ca2+-binding affinity affects cooperative thin filament activation and contraction in single demembranated rabbit psoas fibres. Three sTnC mutants were created and incorporated into skeletal troponin (sTn) for measurement of Ca2+ dissociation, resulting in the following order of rates: wild-type (WT) sTnC-sTn>sTnC(F27W)-sTn>M80Q sTnC-sTn>M80Q sTnCF27W-sTn. Reconstitution of sTnC-extracted fibres increased Ca2+ sensitivity of steady-state force (pCa(50)) by 0.08 for M80Q sTnC, 0.15 for sTnCF27W and 0.32 for M80Q sTnCF27W with minimal loss of slope (nH, degree of cooperativity). Near-neighbour thin filament regulatory unit (RU) interactions were reduced in fibres by incorporating mixtures of WT or mutant sTnC and D28A, D64A sTnC (xxsTnC) that does not bind Ca2+ at N-terminal sites. Reconstitution with sTnC: xxsTnC mixtures to 20% of pre-exchanged maximal force reduced pCa50 by 0.35 for sTnC: xxsTnC, 0.25 for M80Q sTnC: xxsTnC, and 0.10 for M80Q sTnCF27W: xxsTnC. It is interesting that pCa50 increased by approximately 0.1 for M80Q sTnC and approximately 0.3 for M80Q sTnCF27W when near-neighbour RU interactions were reduced; these values are similar in magnitude to those for fibres reconstituted with 100% mutant sTnC. After reconstitution with sTnC: xxsTnC mixtures, nH decreased to a similar value for all mutant sTnCs. Altered sTnC Ca2+-binding properties (M80Q sTnCF27W) did not affect strong crossbridge inhibition by 2,3-butanedione monoxime when near-neighbour thin filament RU interactions were reduced. Together these results suggest increased sTnC Ca2+ affinity strongly influences Ca2+ sensitivity of steady-state force without affecting near-neighbour thin filament RU cooperative activation or the relative contribution of crossbridges versus Ca2+ to thin filament activation.
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