ArticleJournal of theoretical biology2011
Cross-bridge kinetics in myofibrils containing familial hypertrophic cardiomyopathy R58Q mutation in the regulatory light chain of myosin.
Article in Journal of theoretical biology, 2011. 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, 23 citations in OpenAlex.
- Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022Review
- Induced Pluripotent Stem Cell-Derived Cardiomyocytes from a Patient with MYL2-R58Q-Mediated Apical Hypertrophic Cardiomyopathy Show Hypertrophy, Myofibrillar Disarray, and Calcium Perturbations.Journal of cardiovascular translational research · 2019Article
- Slow-twitch skeletal muscle defects accompany cardiac dysfunction in transgenic mice with a mutation in the myosin regulatory light chain.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- No Difference in Myosin Kinetics and Spatial Distribution of the Lever Arm in the Left and Right Ventricles of Human Hearts.Frontiers in physiology · 2017Article
- High ionic strength depresses muscle contractility by decreasing both force per cross-bridge and the number of strongly attached cross-bridges.Journal of muscle research and cell motility · 2015Article
- Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.American journal of physiology. Heart and circulatory physiology · 2015Article
- A Novel Method of Determining the Functional Effects of a Minor Genetic Modification of a Protein.Frontiers in cardiovascular medicine · 2015Article
- The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse hearts.Biochemistry · 2014Article
- Using baculovirus/insect cell expressed recombinant actin to study the molecular pathogenesis of HCM caused by actin mutation A331P.Journal of molecular and cellular cardiology · 2014Article
- Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific manner.Biophysical journal · 2014Article
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Hypertrophic cardiomyopathy: a heart in need of an energy bar?Frontiers in physiology · 2014Review
- Social network characteristics and body mass index in an elderly Korean population.Journal of preventive medicine and public health = Yebang Uihakhoe chi · 2013Article
- Diversity and similarity of motor function and cross-bridge kinetics in papillary muscles of transgenic mice carrying myosin regulatory light chain mutations D166V and R58Q.Journal of molecular and cellular cardiology · 2013Article
- Discrete effects of A57G-myosin essential light chain mutation associated with familial hypertrophic cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2013Article
- Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.The Journal of biological chemistry · 2013Article
- Mesoscopic analysis of motion and conformation of cross-bridges.Biophysical reviews · 2012Review
- Myosin regulatory light chain mutation found in hypertrophic cardiomyopathy patients increases isometric force production in transgenic mice.The Biochemical journal · 2012Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Familial hypertrophic cardiomyopathy (FHC) is a heritable form of cardiac hypertrophy caused by single-point mutations in genes encoding sarcomeric proteins including ventricular myosin regulatory light chain (RLC). FHC often leads to malignant outcomes and sudden cardiac death. The FHC mutations are believed to alter the kinetics of the interaction between actin and myosin resulting in inefficient energy utilization and compromised function of the heart. We studied the effect of the FHC-linked R58Q-RLC mutation on the kinetics of transgenic (Tg)-R58Q cardiac myofibrils. Kinetics was determined from the rate of change of orientation of actin monomers during muscle contraction. Actin monomers change orientation because myosin cross-bridges deliver periodic force impulses to it. An individual impulse (but not time average of impulses) carries the information about the kinetics of actomyosin interaction. To observe individual impulses it was necessary to scale down the experiments to the level of a few molecules. A small population (∼4 molecules) was selected by using (deliberately) inefficient fluorescence labeling and observing fluorescent molecules by a confocal microscope. We show that the kinetic rates are significantly smaller in the contracting cardiac myofibrils from Tg-R58Q mice then in control Tg-wild type (WT). We also demonstrate a lower force per cross-section of muscle fiber in Tg-R58Q versus Tg-WT mice. We conclude that the R58Q mutation-induced decrease in cross-bridge kinetics underlines the mechanism by which Tg-R58Q fibers develop low force and thus compromise the ability of the mutated heart to efficiently pump blood.
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