ArticleJournal of muscle research and cell motility1999
A single-fiber in vitro motility assay. In vitro sliding velocity of F-actin vs. unloaded shortening velocity in skinned muscle fibers.
Article in Journal of muscle research and cell motility, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Cardiac ventricular myosin and slow skeletal myosin exhibit dissimilar chemomechanical properties despite bearing the same myosin heavy chain isoform.The Journal of biological chemistry · 2022Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity.The Journal of general physiology · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Extraction Protocols for Individual Zebrafish's Ventricle Myosin and Skeletal Muscle Actin forFrontiers in physiology · 2017Article
- Radial stiffness characteristics of the overlap regions of sarcomeres in isolated skeletal myofibrils in pre-force generating state.Biophysics and physicobiology · 2017Article
- Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- ATP turnover by individual myosin molecules hints at two conformers of the myosin active site.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Skeletal muscle myofilament adaptations to aging, disease, and disuse and their effects on whole muscle performance in older adult humans.Frontiers in physiology · 2014Review
- Mechanical and kinetic properties of β-cardiac/slow skeletal muscle myosin.Journal of muscle research and cell motility · 2012Article
- Translational actomyosin research: fundamental insights and applications hand in hand.Journal of muscle research and cell motility · 2012Review
- An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle.The Journal of physiology · 2012Article
- Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Mechanical properties of single myosin molecules probed with the photonic force microscope.Biophysical journal · 2005Article
- Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles.The Journal of physiology · 2003Article
- Mutation of the myosin converter domain alters cross-bridge elasticity.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Actomyosin interactions in a novel single muscle fiber in vitro motility assay.Journal of muscle research and cell motility · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe an approach that allows us to form a micro in vitro motility assay with as little myosin as can be retrieved from a short (approximately 10 mm) segment of a single skinned skeletal muscle fiber (diameter some 100 microm). Myosin is directly extracted from the single fiber segment by a high ionic strength solution in the presence of MgATP, and the extracted myosin is immediately applied to a miniaturized flow cell that has been pretreated with BSA. The observed sliding velocities of fluorescently labeled F-actin are essentially identical with those reported in the literature. Since at the single fiber level most muscle fibers contain only a single myosin heavy chain isoform this approach allows us to determine without additional purification steps, the sliding velocity driven by myosins with different heavy chain isoforms. In addition, this approach can be used to directly correlate under identical experimental conditions unloaded shortening velocity measured in segments of skinned muscle fibers with the in vitro sliding velocity of fluorescently labeled F-actin by extraction of myosin from the same skinned fibers. Such direct correlation was performed with different myosin heavy chain isoforms as well as at different temperatures and ionic strengths. Under all conditions studied, unloaded shortening velocity was 4- to 8-fold faster than sliding velocity in the motility assay even at high temperature (22 degrees C) and ionic strengths >50 mM. This suggests that sliding velocity in the motility assay is limited by additional factors beyond those thought to limit velocity of unloaded shortening in muscle fibers. One such factor might be unspecific ionic interactions between F-actin and the substrate in the motility assay resulting in somewhat higher sensitivity for ionic strength of sliding velocity in the motility assay. This might become of special relevance when using in vitro sliding velocity in assessing functional consequences of mutations involving charged residues of actin or myosin.
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