ArticleBiophysical journal2003
Molecular basis of passive stress relaxation in human soleus fibers: assessment of the role of immunoglobulin-like domain unfolding.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Glycerol storage increases passive stiffness of muscle fibers through effects on titin extensibility.The Journal of general physiology · 2025Article
- Strain-dependent dynamic re-alignment of collagen fibers in skeletal muscle extracellular matrix.Acta biomaterialia · 2024Article
- Deleting Titin's C-Terminal PEVK Exons Increases Passive Stiffness, Alters Splicing, and Induces Cross-Sectional and Longitudinal Hypertrophy in Skeletal Muscle.Frontiers in physiology · 2020Article
- Passive force and viscoelastic properties of single fibers in human aging muscles.European journal of applied physiology · 2019Article
- The Mechanical Power of Titin Folding.Cell reports · 2019Article
- The giant protein titin regulates the length of the striated muscle thick filament.Nature communications · 2017Article
- Work Done by Titin Protein Folding Assists Muscle Contraction.Cell reports · 2016Article
- The toxic effect of R350P mutant desmin in striated muscle of man and mouse.Acta neuropathologica · 2015Article
- Mechanical properties of respiratory muscles.Comprehensive Physiology · 2013Review
- Engineering of an elastic scaffolding polyprotein based on an SH3-binding intrinsically disordered titin PEVK module.Protein expression and purification · 2012Article
- Mechanics on myocardium deficient in the N2B region of titin: the cardiac-unique spring element improves efficiency of the cardiac cycle.Biophysical journal · 2011Article
- Titin based viscosity in ventricular physiology: an integrative investigation of PEVK-actin interactions.Journal of molecular and cellular cardiology · 2011Article
- Genetic variation in titin in arrhythmogenic right ventricular cardiomyopathy-overlap syndromes.Circulation · 2011Article
- Titin-actin interaction: PEVK-actin-based viscosity in a large animal.Journal of biomedicine & biotechnology · 2011Article
- Activation and stretch-induced passive force enhancement--are you pulling my chain? Focus on "Regulation of muscle force in the absence of actin-myosin-based cross-bridge interaction".American journal of physiology. Cell physiology · 2010Article
- Pulling single molecules of titin by AFM--recent advances and physiological implications.Pflugers Archiv : European journal of physiology · 2008Review
- Interaction forces between F-actin and titin PEVK domain measured with optical tweezers.Biophysical journal · 2007Article
- Hierarchical extensibility in the PEVK domain of skeletal-muscle titin.Biophysical journal · 2005Article
- Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner.The Journal of general physiology · 2005Article
- Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?Journal of muscle research and cell motility · 2005Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Titin (also known as connectin) is the main determinant of physiological levels of passive muscle force. This force is generated by the extensible I-band region of the molecule, which is constructed of the PEVK domain and tandem-immunoglobulin segments comprising serially linked immunoglobulin (Ig)-like domains. It is unresolved whether under physiological conditions Ig domains remain folded and act as "spacers" that set the sarcomere length at which the PEVK extends or whether they contribute to titin's extensibility by unfolding. Here we focused on whether Ig unfolding plays a prominent role in stress relaxation (decay of force at constant length after stretch) using mechanical and immunolabeling studies on relaxed human soleus muscle fibers and Monte Carlo simulations. Simulation experiments using Ig-domain unfolding parameters obtained in earlier single-molecule atomic force microscopy experiments recover the phenomenology of stress relaxation and predict large-scale unfolding in titin during an extended period (> approximately 20 min) of relaxation. By contrast, immunolabeling experiments failed to demonstrate large-scale unfolding. Thus, under physiological conditions in relaxed human soleus fibers, Ig domains are more stable than predicted by atomic force microscopy experiments. Ig-domain unfolding did not become more pronounced after gelsolin treatment, suggesting that the thin filament is unlikely to significantly contribute to the mechanical stability of the domains. We conclude that in human soleus fibers, Ig unfolding cannot solely explain stress relaxation.
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