ArticleAmerican journal of physiology. Cell physiology2016
The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.
Article in American journal of physiology. Cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 65 citations in OpenAlex.
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- Characterizing residual and passive force enhancements in cardiac myofibrils.Biophysical journal · 2023Article
- Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023Review
- Titin activates myosin filaments in skeletal muscle by switching from an extensible spring to a mechanical rectifier.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- What Can We Learn from Single Sarcomere and Myofibril Preparations?Frontiers in physiology · 2022Review
- Solution NMR Structure of Titin N2A Region Ig Domain I83 and Its Interaction with Metal Ions.Journal of molecular biology · 2021Article
- Sarcomere Length Nonuniformity and Force Regulation in Myofibrils and Sarcomeres.Biophysical journal · 2020Review
- Force enhancement after stretch of isolated myofibrils is increased by sarcomere length non-uniformities.Scientific reports · 2020Article
- Hypothesis: Single Actomyosin Properties Account for Ensemble Behavior in Active Muscle Shortening and Isometric Contraction.International journal of molecular sciences · 2020Article
- Sarcomere length non-uniformities dictate force production along the descending limb of the force-length relation.Proceedings. Biological sciences · 2020Article
- N2A Titin: Signaling Hub and Mechanical Switch in Skeletal Muscle.International journal of molecular sciences · 2020Review
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- Current Understanding of Residual Force Enhancement: Cross-Bridge Component and Non-Cross-Bridge Component.International journal of molecular sciences · 2019Review
- Muscle thixotropy-where are we now?Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- Extensive eccentric contractions in intact cardiac trabeculae: revealing compelling differences in contractile behaviour compared to skeletal muscles.Proceedings. Biological sciences · 2019Article
- Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.American journal of physiology. Cell physiology · 2019Review
- The effects of fatigue and oxidation on contractile function of intact muscle fibers and myofibrils isolated from the mouse diaphragm.Scientific reports · 2019Article
- A mechanical model of the half-sarcomere which includes the contribution of titin.Journal of muscle research and cell motility · 2019Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Skeletal muscles present a non-cross-bridge increase in sarcomere stiffness and tension on Ca(2+) activation, referred to as static stiffness and static tension, respectively. It has been hypothesized that this increase in tension is caused by Ca(2+)-dependent changes in the properties of titin molecules. To verify this hypothesis, we investigated the static tension in muscles containing different titin isoforms. Permeabilized myofibrils were isolated from the psoas, soleus, and heart ventricle from the rabbit, and tested in pCa 9.0 and pCa 4.5, before and after extraction of troponin C, thin filaments, and treatment with the actomyosin inhibitor blebbistatin. The myofibrils were tested with stretches of different amplitudes in sarcomere lengths varying between 1.93 and 3.37 μm for the psoas, 2.68 and 4.21 μm for the soleus, and 1.51 and 2.86 μm for the ventricle. Using gel electrophoresis, we confirmed that the three muscles tested have different titin isoforms. The static tension was present in psoas and soleus myofibrils, but not in ventricle myofibrils, and higher in psoas myofibrils than in soleus myofibrils. These results suggest that the increase in the static tension is directly associated with Ca(2+)-dependent change in titin properties and not associated with changes in titin-actin interactions.
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