ArticleJournal of biomedicine & biotechnology2010
Titin-isoform dependence of titin-actin interaction and its regulation by S100A1/Ca2+ in skinned myocardium.
Article in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- CaBiophysical journal · 2025Article
- The calcium-binding protein S100A1 binds to titin's N2A insertion sequence in a pH-dependent manner.The Journal of general physiology · 2025Article
- S100 proteins in cardiovascular diseases.Molecular medicine (Cambridge, Mass.) · 2023Review
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Molecular Basis of S100A1 Activation and Target Regulation Within Physiological Cytosolic CaFrontiers in molecular biosciences · 2020Article
- Extensive eccentric contractions in intact cardiac trabeculae: revealing compelling differences in contractile behaviour compared to skeletal muscles.Proceedings. Biological sciences · 2019Article
- Cardiomyocytes, endothelial cells and cardiac fibroblasts: S100A1's triple action in cardiovascular pathophysiology.Future cardiology · 2015Review
- A novel three-filament model of force generation in eccentric contraction of skeletal muscles.PloS one · 2015Article
- Joining S100 proteins and migration: for better or for worse, in sickness and in health.Cellular and molecular life sciences : CMLS · 2014Review
- The passive properties of muscle fibers are velocity dependent.Journal of biomechanics · 2014Article
- Heart failure gene therapy: the path to clinical practice.Circulation research · 2013Review
- Targeting S100A1 in heart failure.Gene therapy · 2012Review
- Gene therapy targets in heart failure: the path to translation.Clinical pharmacology and therapeutics · 2011Review
- Titin based viscosity in ventricular physiology: an integrative investigation of PEVK-actin interactions.Journal of molecular and cellular cardiology · 2011Article
- Titin-actin interaction: PEVK-actin-based viscosity in a large animal.Journal of biomedicine & biotechnology · 2011Article
- S100A1: a multifaceted therapeutic target in cardiovascular disease.Journal of cardiovascular translational research · 2010Review
- Titin-based tension in the cardiac sarcomere: molecular origin and physiological adaptations.Progress in biophysics and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Titin, also known as connectin, is a large filamentous protein that greatly contributes to passive myocardial stiffness. In vitro evidence suggests that one of titin's spring elements, the PEVK, interacts with actin and that this adds a viscous component to passive stiffness. Differential splicing of titin gives rise to the stiff N2B and more compliant N2BA isoforms. Here we studied the titin-isoform dependence of titin-actin interaction and studied the bovine left atrium (BLA) that expresses mainly N2BA titin, and the bovine left ventricle (BLV) that expresses a mixture of both N2B and N2BA isoforms. For comparison we also studied mouse left ventricular (MLV) myocardium which expresses predominately N2B titin. Using the actin-severing protein gelsolin, we obtained evidence that titin-actin interaction contributes significantly to passive myocardial stiffness in all tissue types, but most in MLV, least in BLA, and an intermediate level in BLV. We also studied whether titin-actin interaction is regulated by S100A1/calcium and found that calcium alone or S100A1 alone did not alter passive stiffness, but that combined they significantly lowered stiffness. We propose that titin-actin interaction is a "viscous break" that is on during diastole and off during systole.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.