ArticleJournal of biomedicine & biotechnology2011
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
Article in Journal of biomedicine & biotechnology, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Diastolic contributors in cardiomyocytes of a cardiometabolic HFpEF-like mouse model.The Journal of general physiology · 2026Article
- Skeletal muscle knockout of NAD(P)H oxidase 2 delays the development of isotonic diaphragm fatigue in mice.Free radical biology & medicine · 2025Article
- CaBiophysical journal · 2025Article
- The L348P point mutation in cardiac myosin binding protein-C alters transient responses to stretch, slows cardiac relaxation, and is embryonic lethal in homozygous CRISPR gene-edited mice.Journal of molecular and cellular cardiology · 2025Article
- Modeling sepsis, with a special focus on large animal models of porcine peritonitis and bacteremia.Frontiers in physiology · 2022Review
- The titin N2B and N2A regions: biomechanical and metabolic signaling hubs in cross-striated muscles.Biophysical reviews · 2021Review
- The Effects of Mechanical Preload on Transmural Differences in Mechano-Calcium-Electric Feedback in Single Cardiomyocytes: Experiments and Mathematical Models.Frontiers in physiology · 2020Article
- 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 enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- The multiple roles of titin in muscle contraction and force production.Biophysical reviews · 2018Review
- Cell- and molecular-level mechanisms contributing to diastolic dysfunction in HFpEF.Journal of applied physiology (Bethesda, Md. : 1985) · 2015Review
- A novel three-filament model of force generation in eccentric contraction of skeletal muscles.PloS one · 2015Article
- Increased myocardial short-range forces in a rodent model of diabetes reflect elevated content of β myosin heavy chain.Archives of biochemistry and biophysics · 2014Article
- Small and large animal models in cardiac contraction research: advantages and disadvantages.Pharmacology & therapeutics · 2014Review
- Temperature and transmural region influence functional measurements in unloaded left ventricular cardiomyocytes.Physiological reports · 2013Article
- Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.The Journal of biological chemistry · 2013Article
- The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements.Journal of molecular and cellular cardiology · 2013Article
- Conformational dynamics of titin PEVK explored with FRET spectroscopy.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Titin exhibits an interaction between its PEVK segment and the actin filament resulting in viscosity, a speed dependent resistive force, which significantly influences diastolic filling in mice. While diastolic disease is clinically pervasive, humans express a more compliant titin (N2BA:N2B ratio ~0.5-1.0) than mice (N2BA:N2B ratio ~0.2). To examine PEVK-actin based viscosity in compliant titin-tissues, we used pig cardiac tissue that expresses titin isoforms similar to that in humans. Stretch-hold experiments were performed at speeds from 0.1 to 10 lengths/s from slack sarcomere lengths (SL) to SL of 2.15 μm. Viscosity was calculated from the slope of stress-relaxation vs stretch speed. Recombinant PEVK was added to compete off native interactions and this found to reduce the slope by 35%, suggesting that PEVK-actin interactions are a strong contributor of viscosity. Frequency sweeps were performed at frequencies of 0.1-400 Hz and recombinant protein reduced viscous moduli by 40% at 2.15 μm and by 50% at 2.25 μm, suggesting a SL-dependent nature of viscosity that might prevent SL "overshoot" at long diastolic SLs. This study is the first to show that viscosity is present at physiologic speeds in the pig and supports the physiologic relevance of PEVK-actin interactions in humans in both health and disease.
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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.