ArticleAmerican journal of physiology. Heart and circulatory physiology2012
Magnitude of length-dependent changes in contractile properties varies with titin isoform in rat ventricles.
Article in American journal of physiology. Heart and circulatory physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 39 citations in OpenAlex.
- Human atrial skinned muscle fibers exhibit reduced length-dependent activation but show faster force development kinetics than ventricular muscle.Journal of molecular and cellular cardiology · 2026Article
- GSK3β-driven phosphorylation of ABLIM1 regulates its interactions with titin cardiac muscle.The Journal of general physiology · 2025Article
- Does force depression resulting from shortening against series elasticity contribute to the activation dependence of optimum length?American journal of physiology. Cell physiology · 2025Article
- cMyBP-C ablation in human engineered cardiac tissue causes progressive Ca2+-handling abnormalities.The Journal of general physiology · 2023Article
- Titin (TTN): from molecule to modifications, mechanics, and medical significance.Cardiovascular research · 2022Review
- cMyBP-C phosphorylation modulates the time-dependent slowing of unloaded shortening in murine skinned myocardium.The Journal of general physiology · 2021Article
- End-diastolic force pre-activates cardiomyocytes and determines contractile force: role of titin and calcium.The Journal of physiology · 2019Article
- Omecamtiv Mecarbil Slows Myosin Kinetics in Skinned Rat Myocardium at Physiological Temperature.Biophysical journal · 2019Article
- Deletion of Enigma Homologue from the Z-disc slows tension development kinetics in mouse myocardium.The Journal of general physiology · 2019Article
- Recovery of left ventricular function following in vivo reexpression of cardiac myosin binding protein C.The Journal of general physiology · 2019Article
- Force-Dependent Recruitment from the Myosin Off State Contributes to Length-Dependent Activation.Biophysical journal · 2018Article
- Organ-level right ventricular dysfunction with preserved Frank-Starling mechanism in a mouse model of pulmonary arterial hypertension.Journal of applied physiology (Bethesda, Md. : 1985) · 2018Article
- Impact of titin strain on the cardiac slow force response.Progress in biophysics and molecular biology · 2017Article
- Tampering with springs: phosphorylation of titin affecting the mechanical function of cardiomyocytes.Biophysical reviews · 2017Review
- Distinct contributions of the thin and thick filaments to length-dependent activation in heart muscle.eLife · 2017Article
- Altered Right Ventricular Mechanical Properties Are Afterload Dependent in a Rodent Model of Bronchopulmonary Dysplasia.Frontiers in physiology · 2017Article
- Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion.The Journal of physiology · 2016Article
- Molecule specific effects of PKA-mediated phosphorylation on rat isolated heart and cardiac myofibrillar function.Archives of biochemistry and biophysics · 2016Article
- Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin- and thick-filament proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The effects of differential expression of titin isoforms on sarcomere length (SL)-dependent changes in passive force, maximum Ca(2+)-activated force, apparent cooperativity in activation of force (n(H)), Ca(2+) sensitivity of force (pCa(50)), and rate of force redevelopment (k(tr)) were investigated in rat cardiac muscle. Skinned right ventricular trabeculae were isolated from wild-type (WT) and mutant homozygote (Ho) hearts expressing predominantly a smaller N2B isoform (2,970 kDa) and a giant N2BA-G isoform (3,830 kDa), respectively. Stretching WT and Ho trabeculae from SL 2.0 to 2.35 μm increased passive force, maximum Ca(2+)-activated force, and pCa(50), and it decreased n(H) and k(tr). Compared with WT trabeculae, the magnitude of SL-dependent changes in passive force, maximum Ca(2+)-activated force, pCa(50), and n(H) was significantly smaller in Ho trabeculae. These results suggests that, at least in rat ventricle, the magnitude of SL-dependent changes in passive force, maximum Ca(2+)-activated force, pCa(50), n(H), and k(tr) is defined by the titin isoform.
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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.