ArticleBiochimica et biophysica acta2013
Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 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
- Does force depression resulting from shortening against series elasticity contribute to the activation dependence of optimum length?American journal of physiology. Cell physiology · 2025Article
- Neurophysiology of ACL Injury.Orthopedic reviews · 2025Article
- The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.Nature communications · 2024Article
- Myosin-binding protein C forms C-links and stabilizes OFF states of myosin.bioRxiv : the preprint server for biology · 2023Article
- Muscle Mechanics and Thick Filament Activation: An Emerging Two-Way Interaction for the Vertebrate Striated Muscle Fine Regulation.International journal of molecular sciences · 2023Review
- Rbm20International journal of molecular sciences · 2022Article
- Titin force in muscle cells alters lattice order, thick and thin filament protein formation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cross-bridge mechanics estimated from skeletal muscles' work-loop responses to impacts in legged locomotion.Scientific reports · 2021Article
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- Mechano-calcium and mechano-electric feedbacks in the human cardiomyocyte analyzed in a mathematical model.The journal of physiological sciences : JPS · 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
- Megaesophagus Is a Major Pathological Condition in Rats With a Large Deletion in theVeterinary pathology · 2020Article
- End-diastolic force pre-activates cardiomyocytes and determines contractile force: role of titin and calcium.The Journal of physiology · 2019Article
- Sarcomere length-dependent effects on CaThe Journal of general physiology · 2019Article
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- The Frank-Starling Law: a jigsaw of titin proportions.Biophysical reviews · 2017Review
- Reply to "Letter to the editor: Comments on Cornachione et al. (2016): "The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms".American journal of physiology. Cell physiology · 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
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The magnitude of length dependent activation in striated muscle has been shown to vary with titin isoform. Recently, a rat that harbors a homozygous autosomal mutation (HM) causing preferential expression of a longer, giant titin isoform was discovered (Greaser et al. 2005). Here, we investigated the impact of titin isoform on myofilament force development and cross-bridge cycling kinetics as function of sarcomere length (SL) in tibialis anterior skeletal muscle isolated from wild type (WT) and HM. Skeletal muscle bundles from HM rats exhibited reductions in passive tension, maximal force development, myofilament calcium sensitivity, maximal ATP consumption, and tension cost at both short and long sarcomere length (SL=2.8μm and SL=3.2μm, respectively). Moreover, the SL-dependent changes in these parameters were attenuated in HM muscles. Additionally, myofilament Ca(2+) activation-relaxation properties were assessed in single isolated myofibrils. Both the rate of tension generation upon Ca(2+) activation (kACT) as well as the rate of tension redevelopment following a length perturbation (kTR) were reduced in HM myofibrils compared to WT, while relaxation kinetics were not affected. We conclude that presence of a long isoform of titin in the striated muscle sarcomere is associated with reduced myofilament force development and cross-bridge cycling kinetics, and a blunting of myofilament length dependent activation. This article is part of a Special Issue entitled: Cardiomyocyte Biology: Cardiac Pathways of Differentiation, Metabolism and Contraction.
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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.