ArticleJournal of muscle research and cell motility2011
Expression of tropomyosin-κ induces dilated cardiomyopathy and depresses cardiac myofilament tension by mechanisms involving cross-bridge dependent activation and altered tropomyosin phosphorylation.
Article in Journal of muscle research and cell motility, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Transcriptome Reprogramming in Heart Failure: The Hidden Splicing Code.Current cardiology reports · 2026Review
- The splicing factor hnRNPL demonstrates conserved myocardial regulation across species and is altered in heart failure.FEBS letters · 2024Article
- Development and disease-specific regulation of RNA splicing in cardiovascular system.Frontiers in cell and developmental biology · 2024Review
- Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023Article
- Functional assays reveal the pathogenic mechanism of a de novo tropomyosin variant identified in patient with dilated cardiomyopathy.Journal of molecular and cellular cardiology · 2023Article
- Myocardial Injury Caused by Chronic Alcohol Exposure-A Pilot Study Based on Proteomics.Molecules (Basel, Switzerland) · 2022Article
- Nanopore sequencing reveals full-length Tropomyosin 1 isoforms and their regulation by RNA-binding proteins during rat heart development.Journal of cellular and molecular medicine · 2021Article
- Crucial Role of Mammalian Glutaredoxin 3 in Cardiac Energy Metabolism in Diet-induced Obese Mice Revealed by Transcriptome Analysis.International journal of biological sciences · 2021Article
- mRNA Metabolism in Cardiac Development and Disease: Life After Transcription.Physiological reviews · 2020Review
- Sarcomeric Gene Variants and Their Role with Left Ventricular Dysfunction in Background of Coronary Artery Disease.Biomolecules · 2020Review
- Phenotyping cardiomyopathy in adult zebrafish.Progress in biophysics and molecular biology · 2018Review
- Alternative splicing of the Caenorhabditis elegans lev-11 tropomyosin gene is regulated in a tissue-specific manner.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Pre-mRNA mis-splicing of sarcomeric genes in heart failure.Biochimica et biophysica acta. Molecular basis of disease · 2017Review
- Green Tea Catechin Normalizes the Enhanced Ca2+ Sensitivity of Myofilaments Regulated by a Hypertrophic Cardiomyopathy-Associated Mutation in Human Cardiac Troponin I (K206I).Circulation. Cardiovascular genetics · 2015Article
- Expression of Tropomyosin 1 Gene Isoforms in Human Breast Cancer Cell Lines.International journal of breast cancer · 2015Article
- Sarcomeric protein isoform transitions in cardiac muscle: a journey to heart failure.Biochimica et biophysica acta · 2015Review
- Expression of TPM1κ, a Novel Sarcomeric Isoform of the TPM1 Gene, in Mouse Heart and Skeletal Muscle.Molecular biology international · 2014Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle.Biochimica et biophysica acta · 2013Article
- Regulation of endothelial permeability and transendothelial migration of cancer cells by tropomyosin-1 phosphorylation.Vascular cell · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Tropomyosin-kappa (TPM1-κ) is a newly discovered tropomyosin (TM) isoform that is exclusively expressed in the human heart and generated by an alternative splicing of the α-TM gene. We reported that TPM1-κ expression was increased in the hearts of patients with chronic dilated cardiomyopathy (DCM). To increase our understanding of the significance of this shift in isoform population, we generated transgenic (TG) mice expressing TPM1-κ in the cardiac compartment where TPM1-κ replaces 90% of the native TM. We previously showed that there was a significant inhibition of the ability of strongly bound cross-bridges to induce activation of TG myofilaments (Rajan et al., Circulation 121:410-418, 2010). Here, we compared the force-Ca(2+) relations in detergent extracted (skinned) fiber bundles isolated from non-transgenic (NTG) and TG-TPM1-κ hearts at two sarcomere lengths (SLs). Our data demonstrated a significant decrease in the Ca(2+) sensitivity of the myofilaments from TG-TPM1-κ hearts with no change in the maximum developed tension, length-dependent activation, and the ratio of ATPase rate to tension. There was also no difference in the affinity and cooperativity of Ca(2+)-binding to troponin in thin filaments reconstituted with either TPM1-κ or α-TM. We also compared protein phosphorylation in NTG and TG-TPM1-κ myofilaments. There was a decrease in the total phosphorylation of TPM1-κ compared to α-TM, but no significant change in other major sarcomeric proteins. Our results identify a novel mode of myofilament desensitization to Ca(2+) associated with a DCM linked switch in TM isoform population.
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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.