ArticleJournal of muscle research and cell motility2010
Striated muscle tropomyosin isoforms differentially regulate cardiac performance and myofilament calcium sensitivity.
Article in Journal of muscle research and cell motility, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 20 citations in OpenAlex.
- Identification of Differential Proteins in Thrombi of Cardioembolic and Atherothrombotic Etiology in Patients with Ischemic Stroke.International journal of molecular sciences · 2025Article
- Genetic predisposition study of heart failure and its association with cardiomyopathy.The Egyptian heart journal : (EHJ) : official bulletin of the Egyptian Society of Cardiology · 2022Review
- 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
- Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020Review
- Association of single nucleotide polymorphisms in the 3'UTR region of TPM1 gene with dilated cardiomyopathy: A case-control study.Medicine · 2019Article
- Selection signatures in four German warmblood horse breeds: Tracing breeding history in the modern sport horse.PloS one · 2019Article
- HIC2 regulates isoform switching during maturation of the cardiovascular system.Journal of molecular and cellular cardiology · 2018Article
- Tropomyosin 1: Multiple roles in the developing heart and in the formation of congenital heart defects.Journal of molecular and cellular cardiology · 2017Article
- Differences in Contractile Function of Myofibrils within Human Embryonic Stem Cell-Derived Cardiomyocytes vs. Adult Ventricular Myofibrils Are Related to Distinct Sarcomeric Protein Isoforms.Frontiers in physiology · 2017Article
- Instability in the central region of tropomyosin modulates the function of its overlapping ends.Biophysical journal · 2013Article
- Decreasing tropomyosin phosphorylation rescues tropomyosin-induced familial hypertrophic cardiomyopathy.The Journal of biological chemistry · 2013Article
- In-depth proteomic analysis of human tropomyosin by top-down mass spectrometry.Journal of muscle research and cell motility · 2013Article
- Identification of two new regions in the N-terminus of cardiac troponin T that have divergent effects on cardiac contractile function.The Journal of physiology · 2013Article
- Top-down targeted proteomics for deep sequencing of tropomyosin isoforms.Journal of proteome research · 2013Article
- Tropomyosin flexural rigidity and single ca(2+) regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy.Frontiers in physiology · 2012Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Tropomyosin (TM) plays a central role in calcium mediated striated muscle contraction. There are three muscle TM isoforms: alpha-TM, beta-TM, and gamma-TM. alpha-TM is the predominant cardiac and skeletal muscle isoform. beta-TM is expressed in skeletal and embryonic cardiac muscle. gamma-TM is expressed in slow-twitch musculature, but is not found in the heart. Our previous work established that muscle TM isoforms confer different physiological properties to the cardiac sarcomere. To determine whether one of these isoforms is dominant in dictating its functional properties, we generated single and double transgenic mice expressing beta-TM and/or gamma-TM in the heart, in addition to the endogenously expressed alpha-TM. Results show significant TM protein expression in the betagamma-DTG hearts: alpha-TM: 36%, beta-TM: 32%, and gamma-TM: 32%. These betagamma-DTG mice do not develop pathological abnormalities; however, they exhibit a hyper contractile phenotype with decreased myofilament calcium sensitivity, similar to gamma-TM transgenic hearts. Biophysical studies indicate that gamma-TM is more rigid than either alpha-TM or beta-TM. This is the first report showing that with approximately equivalent levels of expression within the same tissue, there is a functional dominance of gamma-TM over alpha-TM or beta-TM in regulating physiological performance of the striated muscle sarcomere. In addition to the effect expression of gamma-TM has on Ca(2+) activation of the cardiac myofilaments, our data demonstrates an effect on cooperative activation of the thin filament by strongly bound rigor cross-bridges. This is significant in relation to current ideas on the control mechanism of the steep relation between Ca(2+) and tension.
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Registered trials
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