ArticleAnalytical chemistry2015
Effective top-down LC/MS+ method for assessing actin isoforms as a potential cardiac disease marker.
Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Structural-Molecular Linkage Shapes the Adaptive Traits of Nuptial Pads in Male Rana chensinensis.Cell biochemistry and function · 2026Article
- Top-Down Mass Spectrometry and Its Current Applications in Biomarker Discovery in Aging and Age-Related Diseases.International journal of molecular sciences · 2026Review
- Structural and functional mechanisms of actin isoforms.The FEBS journal · 2025Review
- Dilated cardiomyopathy-associated skeletal muscle actin (ACTA1) mutation R256H disrupts actin structure and function and causes cardiomyocyte hypocontractility.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Proteomics of the heart.Physiological reviews · 2024Review
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics.Journal of proteome research · 2023Article
- Integrated proteomics reveals alterations in sarcomere composition and developmental processes during postnatal swine heart development.Journal of molecular and cellular cardiology · 2023Article
- Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021Review
- Top-down proteomics: challenges, innovations, and applications in basic and clinical research.Expert review of proteomics · 2020Article
- Comprehensive Characterization of the Recombinant Catalytic Subunit of cAMP-Dependent Protein Kinase by Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Intact-Mass Analysis Facilitating the Identification of Large Human Heart Proteoforms.Analytical chemistry · 2019Article
- A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.Analytical chemistry · 2019Article
- Comprehensive Characterization of Swine Cardiac Troponin T Proteoforms by Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Top-Down Proteomics of Large Proteins up to 223 kDa Enabled by Serial Size Exclusion Chromatography Strategy.Analytical chemistry · 2017Article
- Complete Characterization of Cardiac Myosin Heavy Chain (223 kDa) Enabled by Size-Exclusion Chromatography and Middle-Down Mass Spectrometry.Analytical chemistry · 2017Article
- Ubiquitin Chain Enrichment Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains in Cellulo.Analytical chemistry · 2017Article
- Top-down Proteomics: Technology Advancements and Applications to Heart Diseases.Expert review of proteomics · 2016Review
- Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics.Journal of muscle research and cell motility · 2016Article
- MASH Suite Pro: A Comprehensive Software Tool for Top-Down Proteomics.Molecular & cellular proteomics : MCP · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Actin is the major component of the cytoskeleton, playing an essential role in the structure and motility of both muscle and nonmuscle cells. It is highly conserved and encoded by a multigene family. α-Cardiac actin (αCAA) and α-skeletal actin (αSKA), encoded by two different genes, are the primary actin isoforms expressed in striated muscles. The relative expression levels of αSKA and αCAA have been shown to vary between species and under pathological conditions. In particular, an increased αSKA expression is believed to be a programmed response of a diseased heart. Therefore, it is essential to quantify the relative expression of αSKA and αCAA, which remains challenging due to the high degree of sequence similarity between these isoforms (98.9%). Herein, we developed a top-down liquid chromatography/mass spectrometry-based ("LC/MS+") method for the rapid purification and comprehensive analysis of α-actin extracted from muscle tissues. We thoroughly investigated all of the actin isoforms in healthy human cardiac and skeletal muscles. We found that αSKA is the only isoform expressed in skeletal muscle, whereas αCAA and αSKA are coexpressed in cardiac muscle. We then applied our method to quantify the α-actin isoforms in human healthy hearts and failing hearts with dilated cardiomyopathy (DCM). We found that αSKA is augmented in DCM compared with healthy controls, 43.1 ± 0.9% versus 23.7 ± 1.7%, respectively. As demonstrated, top-down LC/MS+ provides an effective and comprehensive method for the purification, quantification, and characterization of α-actin isoforms, enabling assessment of their clinical potential as cardiac disease markers.
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Registered trials
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