ArticlePloS one2014
Phosphoproteomic profiling of human myocardial tissues distinguishes ischemic from non-ischemic end stage heart failure.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Mitochondrial Imaging Detects Early Cardiac Changes Following Cancer Immunotherapy.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026Article
- Phosphoproteomics distinguishes disease-specific mechanisms for human phospholamban cardiomyopathy reversible by RNA therapy.Signal transduction and targeted therapy · 2026Article
- Proteomics of the heart.Physiological reviews · 2024Review
- Deep Learning Resolves Myovascular Dynamics in the Failing Human Heart.JACC. Basic to translational science · 2024Article
- Phenotyping patients with ischaemic heart disease at risk of developing heart failure: an analysis of the HOMAGE trial.ESC heart failure · 2024Article
- Proteomics and phosphoproteomics of failing human left ventricle identifies dilated cardiomyopathy-associated phosphorylation of CTNNA3.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Phosphoproteomic and proteomic profiling in post-infarction chronic heart failure.Frontiers in pharmacology · 2023Article
- Article
- Fibulin-3 Deficiency Protects Against Myocardial Injury Following Ischaemia/ Reperfusion inFrontiers in cardiovascular medicine · 2022Article
- Functional and Molecular Characterisation of Heart Failure Progression in Mice and the Role of Myosin Regulatory Light Chains in the Recovery of Cardiac Muscle Function.International journal of molecular sciences · 2021Article
- Fortilin inhibits p53, halts cardiomyocyte apoptosis, and protects the heart against heart failure.Cell death discovery · 2021Article
- Integrated Quantitative Phosphoproteomics and Cell-based Functional Screening Reveals Specific Pathological Cardiac Hypertrophy-related Phosphorylation Sites.Molecules and cells · 2021Article
- Mapping signalling perturbations in myocardial fibrosis via the integrative phosphoproteomic profiling of tissue from diverse sources.Nature biomedical engineering · 2020Article
- Quantitative proteomic and phosphoproteomic profiling of ischemic myocardial stunning in swine.American journal of physiology. Heart and circulatory physiology · 2020Article
- The Arabidopsis Proteins AtNHR2A and AtNHR2B Are Multi-Functional Proteins Integrating Plant Immunity With Other Biological Processes.Frontiers in plant science · 2020Article
- The nuclear receptor RORα protects against angiotensin II-induced cardiac hypertrophy and heart failure.American journal of physiology. Heart and circulatory physiology · 2019Article
- Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome: Where There Is a Will, There Is a Way.Circulation research · 2018Review
- Quantitative cardiac phosphoproteomics profiling during ischemia-reperfusion in an immature swine model.American journal of physiology. Heart and circulatory physiology · 2017Article
- Proteomic Analysis of Primary Human Airway Epithelial Cells Exposed to the Respiratory Toxicant Diacetyl.Journal of proteome research · 2017Article
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Authors and funding
20 authors at 3 institutions in 1 country.
Funding
Abstract
The molecular differences between ischemic (IF) and non-ischemic (NIF) heart failure are poorly defined. A better understanding of the molecular differences between these two heart failure etiologies may lead to the development of more effective heart failure therapeutics. In this study extensive proteomic and phosphoproteomic profiles of myocardial tissue from patients diagnosed with IF or NIF were assembled and compared. Proteins extracted from left ventricular sections were proteolyzed and phosphopeptides were enriched using titanium dioxide resin. Gel- and label-free nanoscale capillary liquid chromatography coupled to high resolution accuracy mass tandem mass spectrometry allowed for the quantification of 4,436 peptides (corresponding to 450 proteins) and 823 phosphopeptides (corresponding to 400 proteins) from the unenriched and phospho-enriched fractions, respectively. Protein abundance did not distinguish NIF from IF. In contrast, 37 peptides (corresponding to 26 proteins) exhibited a ≥ 2-fold alteration in phosphorylation state (p<0.05) when comparing IF and NIF. The degree of protein phosphorylation at these 37 sites was specifically dependent upon the heart failure etiology examined. Proteins exhibiting phosphorylation alterations were grouped into functional categories: transcriptional activation/RNA processing; cytoskeleton structure/function; molecular chaperones; cell adhesion/signaling; apoptosis; and energetic/metabolism. Phosphoproteomic analysis demonstrated profound post-translational differences in proteins that are involved in multiple cellular processes between different heart failure phenotypes. Understanding the roles these phosphorylation alterations play in the development of NIF and IF has the potential to generate etiology-specific heart failure therapeutics, which could be more effective than current therapeutics in addressing the growing concern of heart failure.
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