ArticlePloS one2015
Overexpression of Catalase Diminishes Oxidative Cysteine Modifications of Cardiac Proteins.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
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- The Action of Cannabidiol on Doxycycline Cytotoxicity in Human Cells-In Vitro Study.Molecules (Basel, Switzerland) · 2025Article
- ROS homeostasis in cell fate, pathophysiology, and therapeutic interventions.Molecular biomedicine · 2025Review
- Protective Action of Cannabidiol on Tiamulin Toxicity in Humans-In Vitro Study.International journal of molecular sciences · 2024Article
- Date seeds powder alleviate the aflatoxin B1 provoked heart toxicity in male offspring rat.Scientific reports · 2024Article
- Pharmacological Evaluation of Newly Synthesized Cannabidiol Derivates on H9c2 Cells.Antioxidants (Basel, Switzerland) · 2023Article
- Catalase deficiency facilitates the shuttling of free fatty acid to brown adipose tissue through lipolysis mediated by ROS during sustained fasting.Cell & bioscience · 2021Article
- Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation.Redox biology · 2020Article
- Osteocytes control myeloid cell proliferation and differentiation through Gsα-dependent and -independent mechanisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Redox RegulationAntioxidants & redox signaling · 2020Review
- Peroxisomal Hydrogen Peroxide Metabolism and Signaling in Health and Disease.International journal of molecular sciences · 2019Review
- Altered Intracellular Calcium Homeostasis and Arrhythmogenesis in the Aged Heart.International journal of molecular sciences · 2019Review
- Mitochondrial stress management: a dynamic journey.Cell stress · 2018Review
- Advanced aging causes diaphragm functional abnormalities, global proteome remodeling, and loss of mitochondrial cysteine redox flexibility in mice.Experimental gerontology · 2018Article
- Combined Catalase and ADH Inhibition Ameliorates Ethanol-Induced Myocardial Dysfunction Despite Causing Oxidative Stress in Conscious Female Rats.Alcoholism, clinical and experimental research · 2017Article
- Catalase overexpression modulates metabolic parameters in a new 'stress-less' leptin-deficient mouse model.Biochimica et biophysica acta. Molecular basis of disease · 2017Article
- Redox regulation of ischemic limb neovascularization - What we have learned from animal studies.Redox biology · 2017Review
- The Peroxisome-Mitochondria Connection: How and Why?International journal of molecular sciences · 2017Review
- Systems biology-opportunities and challenges: the application of proteomics to study the cardiovascular extracellular matrix.Cardiovascular research · 2016Review
- Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Proteomics. Clinical applications · 2016Review
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 1 country.
Funding
Abstract
Reactive protein cysteine thiolates are instrumental in redox regulation. Oxidants, such as hydrogen peroxide (H2O2), react with thiolates to form oxidative post-translational modifications, enabling physiological redox signaling. Cardiac disease and aging are associated with oxidative stress which can impair redox signaling by altering essential cysteine thiolates. We previously found that cardiac-specific overexpression of catalase (Cat), an enzyme that detoxifies excess H2O2, protected from oxidative stress and delayed cardiac aging in mice. Using redox proteomics and systems biology, we sought to identify the cysteines that could play a key role in cardiac disease and aging. With a 'Tandem Mass Tag' (TMT) labeling strategy and mass spectrometry, we investigated differential reversible cysteine oxidation in the cardiac proteome of wild type and Cat transgenic (Tg) mice. Reversible cysteine oxidation was measured as thiol occupancy, the ratio of total available versus reversibly oxidized cysteine thiols. Catalase overexpression globally decreased thiol occupancy by ≥1.3 fold in 82 proteins, including numerous mitochondrial and contractile proteins. Systems biology analysis assigned the majority of proteins with differentially modified thiols in Cat Tg mice to pathways of aging and cardiac disease, including cellular stress response, proteostasis, and apoptosis. In addition, Cat Tg mice exhibited diminished protein glutathione adducts and decreased H2O2 production from mitochondrial complex I and II, suggesting improved function of cardiac mitochondria. In conclusion, our data suggest that catalase may alleviate cardiac disease and aging by moderating global protein cysteine thiol oxidation.
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