ArticleThe Journal of biological chemistry2011
Effects of extracellular DNA on plasminogen activation and fibrinolysis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 70 citations in OpenAlex.
- Thrombolytic resistance: an important factor leading to the failure of intravenous thrombolytic therapy.Journal of neurology · 2026Review
- Optimized TELIP, an Echogenic Liposomal Nano-Carrier Loaded with Alteplase for Preclinical Studies.Pharmaceutics · 2026Article
- Physiopathology of fibrinolysis in sepsis-induced disseminated intravascular coagulation: Emerging mechanisms and pharmacological targets.Annals of intensive care · 2026Review
- Cell-free DNA in sepsis: from molecular insights to clinical management.Military Medical Research · 2025Review
- Cytosolic nucleic acid sensing as driver of critical illness: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2025Review
- The toxic effects of neutrophil extracellular traps on mesenchymal stem cells.Molecular biology reports · 2024Article
- The role of neutrophils in tPA thrombolysis after stroke: a malicious troublemaker.Frontiers in immunology · 2024Review
- Review
- Platelet factor 4 limits neutrophil extracellular trap- and cell-free DNA-induced thrombogenicity and endothelial injury.JCI insight · 2023Article
- Role of Neutrophil Extracellular Traps in Health and Disease Pathophysiology: Recent Insights and Advances.International journal of molecular sciences · 2023Review
- Targeting the PAI-1 Mechanism with a Small Peptide Increases the Efficacy of Alteplase in a Rabbit Model of Chronic Empyema.Pharmaceutics · 2023Article
- Sepsis: network pathophysiology and implications for early diagnosis.American journal of physiology. Regulatory, integrative and comparative physiology · 2023Review
- Coagulation Disorders in Sepsis and COVID-19-Two Sides of the Same Coin? A Review of Inflammation-Coagulation Crosstalk in Bacterial Sepsis and COVID-19.Journal of clinical medicine · 2023Review
- A modified in vitro clot lysis assay predicts outcomes and safety in acute ischemic stroke patients undergoing intravenous thrombolysis.Scientific reports · 2021Observational
- Cell-free DNA as a marker for the outcome of end-stage renal disease patients on haemodialysis.Clinical kidney journal · 2021Article
- From Bedside to the Bench-A Call for Novel Approaches to Prognostic Evaluation and Treatment of Empyema.Frontiers in pharmacology · 2021Review
- On Neutrophil Extracellular Trap (NET) Removal: What We Know Thus Far and Why So Little.Cells · 2020Review
- Extracellular nucleic acid scavenging rescues rats from sulfur mustard analog-induced lung injury and mortality.Archives of toxicology · 2020Article
- Molecular mechanism of two nanobodies that inhibit PAI-1 activity reveals a modulation at distinct stages of the PAI-1/plasminogen activator interaction.Journal of thrombosis and haemostasis : JTH · 2020Article
- Perfluorochemical-facilitated plasminogen activator delivery to the airways: A novel treatment for inhalational smoke-induced acute lung injury.Clinical and translational medicine · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The increased levels of extracellular DNA found in a number of disorders involving dysregulation of the fibrinolytic system may affect interactions between fibrinolytic enzymes and inhibitors. Double-stranded (ds) DNA and oligonucleotides bind tissue-(tPA) and urokinase (uPA)-type plasminogen activators, plasmin, and plasminogen with submicromolar affinity. The binding of enzymes to DNA was detected by EMSA, steady-state, and stopped-flow fluorimetry. The interaction of dsDNA/oligonucleotides with tPA and uPA includes a fast bimolecular step, followed by two monomolecular steps, likely indicating slow conformational changes in the enzyme. DNA (0.1-5.0 μg/ml), but not RNA, potentiates the activation of Glu- and Lys-plasminogen by tPA and uPA by 480- and 70-fold and 10.7- and 17-fold, respectively, via a template mechanism similar to that known for fibrin. However, unlike fibrin, dsDNA/oligonucleotides moderately affect the reaction between plasmin and α(2)-antiplasmin and accelerate the inactivation of tPA and two chain uPA by plasminogen activator inhibitor-1 (PAI-1), which is potentiated by vitronectin. dsDNA (0.1-1.0 μg/ml) does not affect the rate of fibrinolysis by plasmin but increases by 4-5-fold the rate of fibrinolysis by Glu-plasminogen/plasminogen activator. The presence of α(2)-antiplasmin abolishes the potentiation of fibrinolysis by dsDNA. At higher concentrations (1.0-20 μg/ml), dsDNA competes for plasmin with fibrin and decreases the rate of fibrinolysis. dsDNA/oligonucleotides incorporated into a fibrin film also inhibit fibrinolysis. Thus, extracellular DNA at physiological concentrations may potentiate fibrinolysis by stimulating fibrin-independent plasminogen activation. Conversely, DNA could inhibit fibrinolysis by increasing the susceptibility of fibrinolytic enzymes to serpins.
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Registered trials
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.