ArticleJournal of the American Heart Association2025
Enhancement of Tenecteplase Thrombolytic Actions Ex Vivo and In Vivo by Deoxyribonuclease I.
Article in Journal of the American Heart Association, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Immune response to DNA and RNA: structural insights, molecular mechanisms, and therapeutic targeting.Molecular biomedicine · 2026Review
- Thrombolytic resistance: an important factor leading to the failure of intravenous thrombolytic therapy.Journal of neurology · 2026Review
- A 'Tangled Web' in the CNS: unraveling neutrophil extracellular traps in neurological disorders.Molecular neurodegeneration · 2026Review
- Beyond Direct Fibrinolysis: Novel Approaches to Thrombolysis.Pharmaceuticals (Basel, Switzerland) · 2025Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundWe aimed to investigate the phenomenon of thrombolysis resistance in tenecteplase and its underlying causes and evaluate whether DNase-1 (deoxyribonuclease I) targeting neutrophil extracellular traps (NETs) could enhance the thrombolytic efficiency of tenecteplase.
methodsFresh thrombi were retrieved from 25 patients with acute ischemic stroke via endovascular thrombectomy, and 50 artificial blood clots were generated by recalcifying whole blood from healthy donors for ex vivo thrombolysis experiments by tenecteplase±DNase-1. Fibrinolytic resistance was analyzed via histology and scanning electron microscope. Thrombolytic rates were calculated. NETs were observed with immunofluorescence colocalization of NET markers. In vivo experiment was performed in mice with photothrombotic stroke, to evaluate the effects of tenecteplase+DNase-1 versus tenecteplase on cerebral blood flow, infarct volume, and neurological deficits.
resultsThe NET-rich outer shell remained after tenecteplase thrombolysis in thrombi and blood clots. Additive DNase-1 enhanced the thrombolytic efficiency of tenecteplase, resulting in faster thrombolytic rates and lower weights of thrombus (31% versus 48%;
conclusionsThe shell structure of a thrombus, particularly the NETs, may play an important role in fibrinolytic resistance to tenecteplase. Additive DNase-1 may enhance the thrombolytic efficiency of tenecteplase.
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