ArticleResearch and practice in thrombosis and haemostasis2022
A novel ex vivo approach for measuring plasminogen activation upon established plasma clots.
Article in Research and practice in thrombosis and haemostasis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Cytosine base editing of LPA in transgenic mice averts large deletions.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Mapping the Mutational Landscape for Streptokinase Binding to Plasminogen.bioRxiv : the preprint server for biology · 2026Article
- Reversing PAI-1 deficiency in blood using mRNA lipid nanoparticles.Molecular therapy. Methods & clinical development · 2025Article
- Halo fluorescence fibrinolysis test: a novel quantitative assay to evaluate fibrinolysis on established plasma clots.Research and practice in thrombosis and haemostasis · 2025Article
- Tranexamic acid in a mouse model of cerebral amyloid angiopathy: setting the stage for a novel stroke treatment approach.Research and practice in thrombosis and haemostasis · 2023Article
- A novel ex vivo approach for measuring plasminogen activation upon established plasma clots.Research and practice in thrombosis and haemostasis · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Background: The fibrinolytic system plays a critical role in maintaining hemostasis. Central to fibrinolysis is the degradation of fibrin by plasmin, produced in the circulation following the activation of plasminogen by plasminogen activators (PAs). Accurately measuring the plasminogen activation rate is vital for the understanding of fibrinolytic processes, particularly in the context of thrombolysis. Yet, due to the insoluble nature of fibrin, in vitro and ex vivo investigations of PA-mediated plasminogen activation have proven challenging. As researchers frequently adopt soluble fibrinogen fragments and/or alter the experimental system beyond what is physiologically relevant, they limit the validation and interpretation of their findings. Here, we present a novel, high-throughput assay for measuring plasminogen activation rates on natural, plasma-derived fibrin that optimally simulates in vivo conditions. Method: Human plasma was used as the source of plasmin(ogen) and fibrin(ogen). "Halo-shaped" plasma clots were produced in a 96-well plate using a thrombin-containing clotting mixture, ensuring that an optically compatible and plasma-free center is maintained in each well. Subsequent additions of a plasmin chromogenic substrate and different PAs were followed by absorbance measurements over time to extract the corresponding enzyme kinetics information. Results and Discussion: Validation experiments demonstrated the capability of our approach to accurately model fibrin-dependent and -independent plasminogen activation as well as sensitively detect variations in plasminogen and fibrinogen plasma levels. Conclusion: This assay allows a straightforward, yet powerful, measurement of plasminogen activation rates on established plasma clots, with the capability of properly assessing fibrin- and non-fibrin-dependent plasminogen activation by various therapeutic PAs.
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