Recombinant chymase inhibits fibrinolysis induced by endogenous plasmin in clotted human blood
These <i>in vitro</i> experiments with human whole blood suggest that mast cell-derived chymase impairs blood clot resolution by interfering with the fibrinolytic activity of endogenous intra-clot plasmin. Our findings provide evidence that recombinant mast cell chymase interferes with endogenous plasmin activity in human whole blood clots <i>in vitro</i> and support the potential of chymase inhibitors, such as fulacimstat, as fibrinolytic agents for thrombotic and thromboembolic disorders.
Authors
- Hanna Tinel (ORCID: https://orcid.org/0000-0002-5518-384X)
- Stefan Heitmeier
- Pedro D’Orléans-Juste (ORCID: https://orcid.org/0000-0002-9863-3548)
- Patrick P. McDonald (ORCID: https://orcid.org/0000-0003-4862-2784)
- Tienush Rassaf (ORCID: https://orcid.org/0000-0001-8001-0265)
- Catherine Lapointe (ORCID: https://orcid.org/0000-0002-0636-7781)
- Laurence Vincent (ORCID: https://orcid.org/0000-0001-5373-118X)
- Christos Rammos (ORCID: https://orcid.org/0000-0003-3468-9945)
- Maria Köllnberger
Institutions
- University of North Carolina at Chapel Hill (US)
- University of North Carolina Health Care (US)
- Université de Sherbrooke (CA)
- West German Heart and Vascular Center Essen (DE)
- University of Duisburg-Essen (DE)
- Bayer (Germany) (DE)
Publication Details
- Journal
- Frontiers in Immunology
- Published
- 2025-04-17
- DOI
- https://doi.org/10.3389/fimmu.2025.1511990
- Primary Topic
- Mast cells and histamine
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Bayer