ArticleThrombosis and haemostasis2018
Neutrophil-Mediated Proteolysis of Thrombospondin-1 Promotes Platelet Adhesion and String Formation.
Article in Thrombosis and haemostasis, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- N-terminal thrombospondin-1 enhances muscle function and tissue-specific metabolic adaptation in response to exercise and cold exposure.Experimental & molecular medicine · 2026Article
- ADAMTS4 mediates LPS-induced cardiac injury and myocardial fibrosis through proteolytic cleavage of TSP1.Clinical and translational medicine · 2026Article
- Extracellular Trap-Related Genes as Potential Diagnostic Biomarkers for Endometriosis.International journal of women's health · 2025Article
- The many roles of cathepsins in restenosis.Heliyon · 2024Article
- The Role of Neutrophil Extracellular Traps (NETs) in the Pathogenesis of Systemic Lupus Erythematosus and Antiphospholipid Syndrome.International journal of molecular sciences · 2023Article
- Improving cancer immunotherapyActa pharmaceutica Sinica. B · 2023Article
- Identification of genetic polymorphisms in unexplained recurrent spontaneous abortion based on whole exome sequencing.Annals of translational medicine · 2022Article
- Factors Associated with Platelet Activation-Recent Pharmaceutical Approaches.International journal of molecular sciences · 2022Review
- Inflammatory Mediators of Platelet Activation: Focus on Atherosclerosis and COVID-19.International journal of molecular sciences · 2021Review
- The Neutrophil Secretome as a Crucial Link between Inflammation and Thrombosis.International journal of molecular sciences · 2021Review
- Inhibition of thrombospondin-1 reduces glutathione activity and worsens acute liver injury during acetaminophen hepatotoxicity in mice.Toxicology and applied pharmacology · 2020Article
- COVID-19 update: Covid-19-associated coagulopathy.Journal of thrombosis and thrombolysis · 2020Review
- Tissue-level inflammation and ventricular remodeling in hypertrophic cardiomyopathy.Journal of thrombosis and thrombolysis · 2020Review
- Serum Exosomal Proteins F9 and TSP-1 as Potential Diagnostic Biomarkers for Newly Diagnosed Epilepsy.Frontiers in neuroscience · 2020Article
- Nanoparticle exposure driven circulating bioactive peptidome causes systemic inflammation and vascular dysfunction.Particle and fibre toxicology · 2019Article
Corrections and comments
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Authors and funding
16 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thrombospondin-1 (TSP-1) is primarily expressed by platelets and endothelial cells (ECs) and rapidly released upon their activation. It functions in haemostasis as a bridging molecule in platelet aggregation, by promoting platelet adhesion to collagen and by protecting von Willebrand factor strings from degradation. In blood of patients undergoing surgery and in co-cultures of neutrophils with platelets or ECs, we observed proteolysis of the 185 kDa full-length TSP-1 to a 160-kDa isoform. We hypothesized that TSP-1 processing may alter its haemostatic properties. Selective enzyme inhibitors in co-cultures revealed that neutrophil proteases elastase and cathepsin G mediate TSP-1 processing. The cut site of cathepsin G was mapped to TSP-1 amino acids R237/T238 by Edman sequencing. Formation of neutrophil extracellular traps protected TSP-1 from complete degradation and promoted controlled processing to the 160-kDa isoform. Haemostatic properties were tested by platelet aggregation, adhesion, coagulation and string formation under flow. Platelets from TSP-1 deficient mice did not differ from wild-type in platelet aggregation but showed severe impairment of platelet adhesion to collagen and string formation under flow. Reconstitution experiments revealed that the 160-kDa TSP-1 isoform was markedly more potent than the 185-kDa full-length molecule in restoring function. Thus, TSP-1 processing by neutrophil proteases yields a 160-kDa isoform which shows enhanced potency to promote platelet adhesion and string formation. This finding reveals a novel mechanism of neutrophil-mediated thrombus formation and provides first evidence for the impact of TSP-1 proteolysis on its haemostatic properties.
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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.