ArticlePloS one2016
The Role of Putative Phosphatidylserine-Interactive Residues of Tissue Factor on Its Coagulant Activity at the Cell Surface.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Thrombin concentration shapes endothelial extracellular vesicle profiles with divergent inflammatory functions.Blood advances · 2026Article
- Surface cues shape procoagulant properties of amyloidogenic microclots.Cell death & disease · 2026Review
- Article
- Soluble tissue factor generated by necroptosis-triggered shedding is responsible for thrombosis.Cell research · 2025Article
- Trained immunity causes myeloid cell hypercoagulability.Science advances · 2025Article
- Extracellular vesicle tissue factor and tissue factor pathway inhibitor are independent discriminators of sepsis-induced coagulopathy.Research and practice in thrombosis and haemostasis · 2024Article
- The Crossroads of the Coagulation System and the Immune System: Interactions and Connections.International journal of molecular sciences · 2023Review
- Tissue factor in cancer-associated thromboembolism: possible mechanisms and clinical applications.British journal of cancer · 2022Review
- Role of platelet-derived extracellular vesicles in traumatic brain injury-induced coagulopathy and inflammation.Neural regeneration research · 2022Review
- Extracellular Vesicles: A Double-Edged Sword in Sepsis.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Dietary Selenium Deficiency Facilitated Reduced Stomatin and Phosphatidylserine Externalization, Increasing Erythrocyte Osmotic Fragility in Mice.Biological trace element research · 2021Article
- Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation.RSC advances · 2021Article
- How the tissue factor-VIIa complex keeps two substrates in the loop.Journal of thrombosis and haemostasis : JTH · 2021Article
- Neutrophil extracellular traps (NETs): the role of inflammation and coagulation in COVID-19.American journal of translational research · 2021Review
- Oxidative Stress Product, 4-Hydroxy-2-Nonenal, Induces the Release of Tissue Factor-Positive Microvesicles From Perivascular Cells Into Circulation.Arteriosclerosis, thrombosis, and vascular biology · 2021Article
- Biomaterials to Prevent Post-Operative Adhesion.Materials (Basel, Switzerland) · 2020Review
- The procoagulant activity of tissue factor expressed on fibroblasts is increased by tissue factor-negative extracellular vesicles.PloS one · 2020Article
- Extracellular Vesicles Derived From Platelets, Red Blood Cells, and Monocyte-Like Cells Differ Regarding Their Ability to Induce Factor XII-Dependent Thrombin Generation.Frontiers in cell and developmental biology · 2020Article
- Direct Amplification of Tissue Factor:Factor VIIa Procoagulant Activity by Bile Acids Drives Intrahepatic Coagulation.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- Role of Cell Surface Lipids and Thiol-Disulphide Exchange Pathways in Regulating the Encryption and Decryption of Tissue Factor.Thrombosis and haemostasis · 2019Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Exposure of phosphatidylserine (PS) on the outer leaflet of the cell membrane is thought to play a critical role in tissue factor (TF) decryption. Recent molecular dynamics simulation studies suggested that the TF ectodomain may directly interact with PS. To investigate the potential role of TF direct interaction with the cell surface phospholipids on basal TF activity and the enhanced TF activity following the decryption, one or all of the putative PS-interactive residues in the TF ectodomain were mutated and tested for their coagulant activity in cell systems. Out of the 9 selected TF mutants, five of them -TFS160A, TFS161A, TFS162A, TFK165A, and TFD180A- exhibited a similar TF coagulant activity to that of the wild-type TF. The specific activity of three mutants, TFK159A, TFS163A, and TFK166A, was reduced substantially. Mutation of the glycine residue at the position 164 markedly abrogated the TF coagulant activity, resulting in ~90% inhibition. Mutation of all nine lipid binding residues together did not further decrease the activity of TF compared to TFG164A. A similar fold increase in TF activity was observed in wild-type TF and all TF mutants following the treatment of THP-1 cells with either calcium ionomycin or HgCl2, two agents that are commonly used to decrypt TF. Overall, our data show that a few select TF residues that are implicated in interacting with PS contribute to the TF coagulant activity at the cell surface. However, our data also indicate that TF regions outside of the putative lipid binding region may also contribute to PS-dependent decryption of TF.
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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.