ArticleResearch and practice in thrombosis and haemostasis2018
Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors.
Article in Research and practice 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 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- [From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2026Review
- TFPIα inhibition by andexanet alfa is partially restored by protein S and factor V-short.Blood advances · 2026Article
- Mechanisms of thrombin inhibition by protein S and the TFPIα-fVshort-protein S complex.Biophysical journal · 2026Article
- Basic regions of factor V and tissue factor pathway inhibitor mediate heavy chain and acidic region interactions on factor V revealed by tethered chemical cleavage.Journal of thrombosis and haemostasis : JTH · 2025Article
- The role of factor V in trauma-induced coagulopathy: an observational and experimental study.Research and practice in thrombosis and haemostasis · 2025Article
- Article
- Examining downstream effects of concizumab in hemophilia A with a mathematical modeling approach.Journal of thrombosis and haemostasis : JTH · 2025Article
- The common VTE-protective G haplotype of F5 increases factor V-short, TFPI function, and risk of bleeding.Blood advances · 2025Article
- Genetic factors, risk prediction and AI application of thrombotic diseases.Experimental hematology & oncology · 2024Review
- TFPIα anticoagulant function is highly dependent on protein S in vivo.Science advances · 2024Article
- Factor V variants in bleeding and thrombosis.Research and practice in thrombosis and haemostasis · 2024Article
- Post-transcriptional control of haemostatic genes: mechanisms and emerging therapeutic concepts in thrombo-inflammatory disorders.Cardiovascular research · 2023Review
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Inhibition of platelet-surface-bound proteins during coagulation under flow I: TFPI.Biophysical journal · 2023Article
- Dysregulation of Protein S in COVID-19.Best practice & research. Clinical haematology · 2022Review
- A hydrophobic patch (PLVIVG; 1481-1486) in the B-domain of factor V-short is crucial for its synergistic TFPIα-cofactor activity with protein S and for the formation of the FXa-inhibitory complex comprising FV-short, TFPIα, and protein S.Journal of thrombosis and haemostasis : JTH · 2022Article
- Major bleeding during oral anticoagulant therapy associated with factor V activation by factor Xa.Journal of thrombosis and haemostasis : JTH · 2022Article
- Laminin G1 residues of protein S mediate its TFPI cofactor function and are competitively regulated by C4BP.Blood advances · 2022Article
- F5-Atlanta: A novel mutation in F5 associated with enhanced East Texas splicing and FV-short production.Journal of thrombosis and haemostasis : JTH · 2021Article
- F5-Atlanta: Factor V-short strikes again.Journal of thrombosis and haemostasis : JTH · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundFV-Short is a normal splice variant of Factor V (FV) having a short B domain, which exposes a high affinity-binding site for tissue factor pathway inhibitor α (TFPIα). FV-Short and TFPIα circulate in complex in plasma.
objectivesThe aim was to elucidate whether FV-Short affects TFPIα as inhibitor of coagulation FXa and to test whether the TFPIα-cofactor activity of protein S is influenced by FV-Short.
methodsRecombinant FV, wild-type FV-Short and a FV-Short thrombin-cleavage resistant variant were expressed and purified. The influence of FV and FV-Short variants and/or protein S on the FXa inhibitory activity of TFPIα was monitored both in a purified system and in a plasma-based thrombin generation assay.
resultsFV-Short had intrinsically weak TFPIα-cofactor activity but with protein S present, FV-Short yielded efficient inactivation of FXa. Protein S alone did not promote full TFPIα-activity. Intact FV was inefficient at low protein S concentrations and had 10-fold lower activity compared to FV-Short at physiological protein S levels. Activation of FV-Short by thrombin resulted in the loss of the TFPIα-cofactor activity. The synergistic TFPIα-cofactor activity of FV-Short and protein S was also demonstrated in plasma using a thrombin generation assay.
conclusionsFV-Short and protein S are highly efficient, synergistic cofactors to TFPIα in the regulation of FXa activity, whereas full length FV has lower activity. Our results suggest the formation of an efficient FXa-inhibitory complex between FV-Short, TFPIα and protein S on the surface of negatively charged phospholipids.
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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.