ArticleThe Journal of biological chemistry
Regulation of factor V and factor V-short by TFPIα: Relationship between B-domain proteolysis and binding.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
- [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
- Modeling the role of platelet-released polyphosphates in tissue factor-initiated coagulation under flow.Research and practice in thrombosis and haemostasis · 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
- A Novel Human Anti-FV mAb as a Potential Tool for Diagnostic and Coagulation Inhibitory Approaches.International journal of molecular sciences · 2025Article
- 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
- Mathematical modeling identifies clotting factor combinations that modify thrombin generation in normal and factor VIII-, IX-, or XI-deficient blood.Research and practice in thrombosis and haemostasis · 2024Article
- Structural architecture of the acidic region of the B domain of coagulation factor V.Journal of thrombosis and haemostasis : JTH · 2024Article
- Factor V variants in bleeding and thrombosis.Research and practice in thrombosis and haemostasis · 2024Article
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Impaired factor V-related anticoagulant mechanisms and deep vein thrombosis associated with A2086D and W1920R mutations.Blood advances · 2023Article
- Inhibition of platelet-surface-bound proteins during coagulation under flow I: TFPI.Biophysical journal · 2023Article
- Cryo-EM structures of coagulation factors.Research and practice in thrombosis and haemostasis · 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
- Factor V east Texas variant causes bleeding in a three-generation family.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
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Coagulation factor V (FV) plays an anticoagulant role but serves as a procoagulant cofactor in the prothrombinase complex once activated to FVa. At the heart of these opposing effects is the proteolytic removal of its central B-domain, including conserved functional landmarks (basic region, BR; 963-1008 and acidic region 2, AR2; 1493-1537) that enforce the inactive FV procofactor state. Tissue factor pathway inhibitor α (TFPIα) has been associated with FV as well as FV-short, a physiologically relevant isoform with a shortened B-domain missing the BR. However, it is unclear which forms of FV are physiologic ligands for TFPIα. Here, we characterize the binding and regulation of FV and FV-short by TFPIα via its positively charged C-terminus (TFPIα-BR) and examine how bond cleavage in the B-domain influences these interactions. We show that FV-short is constitutively active and functions in prothrombinase like FVa. Unlike FVa, FV-short binds with high affinity (K
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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.