ArticleThe Journal of biological chemistry2013
Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptides.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Structural basis for membrane binding by coagulation factors V and VIII and their specificity for phosphatidylserine-containing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- [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
- 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
- Article
- 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
- Generation of an anticoagulant aptamer that targets factor V/Va and disrupts the FVa-membrane interaction in normal and COVID-19 patient samples.Cell chemical biology · 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
- Article
- Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding.Journal of thrombosis and haemostasis : JTH · 2019Review
- Occlusion of anion-binding exosite 2 in meizothrombin explains its impaired ability to activate factor V.The Journal of biological chemistry · 2019Article
- Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors.Research and practice in thrombosis and haemostasis · 2018Article
- TFPIα interacts with FVa and FXa to inhibit prothrombinase during the initiation of coagulation.Blood advances · 2017Article
- Factor V has an anticoagulant cofactor activity that targets the early phase of coagulation.The Journal of biological chemistry · 2017Article
- Interaction of factor V B-domain acidic region with its basic region and with TFPI/TFPI2: Structural insights from molecular modeling studies.International biology review · 2017Article
- Reduced Prothrombinase Inhibition by Tissue Factor Pathway Inhibitor Contributes to the Factor V Leiden Hypercoagulable State.Blood advances · 2017Article
- Circumventing furin enhances factor VIII biological activity and ameliorates bleeding phenotypes in hemophilia models.JCI insight · 2016Article
- Platelets contain tissue factor pathway inhibitor-2 derived from megakaryocytes and inhibits fibrinolysis.The Journal of biological chemistry · 2014Article
- Biology of tissue factor pathway inhibitor.Blood · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Coagulation factor V (FV) circulates as an inactive procofactor and is activated to FVa by proteolytic removal of a large inhibitory B-domain. Conserved basic and acidic sequences within the B-domain appear to play an important role in keeping FV as an inactive procofactor. Here, we utilized recombinant B-domain fragments to elucidate the mechanism of this FV autoinhibition. We show that a fragment encoding the basic region (BR) of the B-domain binds with high affinity to cofactor-like FV(a) variants that harbor an intact acidic region. Furthermore, the BR inhibits procoagulant function of the variants, thereby restoring the procofactor state. The BR competes with FXa for binding to FV(a), and limited proteolysis of the B-domain, specifically at Arg(1545), ablates BR binding to promote high affinity association between FVa and FXa. These results provide new insight into the mechanism by which the B-domain stabilizes FV as an inactive procofactor and reveal how limited proteolysis of FV progressively destabilizes key regulatory regions of the B-domain to produce an active form of the molecule.
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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.