ArticleJournal of thrombosis and haemostasis : JTH2019
The roles of factor Va and protein S in formation of the activated protein C/protein S/factor Va inactivation complex.
Article in Journal of thrombosis and haemostasis : JTH, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- The common VTE-protective G haplotype of F5 increases factor V-short, TFPI function, and risk of bleeding.Blood advances · 2025Article
- Pro-Coagulant Lipids in Physiological Ratios Found in the Activated Platelet Membrane Do Not Impact Clot Structure or Fibrinolysis in Purified Assays.Journal of blood medicine · 2025Article
- 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
- Impaired factor V-related anticoagulant mechanisms and deep vein thrombosis associated with A2086D and W1920R mutations.Blood advances · 2023Article
- Comparative evaluation of reagents for measuring protein S activity: possibility of harmonization.International journal of hematology · 2021Article
- The roles of factor Va and protein S in formation of the activated protein C/protein S/factor Va inactivation complex.Journal of thrombosis and haemostasis : JTH · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
backgroundActivated protein C (APC)-mediated inactivation of factor (F)Va is greatly enhanced by protein S. For inactivation to occur, a trimolecular complex among FVa, APC, and protein S must form on the phospholipid membrane. However, direct demonstration of complex formation has proven elusive.
objectivesTo elucidate the nature of the phospholipid-dependent interactions among APC, protein S, and FVa.
methodsWe evaluated binding of active site blocked APC to phospholipid-coated magnetic beads in the presence and absence of protein S and/or FVa. The importance of protein S and FV residues were evaluated functionally.
resultsActivated protein C alone bound weakly to phospholipids. Protein S mildly enhanced APC binding to phospholipid surfaces, whereas FVa did not. However, FVa together with protein S enhanced APC binding (>14-fold), demonstrating formation of an APC/protein S/FVa complex. C4b binding protein-bound protein S failed to enhance APC binding, agreeing with its reduced APC cofactor function. Protein S variants (E36A and D95A) with reduced APC cofactor function exhibited essentially normal augmentation of APC binding to phospholipids, but diminished APC/protein S/FVa complex formation, suggesting involvement in interactions dependent upon FVa. Similarly, FVa
conclusionsFVa plays a central role in the formation of its inactivation complex. Furthermore, membrane proximal interactions among FVa, APC, and protein S are essential for its cofactor function.
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Registered trials
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