ArticleJournal of thrombosis and haemostasis : JTH2016
Dual effect of histone H4 on prothrombin activation.
Article in Journal of thrombosis and haemostasis : JTH, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 8 citations in OpenAlex.
- Article
- Clinical significance of neutrophil extracellular traps biomarkers in thrombosis.Thrombosis journal · 2022Review
- Exploratory Investigation of the Plasma Proteome Associated with the Endotheliopathy of Trauma.International journal of molecular sciences · 2022Article
- The Pathophysiology of The Antiphospholipid Syndrome: A Perspective From The Blood Coagulation System.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/HemostasisReview
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
unlabelledEssentials Prothrombin converts slowly to thrombin upon interaction with histone H4. Histone H4 may also affect the reactivity of prothrombin toward factor Xa. Histone H4 enhances or inhibits activation by factor Xa depending on cofactor Va. The results reveal an unanticipated dual effect of histone H4 on prothrombin activation by factor Xa. SUMMARY: Background Recent studies have documented the ability of prothrombin to convert to the mature protease thrombin upon interaction with histone H4. The effect is abrogated by mutation of the catalytic Ser and requires the Gla domain. Objectives To explore the effect of histone H4 on the reactivity of prothrombin to its physiological activator factor (F) Xa, free or assembled in the prothrombinase complex. Methods The effect of histone H4 on prothrombin activation by FXa and prothrombinase is studied with kinetic assays. The potential epitope of prothrombin recognizing histone H4 is explored with electrostatic calculations using recent crystal structures. Results and Conclusions Binding of histone H4 has a dual effect on prothrombin activation by FXa that is of mechanistic significance: it enhances the reaction > 10-fold in the absence of cofactor Va, but produces complete inhibition in the presence of cofactor. Histone H4 binding to prothrombin produces very slow autoactivation independent of the coagulation cascade and promotes slow thrombin generation by FXa in the absence of phospholipids. In addition, histone H4 has a rapid and drastic inhibitory effect on prothrombin activation by prothrombinase that is likely to dominate pathophysiology.
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