ArticleArteriosclerosis, thrombosis, and vascular biology2020
Cardiac Myosin Promotes Thrombin Generation and Coagulation In Vitro and In Vivo.
Article in Arteriosclerosis, thrombosis, and vascular biology, 2020. 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, 8 citations in OpenAlex.
- Characterization of the binding of skeletal muscle myosin to fibrin in trauma.The journal of trauma and acute care surgery · 2026Article
- Full-length plasma skeletal muscle myosin isoform deficiency is associated with coagulopathy in acutely injured patients.Journal of thrombosis and haemostasis : JTH · 2022Article
- Skeletal muscle myosin promotes coagulation by binding factor XI via its A3 domain and enhancing thrombin-induced factor XI activation.The Journal of biological chemistry · 2022Article
- Article
- Skeletal muscle myosin and cardiac myosin attenuate heparin's antithrombin-dependent anticoagulant activity.Journal of thrombosis and haemostasis : JTH · 2021Article
- Novel blood coagulation molecules: Skeletal muscle myosin and cardiac myosin.Journal of thrombosis and haemostasis : JTH · 2021Review
- Procoagulant activities of skeletal and cardiac muscle myosin depend on contaminating phospholipid.Blood · 2020Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
objectiveCardiac myosin (CM) is structurally similar to skeletal muscle myosin, which has procoagulant activity. Here, we evaluated CM's ex vivo, in vivo, and in vitro activities related to hemostasis and thrombosis. Approach and Results: Perfusion of fresh human blood over CM-coated surfaces caused thrombus formation and fibrin deposition. Addition of CM to blood passing over collagen-coated surfaces enhanced fibrin formation. In a murine ischemia/reperfusion injury model, exogenous CM, when administered intravenously, augmented myocardial infarction and troponin I release. In hemophilia A mice, intravenously administered CM reduced tail-cut-initiated bleeding. These data provide proof of concept for CM's in vivo procoagulant properties. In vitro studies clarified some mechanisms for CM's procoagulant properties. Thrombin generation assays showed that CM, like skeletal muscle myosin, enhanced thrombin generation in human platelet-rich and platelet-poor plasmas and also in mixtures of purified factors Xa, Va, and prothrombin. Binding studies showed that CM, like skeletal muscle myosin, directly binds factor Xa, supporting the concept that the CM surface is a site for prothrombinase assembly. In tPA (tissue-type plasminogen activator)-induced plasma clot lysis assays, CM was antifibrinolytic due to robust CM-dependent thrombin generation that enhanced activation of TAFI (thrombin activatable fibrinolysis inhibitor).
conclusionsCM in vitro is procoagulant and prothrombotic. CM in vivo can augment myocardial damage and can be prohemostatic in the presence of bleeding. CM's procoagulant and antifibrinolytic activities likely involve, at least in part, its ability to bind factor Xa and enhance thrombin generation. Future work is needed to clarify CM's pathophysiology and its mechanistic influences on hemostasis or thrombosis.
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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.