ArticleThe Journal of biological chemistry2019
Molecular interaction site on procoagulant myosin for factor Xa-dependent prothrombin activation.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- 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
- N-Methyl-3,4-methylendioxymethamphetamine (MDMA)-related coagulopathy and rhabdomyolysis: A case series and literature review.Research and practice in thrombosis and haemostasis · 2020Article
- Plasma skeletal muscle myosin phenotypes identified by immunoblotting are associated with pulmonary embolism occurrence in young adults.Thrombosis research · 2020Article
- Cardiac Myosin Promotes Thrombin Generation and Coagulation In Vitro and In Vivo.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Skeletal muscle myosin has potent procoagulant activity that is based on its ability to enhance thrombin generation due to binding coagulation factors Xa and Va and accelerating prothrombin activation. A well-studied myosin inhibitor that binds to myosin's neck region inhibits myosin-dependent prothrombin activation. Hence, to identify a potential binding site(s) on skeletal muscle myosin for factor Xa, 19 peptides (25-40 residues) representing the neck region, which consists of a regulatory light chain, an essential light chain, and a heavy chain (HC), were screened for inhibition of myosin-supported prothrombin activation. Peptide HC796-835 comprising residues 796-835 of the heavy chain strongly inhibited myosin-enhanced prothrombin activation by factors Xa and Va (50% inhibition at 1.2 μm), but it did not inhibit phospholipid vesicle-enhanced prothrombin activation. Peptide inhibition studies also implicated several myosin light chain sequences located near HC796-835 as potential procoagulant sites. A peptide comprising HC796-835's C-terminal half, but not a peptide comprising its N-terminal half, inhibited myosin-enhanced prothrombin activation (50% inhibition at 1.2 μm). This inhibitory peptide (HC816-837) did not inhibit phospholipid-enhanced prothrombin activation, indicating its specificity for inhibition of myosin-dependent procoagulant mechanisms. Binding studies showed that purified factor Xa was bound to immobilized peptides HC796-835 and HC816-837 with apparent
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