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Structure and pharmacokinetics/pharmacodynamics of the anticoagulant tetradecasaccharide oHG-14 as an intrinsic tenase inhibitor.
Thromb Res
August 2024
School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan 430074, China.
The intrinsic tenase complex (iXase) is an attractive antithrombotic target to treat or prevent pathological thrombosis with negligible bleeding risk. Fucosylated glycosaminoglycan (FG) is a promising anticoagulant by inhibiting iXase. A depolymerized FG (dHG-5) as an anticoagulant has been approved for clinical trials.
View Article and Find Full Text PDFKinetics and regulation of coagulation factor X activation by intrinsic tenase on phospholipid membranes.
J Theor Biol
April 2024
National Medical and Research Center of Pediatric Hematology, Oncology and Immunology Named After Dmitry Rogachev, 1 Samory Mashela St, Moscow, 117198, Russia; Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, 4 Kosygina St, Moscow, 119991, Russia; Faculty of Physics, Lomonosov Moscow State University, 1/2 Leninskie Gory, Moscow, 119991, Russia. Electronic address:
Background: Factor X activation by the phospholipid-bound intrinsic tenase complex is a critical membrane-dependent reaction of blood coagulation. Its regulation mechanisms are unclear, and a number of questions regarding diffusional limitation, pathways of assembly and substrate delivery remain open.
Methods: We develop and analyze here a detailed mechanism-driven computer model of intrinsic tenase on phospholipid surfaces.
Factor VIII A3 domain residues 1793-1795 represent a factor IXa-interactive site in the tenase complex.
Biochim Biophys Acta Gen Subj
August 2023
Department of Pediatrics, Nara Medical University, Kashihara, Nara 634-8522, Japan.
Background: Factor (F)VIII functions as a cofactor in the tenase complex responsible for conversion of FX to FXa by FIXa. Earlier studies indicated that one of the FIXa-binding sites is located in residues 1811-1818 (crucially F1816) of the FVIII A3 domain. A putative, three-dimensional structure model of the FVIIIa molecule suggested that residues 1790-1798 form a V-shaped loop, and juxtapose residues 1811-1818 on the extended surface of FVIIIa.
View Article and Find Full Text PDFUnraveling the Reaction Mechanism of Russell's Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?
J Chem Inf Model
July 2023
LAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, Porto 4169-007, Portugal.
Snake venom metalloproteinases (SVMPs) are important drug targets against snakebite envenoming, the neglected tropical disease with the highest mortality worldwide. Here, we focus on Russell's viper (), one of the "big four" snakes of the Indian subcontinent that, together, are responsible for ca. 50,000 fatalities annually.
View Article and Find Full Text PDFPreclinical studies of a factor X activator and a phase 1 trial for hemophilia patients with inhibitors.
J Thromb Haemost
June 2023
State Key Laboratory of Experimental Hematology, National Clinical Research Center for Blood Diseases, Haihe Laboratory of Cell Ecosystem, Institute of Hematology & Blood Diseases Hospital, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin Key Laboratory of Gene Therapy for Blood Diseases, Chinese Academy of Medical Sciences Key Laboratory of Gene Therapy for Blood Diseases, Tianjin, China. Electronic address:
Background: Bleeding episodes in hemophiliacs with inhibitors are difficult to control. Staidson protein-0601 (STSP-0601), a specific factor (F)X activator purified from the venom of Daboia russelii siamensis, has been developed.
Objectives: We aimed to investigate the efficacy and safety of STSP-0601 in preclinical and clinical studies.
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