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hemophilia a/carbohydrate
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Comparison of factor VIII transgenes bioengineered for improved expression in gene therapy of hemophilia A.
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Successful gene therapy of hemophilia A depends on the sustained expression of therapeutic levels of factor VIII (fVIII). Because of mRNA instability, interactions with resident endoplasmic reticulum (ER) chaperones, and the requirement for carbohydrate-facilitated transport from the ER to the Golgi
Characterization of three abnormal factor IX variants (Bm Lake Elsinore, Long Beach, and Los Angeles) of hemophilia-B. Evidence for defects affecting the latent catalytic site.
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Abnormal factor IX variant proteins were isolated from the plasmas of three unrelated severe hemophilia-B families that had been previously shown to contain functionally impaired molecules immunologically similar to normal factor IX. The families studied were: (1) a patient with markedly prolonged
Low-dose rituximab in the treatment of acquired haemophilia.
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OBJECTIVE
Acquired haemophilia is a rare hemorrhagic disease caused by inhibitory autoantibodies against coagulation factor VIII. Rituximab has become a popular choice for immunosuppressive therapy in acquired haemophilia, almost with the same schedule of 375 mg/m(2) per week for 4-6 doses. While
Elucidation of N-linked oligosaccharide structures of recombinant human factor VIII using fluorophore-assisted carbohydrate electrophoresis.
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Characterization of the carbohydrate moiety is a critical measure of manufacturing process consistency of recombinant human Factor VIII (rFVIII) in Chinese-hamster ovary (CHO) cells. FVIII, a large (300 kDa) glycoprotein, is employed therapeutically for the correction of haemophilia A. While
Molecular defects in haemophilia A and von Willebrand's disease.
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A model is proposed for the synthesis of the factor VII/von Willebrand factor protein. The defect(s) in von Willebrand's disease are related to abnormalities of the protein subunit and/or its carbohydrate content, while in haemophilia the abnormality is related to a deficiency or abnormality of the
An Arg/Ser substitution in the second epidermal growth factor-like module of factor IX introduces an O-linked carbohydrate and markedly impairs activation by factor XIa and factor VIIa/Tissue factor and catalytic efficiency of factor IXa.
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Factor IXR94S is a naturally occurring hemophilia B defect, which results from an Arg 94 to Ser mutation in the second epidermal growth factor (EGF)-like module of factor IX. Recombinant factor IXR94S was activated by factor XIa/calcium with an approximately 50-fold reduced rate and by factor
Diabetes mellitus and acquired haemophilia: new association?
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Diabetes mellitus encompasses a group of highly prevalent carbohydrate metabolic disorders with an increasing incidence. Some subtypes are thought to be associated with other immune-mediated diseases. Acquired haemophilia on the other hand is a quite rare autoimmune disease that is thought to be
Fibrinogen St. Louis: a new inherited fibrinogen variant, coincidentally associated with hemophilia A.
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A patient with classical hemophilia (factor VIII deficiency) was found to have a new abnormal fibrinogen (fibrinogen St. Louis). Other family members exhibited either defect alone. Fibrinogen St. Louis was inherited as an autosomal dominant and was not associated with clinical bleeding. When
Manufacturing challenges in the commercial production of recombinant coagulation factor VIII.
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Advances in gene technology have led to the development of a method to manufacture recombinant coagulation Factor VIII (rFVIII) for haemophilia A. Because rFVIII is a large and complex protein, its commercialization has required that many challenges in manufacturing, purification and processing be
Anxiety-Related Bleeding and Thrombosis.
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Anxiety, a normal response to stressful situations, is characterized by increased levels of factor VIII, fibrinogen, and von Willebrand factor, and by enhanced platelet aggregability. One would expect acute anxiety to be a prothrombotic state, but since acute mental stress induces tissue plasminogen
Posttranslational modifications of recombinant myotube-synthesized human factor IX.
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Recent data demonstrate that the introduction into skeletal muscle of an adeno-associated viral (AAV) vector expressing blood coagulation factor IX (F.IX) can result in long-term expression of the transgene product and amelioration of the bleeding diathesis in animals with hemophilia B. These data
Isolation and characterization of canine factor IX.
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Canine plasma factor IX was purified to homogeneity by a combination of barium citrate precipitation and three-step column chromatographies of DEAE sepharose, heparin agarose and a monoclonal antifactor IX antibody-linked agarose. Canine factor IX has an apparent molecular size of 61 kDa, which is
Removal of Mannose-Ending Glycan at Asn2118 Abrogates FVIII Presentation by Human Monocyte-Derived Dendritic Cells.
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The development of an immune response against therapeutic factor VIII is the major complication in hemophilia A patients. Oligomannose carbohydrates at N239 and/or N2118 on factor VIII allow its binding to the macrophage mannose receptor expressed on human dendritic cells, thereby leading to factor
Characterization of recombinant factor VIII and a recombinant factor VIII deletion mutant using a rabbit immunogenicity model system.
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The use of factor VIII prepared genetically engineered cell lines (rFVIII) may avoid some of the problems inherently associated with administering plasma-derived factor VIII (pdFVIII) concentrates to hemophilia A patients. Although rFVIII may represent an improvement over traditional therapeutics,
Purification and characterization of rabbit factor IX and its existence as a two-chain factor IX alpha in circulating plasma.
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The long term objective of this study is to immunodeplete rabbits of factor IX as a means of developing a rabbit model for hemophilia B for use in studies of tissue factor-dependent blood coagulation. As a first step, we have purified rabbit factor IX by basically two different methods: (1)
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