Recombinant Factor Ix
Mostrando 1-12 de 40 artigos, teses e dissertações.
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1. Animais transgênicos utilizados como biorreatores
The increasing demand for production of pharmaceutical interest recombinant proteins has been the goal for the development of additional systems to its production on a large scale and reduced costs. Eukaryotes expression systems are possible alternatives to the production of recombinant protein (Leite, 2000). The secretion of these polypeptides in the milk o
Publicado em: 2008
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2. ExpressÃo de cinco diferentes proteÃnas de interesse farmacolÃgico em sementes transgÃnicas de soja [Glycine Max L. (Merril)]
Superior plants represent a convenient system for large-scale production of heterologous proteins. Its potential has been confirmed by the commercial success of such production systems, based on genetic transformation of a broad range of vegetable species, resulting in efficient production of more than 100 different heterologous proteins. A representative pe
Publicado em: 2008
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3. Replacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B.
Using the techniques of molecular biology, we made a chimeric Factor IX by replacing the first epidermal growth factor-like domain with that of Factor VII. The resulting recombinant chimeric molecule, Factor IXVIIEGF1, had at least a twofold increase in functional activity in the one-stage clotting assay when compared to recombinant wild-type Factor IX. The
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4. Expression of human factor IX in rat capillary endothelial cells: toward somatic gene therapy for hemophilia B.
In aiming to develop a gene therapy approach for hemophilia B, we expressed and characterized human factor IX in rat capillary endothelial cells (CECs). Moloney murine leukemia virus-derived retrovirus vectors that contain human factor IX cDNA linked to heterologous promoters and the neomycin-resistant gene were constructed and employed to prepare recombinan
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5. Expression of human factor IX in rabbit hepatocytes by retrovirus-mediated gene transfer: potential for gene therapy of hemophilia B.
Hemophilia B (Christmas disease) is a chromosome X-linked blood clotting disorder which results when factor IX is deficient or functionally defective. The enzyme is synthesized in the liver, and the existence of animal models for this genetic disease will permit the development of somatic gene therapy protocols aimed at transfer of the functional gene into t
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6. Expression of human factor IX in mice after injection of genetically modified myoblasts.
Hemophilia B is an X chromosome-linked recessive bleeding disorder. To develop a somatic gene therapy for this disease, we have examined whether mouse skeletal myoblasts can serve as efficient vehicles for systemic delivery of recombinant factor IX. When mouse myoblasts (C2C12) transduced with a Moloney murine leukemia virus-based vector containing the bacte
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7. In vivo hepatic gene therapy: complete albeit transient correction of factor IX deficiency in hemophilia B dogs.
Hemophilia B is a bleeding disorder caused by mutations in the factor IX gene. The disorder is X-linked recessive with a prevalence of about 1 in 30,000 Caucasian males. Factor IX is naturally synthesized in the liver and secreted into blood. Here we report the construction of recombinant adenoviral vectors containing the canine factor IX cDNA that are capab
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8. Sustained correction of bleeding disorder in hemophilia B mice by gene therapy
Mice generated by disrupting the clotting factor IX gene exhibit severe bleeding disorder and closely resemble the phenotype seen in hemophilia B patients. Here we demonstrate that a single intraportal injection of a recombinant adeno-associated virus (AAV) vector encoding canine factor IX cDNA under the control of a liver-specific enhancer/promoter leads to
The National Academy of Sciences.
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9. The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor.
The human coagulation system continuously generates very small quantities of Factor Xa and thrombin. Current evidence suggests that basal level activation of the hemostatic mechanism occurs via Factor VIIa-dependent activation of Factor X, but direct proof has not been available for the participation of tissue factor in this pathway. To examine this issue, w
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10. An alternative approach to somatic cell gene therapy.
Mouse primary skin fibroblasts were infected with a recombinant retrovirus containing human factor IX cDNA. Bulk infected cells capable of synthesizing and secreting biologically active human factor IX protein were embedded in collagen, and the implant was grafted under the epidermis. Sera from the transplanted mice contain human factor IX protein for at lea
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11. Phenotypic correction of factor IX deficiency in skin fibroblasts of hemophilic dogs.
Primary skin fibroblasts from hemophilic dogs were transduced by recombinant retrovirus (LNCdF9L) containing a canine factor IX cDNA. High levels of biologically active canine factor IX (1.0 micrograms per 10(6) cells per 24 hr) were secreted in the medium. The level of factor IX produced increased substantially if the cells were stimulated by basic fibrobla
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12. The propeptide region of clotting factor IX is a signal for a vitamin K dependent carboxylase: evidence from protein engineering of amino acid -4.
Homologous "propeptide" regions are present in a family of vitamin K-dependent mammalian proteins, including clotting factors II, VII, IX, X, protein C, protein S and bone "gla" proteins. To test the hypothesis that the propeptide is a signal for the correct gamma-carboxylation of the adjacent gamma-carboxy region, we have mutated amino acid -4 of human fact