Academic literature on the topic 'Factor VIII (FVIII)'
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Journal articles on the topic "Factor VIII (FVIII)":
Yada, Koji, Kenichi Ogiwara, Masaru Shibata, Midori Shima, and Keiji Nogami. "Effects of anti-factor VIII inhibitor antibodies on factor VIIa/tissue factor-catalysed activation and inactivation of factor VIII." Thrombosis and Haemostasis 105, no. 06 (2011): 989–98. http://dx.doi.org/10.1160/th10-12-0781.
Yada, Koji, Keiji Nogami, Kenichi Ogiwara, Katsumi Nishiya, Masahiro Takeyama, and Midori Shim. "Effects of Anti-FVIII Inhibitors On Factor VIIa/Tissue Factor-Catalyzed Activation and Inactivation of Factor VIII." Blood 114, no. 22 (November 20, 2009): 3169. http://dx.doi.org/10.1182/blood.v114.22.3169.3169.
Nakajima, Yuto, Koji Yada, Keiji Nogami, and Midori Shima. "A Novel Mechanism of Factor VIIa/Tissue Factor (TF)-Catalyzed Activation and Inactivation of B-Domain-Deleted Factor VIII in the Early Initiation Phases of Coagulation." Blood 132, Supplement 1 (November 29, 2018): 1162. http://dx.doi.org/10.1182/blood-2018-99-115645.
Ogiwara, Kenichi, Keiji Nogami, Masahiro Okuda, Katsumi Nishiya, Masahiro Takeyama, and Midori Shima. "Interactions of Factor VIII with Tissue Factor Contributes to the Acceleration of Factor Xa Generation in the Initiation Phase of Blood Coagulation." Blood 114, no. 22 (November 20, 2009): 3177. http://dx.doi.org/10.1182/blood.v114.22.3177.3177.
Ogiwara, Kenichi, Keiji Nogami, Tetsuhiro Soeda, Tomoko Matsumoto, Katsumi Nishiya, and Midori Shima. "Mechanisms of Factor VIII Activation by Recombinant Factor VIIa Analog through Tissue Factor-Independent Manner." Blood 112, no. 11 (November 16, 2008): 1028. http://dx.doi.org/10.1182/blood.v112.11.1028.1028.
Meeks, Shannon, Ernest T. Parker, Amy L. Dunn, John F. Healey, and Pete Lollar. "Proteolytically Inactivatable Factor VIII is Less Immunogenic than Factor VIII in a Murine Hemophilia A Model." Blood 114, no. 22 (November 20, 2009): 27. http://dx.doi.org/10.1182/blood.v114.22.27.27.
Soeda, Tetsuhiro, Keiji Nogami, Tomoko Matsumoto, Kenichi Ogiwara, Katsumi Nishiya, and Midori Shima. "Tissue Factor-Dependent Activation of Factor VIII by Factor VIIa in the Early Phase of Blood Coagulation." Blood 112, no. 11 (November 16, 2008): 1036. http://dx.doi.org/10.1182/blood.v112.11.1036.1036.
Messer, Amanda S., Barbara Ulmasov, Yogesh Kumar, Kanagasabai Vadivel, Degang Zhong, Philip Fay, and S. Paul Bajaj. "Epitope Mapping of a Monoclonal Antibody to Factor VIII That Inhibits Factor IXa:Factor VIIIa Interaction and Thrombin Activation of Factor VIII." Blood 118, no. 21 (November 18, 2011): 1177. http://dx.doi.org/10.1182/blood.v118.21.1177.1177.
Zakas, Philip, Kristopher Knight, Ernest T. Parker, H. Trent Spencer, Eric Gaucher, and Christopher B. Doering. "Bioengineering Coagulation Factor VIII through Ancestral Protein Reconstruction." Blood 126, no. 23 (December 3, 2015): 123. http://dx.doi.org/10.1182/blood.v126.23.123.123.
Radtke, Klaus-Peter, Dean Chamberlain, John H. Griffin, and Andrew J. Gale. "Whole Blood Thromboelastogram Assays Demonstrate Prolonged Factor VIIIa Potency for Recombinant Disulfide Bond-Stabilized Factor VIII Variants." Blood 104, no. 11 (November 16, 2004): 2976. http://dx.doi.org/10.1182/blood.v104.11.2976.2976.
Dissertations / Theses on the topic "Factor VIII (FVIII)":
Kalandadze, Vakhtang. "Phenotypic characterization of immune cell populations in homeostatic and FVIII-challenged severe HA mice." Doctoral thesis, Università del Piemonte Orientale, 2022. http://hdl.handle.net/11579/142998.
Tolley, Caroline. "Co-expression of Factor VIII with anti-FVIII Camelid antibody ligands : effect on expression levels of bio-therapeutic FVIII." Thesis, University of Kent, 2015. https://kar.kent.ac.uk/54757/.
Sefiane, Thibaud. "Vers une meilleure compréhension des mécanismes moléculaires régissant l'action des thérapies non-substitutives dans l'hémophilie A et comparaison avec le facteur VIII." Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASQ004.
Hemophilia A is a bleeding disorder linked to a deficiency in plasma coagulation protein FVIII. For a long time, the standard treatment consisted in replacing the missing FVIII with exogenous FVIII, but the emergence of inhibitors against FVIII has made replacement therapies ineffective in 30% of patients. Recently, the bispecific anti-FIX/anti-FX antibody emicizumab, which mimics the cofactor action of FVIII, was approved. The aim of my thesis was to study how emicizumab compares with FVIII in terms of its molecular and functional properties.First, we analyzed the case of a patient undergoing prophylaxis with emicizumab. After 6 months of treatment, the patient developed hemarthrosis and anti-emicizumab antibodies were identified, leading to a decrease of emicizumab plasma concentration without directly affecting its activity. Further analysis revealed the first clinical case treated by emicizumab with antibodies causing accelerated clearance of emicizumab.In a second part, we investigated the impact of FVIII/FVIII-Fc vs emicizumab on clot formation, stabilization and structure. The previously reported in vitro studies were limited by the absence of cellular components, therefore leading to contradicting results.We developed a murine bleeding model which demonstrated that emicizumab alters the kinetics of clot formation, which could explain the bleeding observed in 5% of patients treated with emicizumab. Microscopic analysis of clot structure indicates that FVIII and FVIII-Fc have a similar impact on the clot structure, while emicizumab, with its unique mode of action, induces morphological differences.Finally, we investigated the potential use of murine bleeding models to determine equivalence between non-factor therapies (emicizumab and anti-TFPI) and FVIII. Indeed, the important question linked to the use of these therapies concerns the determination of possible equivalence with FVIII. As the data from in vitro activity tests did not answer this question, we proposed to assess this equivalence in vivo using a panel of murine bleeding models. The results showed that equivalence varied according to the severity of the model and led us to propose that absolute equivalence was unrealistic. Indeed, it would be more realistic to talk about an equivalence range in terms of FVIII activity
Bittar, Luis Fernando 1980. "Avaliação de alterações moleculares nos genes do FVW e da ADAMTS 13 e sua correlação com os niveis plasmaticos de FVIII e FVW em pacientes com trombose venenosa profunda." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/310145.
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Ciencias Medicas
Made available in DSpace on 2018-08-13T01:42:43Z (GMT). No. of bitstreams: 1 Bittar_LuisFernando_M.pdf: 1309049 bytes, checksum: 8d7bbcbc4a659300d128bc58336cbb88 (MD5) Previous issue date: 2009
Resumo: Níveis elevados de fator VIII (FVIII) são um fator de risco independente e prevalente para trombose venosa profunda (TVP), e tem influência do FvW. A ADAMTS13 é responsável pela modulação do tamanho molecular do FvW, clivando os multímeros de altíssimo peso molecular. Alterações moleculares no gene da ADAMTS13 têm correlação com sua atividade. Neste estudo avaliamos a prevalência do polimorfismo A4751G no gene do FvW (região de ligação com a ADAMTS13), os polimorfismos C1797T e C1852G e a mutação C4006T no gene da ADAMTS13 em 435 pacientes com TVP (156M/279F; idade mediana=37) e 580 controles (170M/410F, idade mediana=35). Investigamos a relação entre os genótipos e a dosagem de FVIII e FvW no plasma e o risco de TVP. A dosagem de FVIII:C foi realizada por método coagulométrico de um estágio, e as dosagens de FVIII:Ag e FvW:Ag por método imunoenzimático. As alterações moleculares foram determinadas por PCR e digestão com enzimas específicas, ou SSCP e sequenciamento para confirmação. Pacientes com TVP mostraram níveis significantemente aumentados de FVIII:C (203.7 UI/dl vs. 127 UI/dl; p<0.001), FVIII:Ag (109.6 UI/dl vs. 82.4 UI/dl; p<0.001) e FvW:Ag (154.2 UI/dl vs. 108 UI/dl; p<0.001) quando comparados com o grupo controle. Não houve diferença significativa entre os grupos na prevalência das alterações moleculares estudadas. Os indivíduos com genótipo AG (FvW A4751G) apresentavam níveis significativamente reduzidos de FVIII:C (p=0.04). Embora também tenha demonstrado uma discreta associação com níveis diminuídos de FvW:Ag, esta não foi estatisticamente significativa (p= 0.07). Os indivíduos com genótipo CG (ADAMTS13 C1852G) apresentavam níveis significativamente aumentados de FVIII:Ag (p=0.05) e FvW:Ag (p= 0.01). Apesar da relação com diminuição do FVIII o polimorfismo A4751G não mostrou um efeito protetor para TVP. O polimorfismo ADAMTS13 C1852G está associado à diminuição desta metaloprotease, e sua associação com níveis aumentados de FVIII:Ag e FvW:Ag neste estudo favorece essa hipótese.
Abstract: Elevated levels of factor VIII (FVIII) are a prevalent and independent risk factor for deep venous thrombosis (DVT), and are affected by von Willebrand factor (vWF) levels. ADAMTS13 is responsible for the modulation of the molecular size of vWF, cleaving the ultra large multimers. Mutations and polymorphisms in the ADAMTS13 gene are related with its activity. This study evaluated the prevalence of polymorphism A4751G in the vWF gene, polymorphisms C1797T, C1852G and the mutation C4006T in the ADAMTS13 gene in 435 patients with DVT and 580 healthy controls. Subsequently, we investigated the relationship between the genotypes and plasma levels of FVIII and vWF and DVT risk. FVIII:C was measured by a one-stage clotting method, and FVIII:Ag and vWF:Ag were measured by chromogenic method. The molecular changes were determined by restriction endonucleases or single strand conformation polymorphism followed by sequencing. Statistical test:U Mann-Whitney, = 0.05. Patients with DVT had higher plasma levels of FVIII:C (mean 203,7 UI/dl vs. 127 UI/dl; p<0.001), FVIII:Ag (mean 109,6 UI/dl vs. 82,4 UI/dl; p<0.001) and vWF:Ag (154,2 UI/dl vs. 108 UI/dl; p<0.001) when compared to controls. We observed no statistical difference in the prevalence of all molecular changes studied between patients and controls. A4751G heterozygotes had significantly reduced levels of FVIII:C (p=0,04). Althought there was a slight association with reduced levels of vWF: Ag, this association was not statistically significant (p= 0,07). C1852G heterozygotes had significantly elevated levels of FVIII:Ag (p=0.05) and vWF:Ag (p= 0,01). Despite the relative decline of FVIII:C with the A4751G polymorphism there was no protective effect for DVT. The C1852G polymorphism is associated with a reduction of ADAMTS13, and its association with increased levels of FVIII: Ag and vWF: Ag observed in this study supports this hypothesis.
Mestrado
Biologia Estrutural, Celular, Molecular e do Desenvolvimento
Mestre em Fisiopatologia Médica
Delignat-Heudier, Sandrine. "Stratégies thérapeutiques contre la réponse immunitaire anti-Facteur VIII chez l'hémophile A : par modification de la structure du FVIII, par inhibition de la signalisation des lymphocytes B." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066002/document.
Administration of therapeutic factor VIII (FVIII) to hemophilia A patients leads to the development of anti-FVIII antibodies called “inhibitors” in 30% of severe hemophilia A patients. Despite a well characterization of T and B effectors cells involved in this immune response, there is still no therapeutic strategy proposed to the patients to prevent the occurrence of FVIII inhibitors. The first part of my thesis explores the possibility to prevent the anti-FVIII immune response by blocking FVIII capture and processing by antigen presenting cells (APC). It has been previously demonstrated that the two highly mannosylated structures on FVIII, on asparagines 239 and 2118, were recognized by the CD206 expressed on human monocyte-derived dendritic cells. This endocytic pathway led to FVIII processing and presentation to T cells. Therefore, I have investigated the possibility to reduce FVIII immunogenicity by eliminating those two glycosylations. The second part of my thesis focuses on the possibility to prevent or eradicate the anti-FVIII immune response by inhibiting a molecule involved in B cell receptor signaling: the Bruton’s tyrosine kinase (BTK). BTK plays a key role in B cells signaling and inhibition of BTK has shown a great interest in B cell malignancies, but also in some auto-immune diseases. Therefore, I have investigated the therapeutic potential of a new BTK inhibitor against the development of the anti-FVIII immune response
Lavigne, Géraldine. "Caractérisation épitopique des anticorps anti-FVIII chez les patients hémophiles A traités par facteur anti-hémophilique." Montpellier 1, 2006. http://www.theses.fr/2006MON1T015.
Khandekar, Gauri. "Origin and Role of Factor Viia." Thesis, University of North Texas, 2013. https://digital.library.unt.edu/ark:/67531/metadc407814/.
Repessé, Yohann. "Importance du facteur von Willebrand et des mutations du FVIII pour l'allo-immunisation contre le FVIII thérapeutique chez le patient hémophile A." Caen, 2007. http://www.theses.fr/2007CAEN3086.
Haemophilia A is a genetic disorder that results in insufficient levels of functional factor VIII in plasma. The treatment of bleeding episodes in hemophilia A patients involves the passive administration of exogenous human FVIII to restore normal hemostasis. The developement of anti-FVIII antibodies, called inhibitors, is the major complication of the treatment. Patients with FVIII inhibitors become resistant to conventional FVIII replacement therapy. We were interested in studying risk factors that influenced FVIII inhibitors development and cellular mechanisms involved in the initiation of the anti-FVIII immune response. In the work, we studied a population of 120 haemophilia A patients. Our results extend our insight into the mechanisms by which novel amino acid substitutions may lead to HA, and how HA patient genotypes influence the risk of FVIII inhibitor development. In addition, we studied the endocytosis of FVIII by dendritic cells, a model of professionnal antigen presenting cells, which is the first step upstream from the activation of immune effectors. Our data highlight that LRP is not implicated in FVIII endocytosis. Moreover, we described for the first time the immunoprotective effect of VWF that inhibits the endocytosis of FVIII in vitro. This work confirms the role of genetic factors in FVIII inhibitors development and improve our knowledge an the anti-FVIII immune response
Dahri, Latifa. "Épuration plasmatique des anticorps dirigés contre le facteur VIII de la coagulation (anti FVIII) sur des résines de polystyrène fonctionnalisé." Nancy 1, 1995. http://www.theses.fr/1995NAN10440.
Gilardin, Laurent. "Identification des épitopes T d’ADAMTS13 chez les patients atteints de Purpura Thrombotique Thrombocytopénique The ADAMTS13¹²³⁹-¹²⁵³ peptide is a dominant HLA-DR1-restricted CD4⁺ T-cell epitope Purpura Thrombotique Thrombocytopénique : physiopathologie, clinique, pronostic et traitement In silico calculated affinity of FVIII-derived peptides for HLA class II alleles predicts inhibitor development in haemophilia A patients with missense mutations in the F8 gene In silico prediction of immuno-dominant T-cell epitopes on human therapeutic factor VIII Predictive immunogenicity of Refacto AF Complement C3 is a novel modulator of the anti-factor VIII immune response Anti-ADAMTS13 Autoantibodies against Cryptic Epitopes in Immune-Mediated Thrombotic Thrombocytopenic Purpura." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS520.
Thrombotic thrombocytopenic purpura (TTP) is a rare and severe disease characterized by auto-antibodies directed against ADAMTS13 (A13), a plasmatic protein involved in haemostasis. The implication of CD4⁺ T cells in the pathogenesis of the disease is suggested by the existence of a restriction to particular HLA-DR alleles and by the IgG isotype of the antibodies. In this study, we wished to determine the T cell epitopes of A13. First, we selected in silico the immunodominant peptides, based on their binding capacity to HLA-DR11 molecules. Second, their binding capacity to purified HLA-DR11 molecules using a ELISA competitive assay led us to identify the best binder peptides. Finally, we determined the peptides recognized by human CD4⁺ T cells from DR11 healthy donors and patients. These results were reproduced for the HLA-DR1 haplotype and in a transgenic humanized HLA-DR1 mouse model. In a perspective point of view, our results will allow us to further isolate the specific CD4⁺ T cells in order to characterize them at different steps of the disease and during follow-up to better anticipate relapses
Books on the topic "Factor VIII (FVIII)":
Pratt, Kathleen P., and Sébastien Lacroix-Desmazes, eds. Tolerating Factor VIII: Novel Strategies to Prevent and Reverse Anti-FVIII Inhibitors. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88966-564-8.
Book chapters on the topic "Factor VIII (FVIII)":
Herrmann, F. H., K. Wulff, G. Auerswald, J. Astermark, A. Batorova, W. Kreuz, H. Pollmann, A. Ruiz-Saez, L. Salazar-Sanchez, and S. Schulman. "Factor VII Deficiency: Clinical Manifestation and Molecular Genetics of 718 Subjects with FVII Gene Mutations." In 37th Hemophilia Symposium, 238–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-73535-9_51.
Becker, Richard C., and Frederick A. Spencer. "Fundamentals and Patient Evaluation." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0033.
Hernaningsih, Yetti. "ABO Blood Group and Thromboembolic Diseases." In Blood Groups - More Than Inheritance of Antigenic Substances [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102757.
Silva, Eclesiastes Gean da, Caio Victor Barros Gonçalves da Silva, Gabriel Lúcio Guimarães dos Santos, Laís Macêdo Maciel, Bruna Barros de Queiroz, and Beatriz Santana Rocha. "Perspectivas da terapia gênica como alternativa para o tratamento da hemofilia A: uma revisão de literatura." In Avanços em Genética Humana um panorama do 1° simpósio da LAGH, 29–31. Instituto Internacional Despertando Vocações, 2024. http://dx.doi.org/10.31692/978-65-88970-44-7.29-31.
Becker, Richard C., and Frederick A. Spencer. "Historical Perspectives in Hemostasis, Coagulation, and Fibrinolysis: A Foundation for Understanding Thrombotic Disorders and Developing Effective Treatment." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0005.
Conference papers on the topic "Factor VIII (FVIII)":
Koedam, Joost A., Rob J. Hamer, Nel H. Beeser-Visser, Etienne Jap Tjoen San, Kees Schippers, and Jan J. Sixma. "THE INTERACTION BETWEEN FACTOR VIII AND VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644771.
Fulcher, C. A., R. A. Houghten, S. de Graaf Mahoney, J. R. Roberts, and T. S. Zimmerman. "SYNTHETIC PEPTIDE PROBES OF FACTOR VIII IMMUNOLOGY AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644768.
Tran, T. H., U. Zuhlke, J. Hauert, F. Duckert, G. A. Marbet, and R. Wagenwoord. "INFLUENCE OF HEPARIN ON FACTOR VIII (FVIII) ASSAY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644031.
Patrassi, G. M., A. Santarossa, F. Fallo, M. T. Sartori, M. Viero, and A. Girolami. "FACTOR VIII AND FACTOR XII LEVELS IN BORDERLINE HYPERTENSION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644259.
Joost, S., A. Koedam, Joost C. M. Meijers, Jan J. Sixma, and Bonno N. Bouma. "VON WILLEBRAND FACTOR PROTECTS FACTOR VIII FROM INACTIVATION BY ACTIVATED PROTEIN C AND PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643618.
Grant, P. J., K. K. Hampton, P. G. Wiles, and C. R. M. Prentice. "THE EFFECTS OF VASOPRESSIN ON FIBRINOLYSIS AND FACTOR VIII ARE NOT MEDIATED THROUGH V2 RECEPTORS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644712.
Váradi, K., J. Kárpáti, and S. Elödi. "ENZYME LINKED IMMUNOASSAY (ELISA) FOR FACTOR VIII ANTIGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644033.
Pötzsch, B., U. Delvos, E. Anders, N. Heimburger, and G. Müller-Berghaus. "FACTOR VIII/VON WILLEBRAND FACTOR COMPLEX: ONLY THE 440 000 SUBUNIT OF ENDOTHELIAL CELL-DERIVED VON WILLEBRAND FACTOR FORMS A COMPLEX WITH PURIFIED PLASMA FACTOR VIIIC." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644092.
Pittman, Debra D., Louise C. Wasley, Beth L. Murray, Jack H. Wang, and Randal J. Kaufman. "ANALYSIS OF STRUCTURAL REQUIREMENTS FOR FACTOR VIII FUNCTION USING SITE-DIRECTED MUTAGENESIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644044.
Verbeet, M. Ph, R. F. Evers, A. Leyte, H. L. Lamain, A. J. J. Van Ooyen, J. A. Van Mourik, and H. Pannekoek. "DETERMINATION OF THE DOMAINS OF FACTOR VIII ESSENTIAL FOR PROCOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643613.