Factor VIII structure and function☆
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Cited by (42)
Immunogenicity of Therapeutic Biological Modalities - Lessons from Hemophilia A Therapies
2023, Journal of Pharmaceutical SciencesIntravenous administration of Factor VIII–O-Phospho-L-Serine (OPLS) complex reduces immunogenicity and preserves pharmacokinetics of the therapeutic protein
2015, European Journal of Pharmaceutical SciencesCitation Excerpt :Factor VIII is a multi-domain protein (Vehar et al., 1984) consisting of six domains viz. NH2-A1-A2-B-A3-C1-C2-COOH. It is an important co-factor in the blood clotting cascade (Foster and Zimmerman, 1989). Deficiency or lack of an active form of FVIII leads to a debilitating bleeding disorder called Hemophilia A. Although, recombinant human Factor VIII (FVIII) is commercially available as the option of choice to treat hemophiliacs, the protein is inflicted with several drawbacks including protein aggregation, short circulation half-life and adverse immune response.
Downregulation of CD40 signal and induction of TGF-β by phosphatidylinositol mediates reduction in immunogenicity against recombinant human Factor VIII
2012, Journal of Pharmaceutical SciencesCitation Excerpt :Factor VIII (FVIII) is a large protein containing six domains (NH2-A1-A2-B-A3-C1-C2-COOH), and it is a critical cofactor in the blood coagulation cascade.1–3
Optimisation of the Factor VIII yield in mammalian cell cultures by reducing the membrane bound fraction
2011, Journal of BiotechnologyCitation Excerpt :Haemophilia A is an X chromosome-linked disorder characterised by insufficient production of functional Factor VIII (FVIII) (Larner, 1987). FVIII contains the domain structure A1-A2-B-A3-C1-C2 (Fay, 1993; Foster and Zimmerman, 1989), which is defined based on internal homology. The A-domains are homologous to the copper-binding protein ceruloplasmin (Kane and Davie, 1986; Church et al., 1984) and the two C domains are homologous to the C domains of Factor V and lactadherin (Stubbs et al., 1990; Hvarregaard et al., 1996).
Passive transfer of polyethylene glycol to liposomal-recombinant human FVIII enhances its efficacy in a murine model for hemophilia A
2008, Journal of Pharmaceutical SciencesCitation Excerpt :Nevertheless, inhibitory antibodies represent a significant challenge in the efficient management of the disease and alternate strategies are warranted. FVIII is a large multi-domain glycoprotein consisting of domains A1, A2, B, A3, C1, and C2.9, 10 Epitope mapping experiments have revealed that anti-FVIII antibodies mainly target defined regions in the A2 (heavy chain), A3 and C2 domains (light chain) of FVIII.11, 12
Phosphatidylserine containing liposomes reduce immunogenicity of recombinant human factor VIII (rFVIII) in a murine model of hemophilia A
2008, Journal of Pharmaceutical Sciences
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This work was supported in part by Grants HL 15491, HL 31950 and DK 07022 from the National Institutes of Health. This is publication number 5538-BCR from the Research institute of Scripps Clinic.