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Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor.
BO2C11 is the first human monoclonal anti-fVIII IgG antibody that has been isolated and allows the study of fVIII inactivation at the molecular level.
CD4+CD25+ T Cells Lyse Antigen-Presenting B Cells by Fas-Fas Ligand Interaction in an Epitope-Specific Manner 1
- W. Janssens, V. Carlier, Bo Wu, L. Vanderelst, M. Jacquemin, J. Saint-Remy
- BiologyThe Journal of Immunology
- 1 November 2003
Suppression by regulatory T cells is now acknowledged to play a key role in the down-regulation of T cell responses to foreign and self Ags. In addition to the naturally occurring CD4+CD25+…
VWF protects FVIII from endocytosis by dendritic cells and subsequent presentation to immune effectors.
It is demonstrated that VWF protects FV III from being endocytosed by human dendritic cells and subsequently presented to FVIII-specific T cells and had no direct inhibitory effect either on the ability of DCs to present antigenic peptides or on the activation potency of CD4+ T cells.
Characterization of proposed human B-1 cells reveals pre-plasmablast phenotype.
Controversy has arisen about the nature of circulating human CD20(+)CD27(+)CD43(+)CD70(-)CD69(-) B cells. Although originally described as being the human counterpart of murine B-1 B cells, some…
A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor.
C1 is identified as a novel target for fVIII inhibitors and it is demonstrated that Arg2150His substitution alters a B-cell epitope in the C1 domain, which may contribute to the higher inhibitor incidence in patients carrying such substitution.
A novel therapy for atopic dermatitis with allergen-antibody complexes: a double-blind, placebo-controlled study.
Structure of a factor VIII C2 domain-immunoglobulin G4kappa Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII.
This atomic resolution structure suggests a variety of amino acid substitutions in the C2 domain offactor VIII that might prevent the binding of anti-C2 inhibitor antibodies without significantly compromising the procoagulant functions of factor VIII.
Antigenicity of putative phospholipid membrane-binding residues in factor VIII.
Results suggest that C2 inhibitors frequently target the Met2199/Phe2200 and Leu2251/Leu2252 beta-hairpins and are consistent with the hypothesis that these residues participate in binding to phospholipid membranes.
In Vivo Induction of Type 1-Like Regulatory T Cells Using Genetically Modified B Cells Confers Long-Term IL-10-Dependent Antigen-Specific Unresponsiveness1
Regulatory T cells (Tregs) hold much promise for the therapy of allergy and autoimmunity, but their use is hampered by lack of Ag specificity (natural Tregs) and difficulty to expand in vitro or in…
A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function.
The results identify a membrane-binding face of the factor VIII C1 domain, indicate an influence of the C2 domain on factor VIII binding to factor X, and indicate that cooperation between the C1 and C2 domains is necessary for full activity of thefactor Xase complex.