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Blood ; 104(8): 2540-2, 2004 Oct 15.
Article in English | MEDLINE | ID: mdl-15213098

ABSTRACT

The chimeric anti-CD20 monoclonal antibody (mAb), rituximab, is an established part of the management of many non-Hodgkin lymphomas. The in vivo action of rituximab remains elusive, and this partially reflects a lack of highly specific reagents to detect rituximab binding at the cell surface. Here we report a new high-affinity mAb (MB2A4) with fine specificity for the idiotype of rituximab. It is able to detect rituximab in vitro, in the presence of high levels of human immunoglobulin G (IgG), in the serum of patients receiving rituximab therapy, and, surprisingly, when rituximab is bound to CD20 on the cell surface. We propose that the anti-idiotype (Id) binds to rituximab molecules bound univalently at the cell surface, facilitated by the relatively high off-rate of rituximab. This reagent provides new insights into the binding of rituximab at the cell surface and demonstrates a mode of binding that could be exploited for the surface detection of other mAbs with clinical and biologic applications.


Subject(s)
Antibodies, Anti-Idiotypic/immunology , Antibodies, Monoclonal/immunology , Antibodies, Monoclonal/therapeutic use , Lymphoma, B-Cell/drug therapy , Lymphoma, B-Cell/pathology , Animals , Antibodies, Monoclonal/blood , Antibodies, Monoclonal/metabolism , Antibodies, Monoclonal, Murine-Derived , Antigens, CD20/immunology , B-Lymphocytes/immunology , B-Lymphocytes/metabolism , B-Lymphocytes/pathology , Cell Line, Tumor , Cell Membrane/metabolism , Humans , Immunotherapy , Lymphoma, B-Cell/immunology , Rats , Rituximab
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