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- W9796610 abstract "Abstract The receptor CD30 is selectively overexpressed on many human lymphoma cells and therefore an interesting target for antibody-based immunotherapy. However, binding of therapeutic antibodies stimulates CD30 shedding leading to a loss of target antigen and a release of the soluble ectodomain (sCD30). Here, we showed that sCD30 binds to membrane-anchored CD30 ligand (CD153) on mast cells and neutrophils which are frequently found among the bystander cells in lymphoma tissue. Using sCD30 as a linker, CD30 antibodies are able to bind to mast cells where they caused the release of interleukin-8 (IL-8) which is involved in angiogenesis and metastasis. To overcome this adverse shedding-dependent mistargeting we used loss-of-function experiments with cells lacking candidate CD30-releasing enzymes ADAM10 and ADAM17 and a selective inhibitor to identify ADAM10 as the main enzyme responsible for antibody-stimulated shedding. In co-culture experiments, the antibody-induced transfer of sCD30 from the human Hodgkin lymphoma cell line L540 to the CD30-negative but CD153-expressing human mast cell line HMC-1 was inhibited by the ADAM10-selective inhibitor GI254023X. These findings suggest that selective metalloproteinase inhibitors blocking antibody-induced shedding of target antigens could be of therapeutic value to increase the specificity and reduce side-effects of immunotherapy with monoclonal antibodies." @default.
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- W9796610 date "2007-04-01" @default.
- W9796610 modified "2023-10-12" @default.
- W9796610 title "Selective metalloproteinase inhibition of human CD30 shedding increases specificity of targeted immunotherapy (48.38)" @default.
- W9796610 doi "https://doi.org/10.4049/jimmunol.178.supp.48.38" @default.
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