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• W2064157818 abstract "CD46 is a major transmembrane glycoprotein that belongs to the regulator of complement activation (RCA) family. Recently, mAbs to human CD46 were shown to suppress IL-12 production. Here, we describe that mAbs against different porcine CD46 epitopes induced a marked adhesion of normal lymphocytes. Addition of low amounts of antibody to freshly isolated lymphocytes or thymocytes resulted in the clustering of the cells. Cross-linking of CD46 molecules seems essential since Fab fragments failed to induce aggregation. This aggregation was dependent on active cell metabolism and on the presence of divalent cations and required a functional cytoskeleton. It was not inhibited by antibodies to CD18, CD29, CD2, CD11a and CD11b. Staurosporine, an inhibitor of protein kinases, partially blocked the aggregation. This finding is indicative of a role of protein kinases in the transduction of the signal generated by CD46 engagement." @default.
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• W2064157818 date "2000-01-01" @default.
• W2064157818 modified "2023-10-17" @default.
• W2064157818 title "Induction of aggregation in porcine lymphoid cells by antibodies to CD46" @default.
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• W2064157818 doi "https://doi.org/10.1016/s0165-2427(99)00154-3" @default.
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