Induction of aggregation in porcine lymphoid cells by antibodies to CD46

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. Copyright (C) 2000 Elsevier Science B.V.

Bibliographic Details

Main Authors:	Bullido, R., Pérez de La Lastra, J., Almazán, F., Ezquerra Martínez, Ángel, Llanes, D., Alonso, F., Domínguez, J.
Format:	artículo biblioteca
Language:	English
Published:	Elsevier 2000
Subjects:	Aggregation, CD46, Membrane cofactor protein (MCP), Monoclonal antibody, Pig,
Online Access:	http://hdl.handle.net/20.500.12792/4929 http://hdl.handle.net/10261/292993
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