Induction of aggregation in porcine lymphoid cells by antibodies to CD46.
Vet Immunol Immunopathol
; 73(1): 73-81, 2000 Jan 31.
Article
em En
| MEDLINE
| ID: mdl-10678400
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.
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Base de dados:
MEDLINE
Assunto principal:
Suínos
/
Glicoproteínas de Membrana
/
Linfócitos
/
Antígenos CD
/
Anticorpos Monoclonais
Limite:
Animals
Idioma:
En
Revista:
Vet Immunol Immunopathol
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Espanha