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The Journal of Immunology, 1999, 162: 6331-6336.
Copyright © 1999 by The American Association of Immunologists

Cross-Linking of Membrane CD43 Mediates Dendritic Cell Maturation1

Silvia Corinti*, Emanuele Fanales-Belasio*, Cristina Albanesi*, Andrea Cavani*, Pavla Angelisova{dagger} and Giampiero Girolomoni2,*

* Laboratory of Immunology, Istituto Dermopatico dell’Immacolata, IRCCS, Rome, Italy; and {dagger} Institute of Molecular Genetics, Academy of Science of the Czech Republic, Prague, Czech Republic

CD43/leukosialin is a major sialoglycoprotein of the dendritic cell (DC) surface, which can regulate cell adhesion and has the potential to mediate cell activation signals. Monocyte-derived DC transiently incubated with the anti-CD43 mAb, MEM-59, or with F(ab')2 fragments, but not with monovalent Fab fragments or control IgG, 24 h later showed increased levels of membrane HLA-DR, CD54, CD40, CD80, CD86, and CD83. In parallel, CD43 cross-linking induced synthesis and release of IL-1ß, IL-6, TNF-{alpha}, IL-12, and IL-10. CD43 ligation inhibited the endocytic activity of DC, and enhanced the capacity of DC to stimulate T cell proliferation in the primary allogeneic and autologous MLR assay. In addition, anti-CD43-treated DC were less efficient at presenting native HIV-1 reverse transcriptase to a specific CD4+ T cell clone, whereas presentation of the reverse transcriptase 55–72 peptide to the same clone was increased. Finally, MEM-59 or its F(ab')2 fragments elicited a rise in intracellular free calcium and tyrosine phosphorylation of a 25-kDa protein in DC. The results thus indicate that CD43 cross-linking with specific ligands induces activation and functional maturation of DC.




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