| Autor: |
Kubin, Marek Z., Parshley, Dorothy L., Din, Wenie, Waugh, Jennifer Y., Davis-Smith, Terri, Smith, Craig A., Macduff, Brian M., Armitage, Richard J., Chin, Wilson, Cassiano, Linda, Borges, Luis, Petersen, Melissa, Trinchieri, Giorgio, Goodwin, Raymond G. |
| Zdroj: |
European Journal of Immunology; November 1999, Vol. 29 Issue: 11 p3466-3477, 12p |
| Abstrakt: |
Using the monoclonal antibody C1.7, which recognizes a signaling, membrane-bound molecule on human NK and a proportion of CD8+ T cells, we cloned a novel molecule we refer to as NK cell activation-inducing ligand (NAIL). It is a 365-amino acid protein that belongs to the immunoglobulin-like superfamily with closest homology to murine 2B4, and human CD84 and CD48. Using a soluble NAIL-Fc fusion protein, we determined the counterstructure for NAIL, CD48, which it binds with high affinity. Stimulation of human B cells with recombinant NAIL in the presence of a suboptimal concentration of human CD40 ligand or IL-4 resulted in increased proliferation. Treatment of human dendritic cells with soluble NAIL-leucine zipper protein resulted in an increased release of IL-12 and TNF-α. Using recombinant CD48 protein, we demonstrated the ability of this molecule to increase NK cell cytotoxicity and induce IFN-γ production. We also showed that 2B4 binds to mouse CD48, suggesting that interaction of these receptors may play a similar role in both species. Taken together these results indicate that the NAIL-CD48 interaction may be an important mechanism regulating a variety of immune responses. |
| Databáze: |
Supplemental Index |
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