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Mediates Induction of the CD11c 
2 Integrin Gene Promoter1
Renal Unit, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129
CD11c is a member of the 
2 integrin family of
adhesion molecules that, together with CD18, forms a heterodimeric
receptor on the surface of myeloid, NK, dendritic, and certain
leukemic, lymphoma, and activated lymphoid cells. Monocytic
differentiation is associated with an induction of both CD11c and CD18
gene expression. The resulting CD11c/CD18 receptor mediates firm
adhesion to the vascular endothelium, transendothelial migration,
chemotaxis, and phagocytosis. Monocytic differentiation can be mimicked
in vitro by treatment of the promonocytic cell line U937 with PMA.
Recently, we reported that in U937 cells, expression of the
CD11c gene is controlled by an unidentified
transcription factor that binds ssDNA. This finding suggested that DNA
secondary structure plays an important role in controlling the
CD11c gene and prompted us to search for additional
ssDNA-binding activities with which this gene interacts. In this study,
we report that in U937 cells, expression of the CD11c
gene is mediated by the ssDNA-binding protein Pur
. During
PMA-induced differentiation, the ability of Pur to activate the
CD11c promoter in U937 cells increases, as does that of
Sp1. Together, these increases in the functional activity of both
Pur and Sp1 combine to induce CD11c
expression.
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