IL-12 acts directly on DC to promote nuclear localization of NF-κB and primes DC for IL-12 production
Immunity, 1998•cell.com
We analyzed the expression of an IL-12 receptor by fresh dendritic cells (DC) and a DC line.
Using RT-PCR, RNAse protection, and electrophoretic mobility shift assay analysis, we
found that DC possess an IL-12 receptor with β1 subunit (downstream box 1)-related
differences from that on T cells. IL-12 signaling through this receptor involved members of
the NF-κB but not STAT family. The unique properties of the IL-12 receptor on DC,
characterized by a single class of binding sites with a K d of about 325 pM, may underlie …
Using RT-PCR, RNAse protection, and electrophoretic mobility shift assay analysis, we
found that DC possess an IL-12 receptor with β1 subunit (downstream box 1)-related
differences from that on T cells. IL-12 signaling through this receptor involved members of
the NF-κB but not STAT family. The unique properties of the IL-12 receptor on DC,
characterized by a single class of binding sites with a K d of about 325 pM, may underlie …
Abstract
We analyzed the expression of an IL-12 receptor by fresh dendritic cells (DC) and a DC line. Using RT-PCR, RNAse protection, and electrophoretic mobility shift assay analysis, we found that DC possess an IL-12 receptor with β1 subunit (downstream box 1)-related differences from that on T cells. IL-12 signaling through this receptor involved members of the NF-κB but not STAT family. The unique properties of the IL-12 receptor on DC, characterized by a single class of binding sites with a Kd of about 325 pM, may underlie rather unique effects, such as IFNγ-independent augmentation of class II antigen expression and priming for LPS-induced production of IL-12.
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