IL-12 is composed of the IL-12p40 subunit linked to the IL-12p35 subunit, and the heterodimer signals through the IL-12 receptor (IL-12R), which comprises the IL-12Rβ1 and IL-12Rβ2 subunits. IL-12 stimulates nonreceptor Janus kinase 2 (JAK2) and tyrosine kinase 2 (TYK2) activity, leading to phosphorylation of signal transducer and activator of transcription (STAT) family members STAT1, STAT3, STAT5 and, in particular, STAT4 homodimers.
IL-23 is composed of the IL-23p19 subunit and the IL-12p40 (here called IL-12/23p40) subunit, which signals through IL-23R and IL-12Rβ1. Like IL-12, IL-23 activates JAK and STAT signaling molecules, but it activates STAT3 predominantly. The difference in mouse IL-12– and IL-23–dependent signaling is due in part to the preferential activation of STAT4 by IL-12 and of STAT3-dependent target genes by IL-23.
IL-12 and IL-23 are secreted by human and mouse dendritic cells and tissue-resident macrophages in response to exogenous or endog¬enous signals associated with host defense and wound healing. Whereas IL-12 promotes differentiation of naive CD4 T cells into interferon (IFN)-γ–producing TH1 cells, IL-23 does not directly promote TH cell differentiation, owing to the absence of IL-23 receptor (IL-23R) on human and mouse naive T cells.
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