Additional Supporting Information may be found in the online version of this article.

HEP_26100_sm_SuppFig1.tif1062KSupporting Information Figure 1. BMDCs were transfected with HO-1 siRNA or NS siRNA (100nM) and incubated with LPS (0.5μg/ml) for 24h. The expression of STAT3 and β-catenin in extracted proteins was evaluated by Western blots. Knockdown of HO-1 diminished STAT3 and β-catenin expression, suggesting that activation of β-catenin in DCs was dependent on HO-1-mediated transcriptional STAT3 activation.
HEP_26100_sm_SuppFig2.tif673KSupporting Information Figure 2. BMDCs (1×106/well) were transfected with β-catenin siRNA or NS siRNA. After 24h culture, DCs were harvested and 1 × 105/well were incubated first with OVA peptide (5 μg/ml) and then LPS (0.5μg/ml). After 24h, spleen T cells (5×105/well) were added into DC cultures. Co-culture supernatants were harvested at 72h. Knockdown of β-catenin increased ELISA-assisted IL-12p40 and IFN-γ production in LPS-stimulated cultures. *p>0.05.
HEP_26100_sm_SuppFig3.tif1064KSupporting Information Figure 3. BMDCs transfected with β-catenin siRNA (100nM) were incubated with LPS (0.5μg/ml) for 24h. Knockdown of β-catenin in LPS-stimulated BMDCs diminished Western assisted expression of β-catenin but increased the expression of PTEN, TLR4 and p-IkBa, compared to cells stimulated with LPS alone.
HEP_26100_sm_SuppFig4.tif1065KSupporting Information Figure 4. Hepatic DCs (5×105/well) transfected with β-catenin siRNA or NS siRNA were stimulated with LPS (0.5μg/ml). After 24h culture, cells were stained with anti-CD4 and CD8a PE-conjugated mAb, and analyzed by FACSCalibur flow cytometer. Disruption of β-catenin signaling did not affect DC populations (CD4+DC and CD8α+DC), as compared with NS siRNA controls.

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