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. 2001 Jul 23;154(2):369–388. doi: 10.1083/jcb.200102028

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Copyright © 2001, The Rockefeller University Press

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Figure 6. — Inhibition of the β-catenin–TCF-4 signaling by 1α,25(OH)₂D₃. (A) 1α,25(OH)₂D₃ induces nuclear export of β-catenin. Quantification of the percentage of SW480-ADH cells showing predominant nuclear (left inset, white bars), mixed nuclear-cytoplasmic (middle inset, gray bars), or exclusively membranous (right inset, black bars) β-catenin localization after treatment with 1α,25(OH)₂D₃ (10⁻⁷ M) for the indicated times. 500 cells were analyzed at each time point. (B) Inhibition of β-catenin–TCF-4 transcriptional activity by 1α,25(OH)₂D₃. SW480-ADH cells were transfected with the wild-type (TOP-flash) or mutated (FOP-flash) β-catenin–TCF4/LEF-1–sensitive reporter plasmids and then left untreated (white bars) or treated (black bars) with 1α,25(OH)₂D₃ (10⁻⁷ M) for 48 h. Mean values and standard deviation of the mean of triplicated obtained in three experiments are shown. (C) Effects of 1α,25(OH)₂D₃ on the expression of β-catenin–TCF-4 target genes. Northern blots analysis of mRNA expression in SW480-ADH cells untreated or treated with 10⁻⁷ M 1α,25(OH)₂D₃ for the indicated times. Conditions were as above. (D) Quantification of the change in ZO-1, PPARδ, CD44, Tcf-1, and c-myc mRNA levels induced by 1α,25(OH)₂D₃. Mean values and error bars corresponding to triplicates obtained in three experiments are shown. (E) Induction and redistribution of ZO-1 protein by 1α,25(OH)₂D₃ treatment. Analysis by immunofluorescence and confocal laser microscopy of ZO-1 expression in SW480-ADH cells after addition of 1α,25(OH)₂D₃ (10⁻⁷ M). Bar, 10 μm.