Fig. 2.

Fig. 2. Kinetin riboside promotes proteasomal degradation of β-catenin. (A) In the presence or absence of Wnt3a- CM, HEK293-FL cells were treated with vehicle (DMSO) or kinetin riboside (10, 20, or 40 μM) for 15 h, and cytosolic proteins were analyzed by Western blotting with anti-β-catenin antibody. (B) In the presence or absence of Wnt3a-CM, HEK293-FL cells were treated with vehicle (DMSO) or kinetin riboside (10, 20, or 40 μM) for 15 h, and β-catenin and GAPDH mRNA levels were detected by semi-quantitative RT-PCR. β-Catenin mRNA levels were normalized to those of GAPDH. (C) In the presence or absence of Wnt3a-CM, HEK293-FL cells were incubated with vehicle (DMSO) or kinetin riboside (20 μM) and then exposed to MG-132 (10 μM) for 8 h. Cytosolic proteins were analyzed by Western blotting with anti-β-catenin antibodies. (D) After treatment of HEK293-FL cells with DMSO or kinetin riboside (10, 20, or 40 μM) for 15 h, cytosolic proteins were analyzed by Western blotting with anti-active-β-catenin antibody. In (A), (C), and (D), β-actin was used as a loading control, and β-catenin levels were normalized to those of β-actin. The bar graph indicates the average volume density corrected for the loading control, and results are expressed as the mean ± SD of three independent experiments. *p < 0.05 and **p < 0.01, comparison between the Wnt3a-CM-treated control and kinetin riboside-treated groups.

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