Impaired suppressive activities of human MUTYH variant proteins against oxidative mutagenesis

Figure 1 Establishment of H1299 human cell lines inducibly expressing MUTYH variant proteins. A: Detection of MUTYH proteins in cumate-inducible stable cell lines expressing MUTYH in the presence of cumate using Western blotting analysis with an anti-MUTYH antibody. Lysates from empty vector-transposed cells and cells inducibly expressing wild-type (WT) MUTYH or p.R154H, p.M255V, p.L360P, or p.P377L MUTYH variants were analyzed. β-tubulin protein was also analyzed as an internal control; B: Immunofluorescence detection of MUTYH proteins expressed in the cell lines used in (A) in the presence of cumate. The MUTYH protein (red) was stained with anti-MUTYH as the primary antibody and Alexa Fluor 594-conjugated goat anti-mouse IgG as the secondary antibody. The nuclei were counterstained with 4’,6-diamidino-2-phenylindole (DAPI) (blue); C: Immunofluorescence detection of endogenous MUTYH proteins in the empty vector-transposed cells as described in (B). The intensity of the signals of MUTYH protein (red) was enhanced with image-editing software to determine the subcellular localization of endogenous MUTYH protein. The nuclei were counterstained with DAPI (blue).