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. 2011 Jun 8;7(6):740–752. doi: 10.7150/ijbs.7.740

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© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.

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MCLR triggers α4/PP2A C subunit dissociation and affects PP2A core enzyme stability. HEK293 cells were treated with MCLR at varying concentrations for 24 h. (A) The α4 protein level was examined by Western blotting, where GAPDH was used as loading control. (B) Immunoprecipitation assay was performed in HEK293 cell lysate using an anti-PP2A/C antibody. The association of PP2A/C with α4 and PP2A/A form precipitated material was detected by Western blotting. Binding of PP2A/A or α4 to PP2A/C was quantified and the ratio of each complex was measured by comparing to total C subunit and displayed by comparing to non-MCLR treated group. Data represent mean ±SD (n=3) *, p<0.05; ***, p<0.001 compared with control. (C) Immunofluorescence assay using antibody against PP2A/C and α4 shows reduced binding between α4 (red) and PP2A/C (green). Nuclei (blue) were stained with DAPI. The merged images showed the co-localization of α4 and PP2A/C.