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. 2014 May 15;25(10):1641–1652. doi: 10.1091/mbc.E13-12-0717

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© 2014 Poletto et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — Depletion of NPM1 positively modulates BER protein amounts. (A) Representative Western blotting analysis on NPM1^+/+ and NPM1^⁻/⁻ whole-cell extracts (60 μg), showing the higher levels of BER proteins in the absence of NPM1 expression (left). Antibodies used are indicated on the right-hand side. Right, histogram reporting densitometric quantification of Western blotting signals from at least three independent experiments. Protein amounts are expressed as mean ± SD of the signal, considering NPM1^+/+ as reference sample. Either actin or tubulin was used as loading control. (B, C). Representative Western blotting analysis on whole-cell extracts (50 μg) from scrambled siRNA (siScr), NPM1 siRNA (siNPM1)-treated NPM1^+/+ cells (B), and mock- or NPM1-reconstituted (pNPM1) NPM1^⁻/⁻ cells (C). Change in BER protein levels upon NPM1 down-regulation or reexpression are indicated on the right-hand side. siScr cells or mock-transfected cells were used as reference, respectively. Values indicated are mean ± SD from at least three independent replicates. Antibodies used are indicated on the right-hand side; tubulin was used as loading control. (D) Real-time PCR analysis comparing the relative amount of transcript for the indicated BER factors between NPM1^+/+ and NPM1^⁻/⁻ cells. Among the genes tested, only Polβ showed a statistically significant increment. Values reported are expressed as mean ± SD of the expression level in three independent replicates, considering NPM1^+/+ as reference sample.