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. 2008 Jul 18;105(30):10408–10413. doi: 10.1073/pnas.0805036105

Fig. 4.

Fig. 4.

rp+/− MPNSTs do not exhibit an overall decrease of translation capacity, but specifically fail to synthesize p53 protein. (A and B) rp+/− MPNST cells and p53M214K/M214K MPNST cells were counted, and an equal number of cells were plated and labeled for a 30-min pulse with [35S]cysteine/methionine. Cells were then lysed for visualization of newly synthesized labeled proteins by autoradiography (A) or for quantification of labeled proteins by TCA precipitation and scintillation counting (B). Both methods reveal equal labeling of newly synthesized proteins in both rp+/− MPNST cells and p53M214K/M214K MPNST cells. (C) Plated rp+/− MPNST cells, p53M214K/M214K MPNST cells, and seminoma pulse-labeled with [35S]cysteine/methionine and immunoprecipitated with antibodies against actin reveal no difference in the amount of actin protein synthesized during the pulse. (D) Plated p53M214K/M214K MPNST and seminoma cells pulse-labeled with [35S]cysteine/methionine and immunoprecipitated with αp53 antibodies display newly synthesized p53 protein in the presence or absence of γ-irradiation and MG132, in contrast to rp+/− MPNST cells, which do not synthesize p53 protein in either condition.