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Fig. 4. LAP2ß induces deacetylation of histone H4 in vitro and in vivo. (A) U2OS cells were transfected with either 1 µg LAP2ß (i) or HDAC1 (ii). Cells were fixed and immunostained with antibodies against acetylated histone H4, LAP2ß or HDAC1, as indicated, and analysed by confocal microscopy. (B) U2OS cells were transfected with LAP2ß (0.1 or 1.0 µg) or HDAC1 (1.0 µg), followed by treatment with 5 mM sodium butyrate. Cellular extracts were detected by western blot analysis, using antibodies against acetylated histone H4, LAP2ß and ß-actin, as indicated. (C) Sodium-butyrate-treated U2OS cells were transfected with 1 µg LAP2ß, HDAC3, LAP2ß and HDAC3, or p300, as indicated. Cellular extracts were prepared and protein amount was detected in each sample. Equal amounts of lysates were incubated with [³H]-acetylated histone H4 peptide. Released [³H]-acetate was measured in cpm using a ß-radiation counter. The experiment was repeated three times.

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