Figure 7.

α-Synuclein-induced blockade of NFκB activation is associated with decreased acetylation of p65 but does not correlate with nuclear translocation or protein levels of NFκB/IκBα. A, B, Nuclear translocation and abundance of NFκB/IκBα were not altered by overexpression of αsyn. Representative immunoblot of p65, p50, and IκBα levels on cytoplasmic and nuclear extracts (A) or whole-cell lysates (B) from αsyn (Syn) and vector control (Vec) cells. C, The p65 acetylation levels were reduced in αsyn cells. Whole-cell lysates was immunoprecipitated (IP) with p65 antibody. The resulting immunoprecipitates were blotted with anti-acetyl-lysine and anti-p65 antibodies. Densitometric quantitation of the ratio of band intensity of acetylated p65 and total p65 from two independent experiments (means ± SEM; **p < 0.01) is shown on the right. D, Sodium butyrate (NaBu) specifically enhanced PKCδ isoform expression in αsyn-expressing N27 cells. αSyn-expressing cells were treated with 1 mm NaBu and 50 μm caspase-3 inhibitor Z-DEVD-FMK, and cell lysates were prepared for blotting with specific anti-PKC isoforms (left panel) and anti-acetyl-lysine (right panel) antibodies.