Blockade of Lysosomal Acid Ceramidase Induces GluN2B-Dependent Tau Phosphorylation in Rat Hippocampal Slices
Figure 3
D-NMAPPD treatment promotes Tau hyperphosphorylation at the Ser262 epitope. Phosphorylated Tau levels were estimated by Western blot on cell extracts obtained from hippocampal slices treated or not with the acid ceramidase inhibitor d-NMAPPD (25 μM, 3 h). Three Tau isoforms were consistently distinguished in immunoblots performed with antibodies directed against various phosphoepitopes (Ser262, Ser199-202, and Ser396). Summary data on pSer262 (a), pSer199-202 (b), and pSer396 (c) epitopes are expressed relative to total Tau (Tau-5) and shown in the bar graph (means ± SEM of 6 different experiments). For statistical analysis, one-way ANOVA was followed by Newman-Keul’s post hoc test. , d-NMAPPD versus the controls. Note the strong ability of d-NMAPPD to enhance Tau phosphorylation at residue Ser262 of the 68 kDa isoform.
