Fig. 2

The epitope-specific AD-like tau hyperphosphorylation and APP/Aβ dysmetabolism found in eyes from Tg2576 animals are strongly reduced by 12A12mAb i.v. injection. Western blots (a) of soluble retinal homogenates from three experimental groups (wild-type, Tg2576 and Tg2576 + mAb) probed with specific antibody against total (HT7), phospho- (AT8, P + Ser198/Ser202 epitopes) and dephospho- (Tau-1, P-Ser198/Ser202 epitopes) tau protein. Arrows on the right side indicate the molecular weight (kDa) of bands calculated from migration of standard proteins. Semi-quantitative densitometric analysis (n = 6) of all retinal tau isoforms was shown in (b) by using β-actin for normalization. Values are from at least three independent experiments and statistically significant differences were calculated by one-way analysis of variance (ANOVA) followed by Bonferroni’s post-hoc test for multiple comparison among more than two groups. p < 0.05 was accepted as statistically significant (*p < 0.05; **p < 0.01; ***p < 0.0005; ****p < 0.0001). Western blotting probed with 6E10 (anti-Aβ/APP protein, 4-9aa) (c) showing that the immunoreactive bands of Amyloid Precursor Protein (APP)-derived, Aβ-containing processing intermediates were significantly reduced in retina and vitreous body from 12A12mAb-injected transgenic AD animals. Semi-quantitative densitometric analysis (n = 6) (d) was calculated by normalizing the smeared signal ranging between 12 and 95 kDa of each lane/sample (the region of interest, ROI) to corresponding β-actin intensities on the same blots. Values are from at least three independent experiments and statistically significant differences were calculated by one-way analysis of variance (ANOVA) followed by Bonferroni’s post-hoc test for multiple comparison among more than two groups. p < 0.05 was accepted as statistically significant (*p < 0.05; **p < 0.01; ***p < 0.0005; ****p < 0.0001)