Representative western blot showing faster Aβ degradation in the liver of non-demented controls subjects when compared to the AD group.

Lyophilized fluorescein-labeled Aβ40 (A) or Aβ42 (B) peptides were added to liver homogenates to quantify its degradation. Sucrose lysis buffer containing complete protease inhibitor cocktail was added to stop the reaction and Western blot performed to visualized Aβ degradation (molecular weight ~7kDA).</p

Antibodies used in western blots.

Antibodies used in western blots.</p

Protein expression of proteolyic degradation enzymes, IDE, CatD and neprilysin in the liver of non-demented controls (NDC) and Alzheimer’s disease (AD) subjects.

Liver protein expression of the proteolytic degradation enzyme insulin degrading enzyme (IDE) was lower in AD subjects (A); while cathepsin (CatD) levels (B) were higher. Neprilysin was not statistically significantly between the two groups (C). GAPDH was used as a total protein loading control.</p

Patient demographics.

Patient demographics.</p

Patient hepatic pathologies.

Miscellaneous Benning Hepatic Pathologies present in all the cases used in this study. (DOCX)</p

ELISA measurements of Aβ40 and Aβ42 degradation in liver homogenates from non-demented controls (NDC) and Alzheimer’s disease (AD) subjects.

Homogenates from NDC degraded Aβ faster than AD subjects. Aβ40 degraded slower (A) than Aβ42 (B) and even though both peptides degraded faster in the NDC group.</p

Additional file 2 of Cellular localization of p-tau217 in brain and its association with p-tau217 plasma levels

Additional file 2: Figure S2. Immunostaining against Ckid. Image in (A and B) show pictures of Cornu Ammonus 1 (CA1) and entorhinal cortex (EC) of and AD patients captured with 20 × magnification. The number of Ckid positive clusters and vesicle within each cluster (indicated with arrows) are several times higher in CA1 (A) compared to EC (B). Scalebar = 20 µ

Additional file 3 of Cellular localization of p-tau217 in brain and its association with p-tau217 plasma levels

Additional file 3: Figure S3. Correlation analysis between p-tau217 plasma and p-tau217 area fraction in amyloid beta negative individuals. Scatter plotts in (A-F) show how p-tau217 plasma values relates to p-tau 217 area fraction in the Entorhinal cortex (EC) (A), Cornu Ammonium 1 (CA1) (B), inferior temporal gyrus (ITG) (C), superior frontal gyrus (SFG) (D), mean value of EC, CA1 and ITG (M1) (E) and mean value of EC, CA1, ITG and SFG (M2) (F) of amyloid beta negative individuals. Each point in (A-F) represents a mean of 3 pictures from 2–3 sections (in total 6–9) from each individual and data was analyzed using Spearman correlations test

Additional file 1 of Cellular localization of p-tau217 in brain and its association with p-tau217 plasma levels

Additional file 1: Figure S1. Immunostaining against P-tau217 and GFAP, Iba-1, tau, p-tau 369/404 and p-FTAA. Image in (A and B) show that neither GFAP positive astrocytes (asterisks in A) nor iba-1 positive microglia (asterisks in B) is assocaited with P-tau217 positive vesicles (arrows in A and B). Images in (C-E) show that not all tangles positive for tau (C) and p-tau396/404 (D), p-FTAA (E) Scalebar = 20 µ

Additional file 2 of A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson’s disease

Additional file 2 Supplementary Fig. S1. α-Syn expression enhances axonal growth in primary hippocampal, mesencephalic and cortical neurons. A. Primary hippocampal cultures from α-Syn−/− (C57BL/6JOlaHsd) mouse brains, virally transduced either with WT α-Syn, A53T α-Syn, K10,12E α-Syn, or a mock-GFP vector. Cells were fixed at 4 DIV and immunoreacted with antibodies against α-Syn (MJFR1, green), α-tubulin (white) and PI4,5P2 (red). Direct fluorescence was captured for GFP (green). Bar = 25 μm. B. Graph showing the average length of the main extension designated as axons (in μm); C. Total length of collaterals per axon (in μm); and D. PI4,5P2 levels within the main axon and its collaterals (per μm2 area) quantified by Fiji (Image J) program. Mean ± SE; n > 17 cells; *, P  15 cells; *, P  20 cells; *, P < 0.05. Supplementary Fig. S2. Specificity of PI4,5P2 signal. A. Specificity of PI4,5P2 signal is detected by ICC in primary neurons, following activation of muscarinic receptors with carbachol (Sigma Aldrich) and PLC-mediated hydrolysis of PI4,5P2. Primary cortical neurons at 5 DIV, treated with 1 mM carbachol for12 minutes. Bar = 20 μM. B. Higher magnification of a cortical neuron (as in A), demonstrating PI4,5P2 signal on PM surrounding cell body. HEK 293 T cells transiently expressing the rapamycin-induced translocatable CFP-PIPK kinase. CFP-PIPK fluorescence is either cytosolic or on the PM in DMSO or rapamycin (respectively) treated cells. CFP-PIPK (blue) is directly detected at 485 nm and PI4,5P2 detected by ICC with anti PI4,5P2 ab (red). Bar = 10 μM. Supplementary Fig. S3. vGluT1 and TH immunoreactivity in control and PD brains. Slides containing caudate of a control (Male 85 years, 3 h PMI) and an early PD case (male 83 years, 2 h PMI, Unified stage IIa), immunoreacted with anti vGluT1 (red) and anti TH (green) antibodies. Bar = 10 μm