Journal: iScience

Article Title: Exposure to fibrillar proteins leads to widespread infiltration but only mild tau pathology in cortical organoids

doi: 10.1016/j.isci.2026.115819

Figure Lengend Snippet: Tau staining patterns in organoids display heterogeneity between and within different treatment groups (A–C) Shows the expression pattern of PHF-1 (A), T22 (B), and tau-5 (C) across the different samples following αSYN, Aβ, and tau exposure; both direct (Fibril) and astrocyte-mediated (Astro). Pictures are from two individual organoids per group. (D) High magnification example images of the tau-positive signal patterns (PHF-1 is from astrocyte-mediated αSYN exposure, T22 and tau-5 are from direct Aβ-treated organoids). (A–C) scale bars, 250 μm, (D) scale bars, 25 μm.

Article Snippet: Primary antibodies; Chicken polyclonal Anti-Vimentin, Rabbit polyclonal Anti-Tau (T22) (Merk), Mouse monoclonal Anti-MAP2 (Synaptic systems), Mouse monoclonal Anti-Tau (TAU-5) (ThermoFisher), Chicken polyclonal Anti-GFAP (Abcam) and Mouse monoclonal Anti-Tau (PHF-1) were diluted in 0.5% NGS 0.1% Triton X-100 in PBS and incubated overnight at 4°C.

Techniques: Staining, Expressing

Journal: iScience

Article Title: Exposure to fibrillar proteins leads to widespread infiltration but only mild tau pathology in cortical organoids

doi: 10.1016/j.isci.2026.115819

Figure Lengend Snippet: Pathology markers in the soluble organoid fraction after 12 weeks of exposure (A) Western blots of organoid lysate supernatant from αSYN, Aβ, and tau-exposed organoids (direct and astrocyte-mediated). Blots were stained for total tau (tau-5) and pathological phospho-tau (PHF-1, T22). Corresponding NOStain total protein normalization blots and uncut membranes are shown in . (B) Quantification of αSYN blots. (C) Quantification of Aβ blots. (D) Quantification of tau blots. n = 6 individual organoids for control and n = 5 for the treated analyzed by one-way ANOVA, with multiple comparisons relative to control. Data are presented as mean ± SD, p values are presented as following: ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.005.

Article Snippet: Primary antibodies; Chicken polyclonal Anti-Vimentin, Rabbit polyclonal Anti-Tau (T22) (Merk), Mouse monoclonal Anti-MAP2 (Synaptic systems), Mouse monoclonal Anti-Tau (TAU-5) (ThermoFisher), Chicken polyclonal Anti-GFAP (Abcam) and Mouse monoclonal Anti-Tau (PHF-1) were diluted in 0.5% NGS 0.1% Triton X-100 in PBS and incubated overnight at 4°C.

Techniques: Western Blot, Staining, Control

Journal: iScience

Article Title: Exposure to fibrillar proteins leads to widespread infiltration but only mild tau pathology in cortical organoids

doi: 10.1016/j.isci.2026.115819

Figure Lengend Snippet: Pathology markers in the insoluble organoid fraction after 12 weeks of exposure (A) Western blots of organoid insoluble pellets from αSYN, Aβ and tau exposed organoids (direct and astrocyte-mediated). Blots are stained for total tau (tau-5) and pathological phospho-tau (PHF-1, T22). Corresponding NOStain total protein normalization blots and uncut membranes are shown in . (B) Quantification of αSYN blots. (C) Quantification of Aβ blots. (D) Quantification of tau blots. n = 5 individual organoids analyzed by one-way ANOVA, with multiple comparisons relative to control. Data are presented as mean ± SD,∗∗ p < 0.01.

Article Snippet: Primary antibodies; Chicken polyclonal Anti-Vimentin, Rabbit polyclonal Anti-Tau (T22) (Merk), Mouse monoclonal Anti-MAP2 (Synaptic systems), Mouse monoclonal Anti-Tau (TAU-5) (ThermoFisher), Chicken polyclonal Anti-GFAP (Abcam) and Mouse monoclonal Anti-Tau (PHF-1) were diluted in 0.5% NGS 0.1% Triton X-100 in PBS and incubated overnight at 4°C.

Techniques: Western Blot, Staining, Control

Journal: iScience

Article Title: Exposure to fibrillar proteins leads to widespread infiltration but only mild tau pathology in cortical organoids

doi: 10.1016/j.isci.2026.115819

Figure Lengend Snippet: Control organoids display high levels of apoptosis and native tau pathology but lack full-length tau isoforms (A) Western blot analysis of unexposed organoids shows a positive signal for pathological tau (PHF-1, T22, pS231) and the astrocytic marker GFAP. Corresponding NOStain total protein normalization blots and uncut membranes are shown in . (B) Relative band intensity demonstrates large variations between the native organoids. Data are presented as values for individual organoids ( n = 15), and lines represent the median. (C) Representative images from apoptotic, TUNEL-labeled cells in organoids. (D) Quantification of TUNEL-positive cells in control and fibril-exposed organoids n = 3 individual organoids. Data are presented as mean ± SD. (E) Western blot analysis demonstrates that 3R-tau is the predominant tau isoform in 26 weeks organoids and that 4R-tau isoforms can barely be detected. Corresponding NOStain total protein normalization blots and uncut membranes are shown in . Scale bars, 250 μm.

Article Snippet: Primary antibodies; Chicken polyclonal Anti-Vimentin, Rabbit polyclonal Anti-Tau (T22) (Merk), Mouse monoclonal Anti-MAP2 (Synaptic systems), Mouse monoclonal Anti-Tau (TAU-5) (ThermoFisher), Chicken polyclonal Anti-GFAP (Abcam) and Mouse monoclonal Anti-Tau (PHF-1) were diluted in 0.5% NGS 0.1% Triton X-100 in PBS and incubated overnight at 4°C.

Techniques: Control, Western Blot, Marker, TUNEL Assay, Labeling

Journal: Progress in neurobiology

Article Title: Pathogenic Oligomeric Tau alters Neuronal RNA Processes through the Formation of Nuclear Heteromeric Amyloids with RNA-Binding Protein Musashi1

doi: 10.1016/j.pneurobio.2025.102742

Figure Lengend Snippet: Representative Co-IF images of MSI1 (green) and MSI2 (green) with Tau-13 (red) in ( A ) PCN P301S (magnification, ×20; scale bar, 100 μm) and ( B ) PCN P301S (magnification, ×100; scale bar, 20 μm). ( C ) Representative Co-IF images in PCN P301S of MSI1 (green) with Tau-13 (red). Magnification, ×100; scale bar, 20 μm. Bottom, colocalizing image of MSI1/Tau-13 (gray) (scale bar, 10 μm). Right panel, PCC scatterplots for the whole image and the isolated nuclei (green box). ( D ) Representative Co-IF images in PCN P301S of MSI2 (green) with Tau-13 (red). Magnification, ×100; scale bar, 20 μm. Bottom, colocalizing image of MSI2/Tau-13 (gray) (scale bar, 10 μm). Right panel, PCC scatterplots for selected MSI2− and MSI2+ cell bodies. ( E ) Pearsons’s correlation coefficient graphical representation of MSI1-Tau colocalization and MSI2-Tau colocalization in PCNs. Asterisks showing a statistically significant difference between MSI1 and MSI2 fluorescent signals colocalization with Tau13 fluorescent signal. ( F ) Schematic approach to studying labeled Tau monomers for cellular and nuclear internalization using flow cytometry. Representative cell and nuclear fluorescence after ( G ) 1 hour or ( H ) 2 hours of incubation with 0.5 μM rTauM-AF488. ( I ) Representative immunofluorescence of MSI1 (green in merged channel) in PCN P301S treated with 0, 0.1, 0.25, or 0.5 μM rTauO-AF568 (red in merged channel). Magnification, ×20; scale bar, 100 μm. ( J ) Representative high-magnification (×100; scale bar, 20 μm) immunofluorescence of MSI1 (green in merged channel) and rTauO-AF568 (red in merged channel) in PCN P301S . Each MSI1 and rTauO-AF568 immunofluorescence image is presented as a single channel (gray). ( K ) Reverse transcriptase–quantitative polymerase chain reaction of MSI1 in PCN P301S treated with 0, 0.1, 0.25, or 0.5 μM rTauO. 0 vs 0.1 μM (unpaired t test, * P = .0102); 0 vs 0.25 μM (unpaired t test, ** P = .0030); 0 vs 0.5 μM (unpaired t test, * P = .0157). ( L ) Reverse transcriptase–quantitative polymerase chain reaction of MSI1 in PCN P301S treated with 0, 0.1, 0.25, or 0.5 μM rTauM. 0 vs 0.1 μM (unpaired t test, *** P = .0005); 0 vs 0.25 μM (unpaired t test, P = .0594, NS); 0 vs 0.5 μM (unpaired t test, ** P = .0019). Representative Western blot and quantification of MSI1 in ( M-N ) cytoplasm, ( O-P ) nucleus, ( Q-R ) cell membrane, and ( S-T ) cytoskeleton fractions of PCN P301S treated with 0, 0.1, 0.25, or 0.5 μM rTauO.Note: Bar graphs represent relative density of total MSI1 in each fraction normalized to compartmentspecific loading controls: β-actin for cytoplasm, histone 3 for nucleus, N-methyl-D-aspartate receptor 1 for cell membrane, and β-III tubulin for cytoskeleton. Multiple comparisons with two-way analysis of variance compared each compartment and concentration. Ordinary one-way ANOVA and Dunnett’s Multiple tests compared 0.1, 0.25, and 0.5 μM Tau oligomers or monomers vs untreated (0.0 μM) PCNs. All bar graphs with individual plots are represented as mean (SD). Abbreviations: AF488, Alexa Fluor 488; AF568, Alexa Fluor 568; DAPI, 4′,6-diamidino-2-phenylindole; mMSI, monomeric Musashi; MSI, Musashi; MW, molecular weight; NMDAR, N-methyl-D-aspartate receptor; NS, not significant; PCC, Pearson correlation coefficient; PCN, primary cortical neuron; ROI, region of interest; rTauM, recombinant Tau monomer; rTauO, recombinant Tau oligomer; WT, wild type.

Article Snippet: P301S-Tau mice (B6;C3-Tg(Prnp-MAPT*P301S)PS19Vle/J; male hemizygous for Tg(Prnp-MAPT*P301S)PS19Vle; 008169, The Jackson Laboratory) overexpress a mutant form of human Tau (P301L mutation in MAPT , specifically the 4R/2N isoform) under the control of the neuron-specific murine prion protein promoter (Prnp).

Techniques: Isolation, Labeling, Flow Cytometry, Fluorescence, Incubation, Immunofluorescence, Reverse Transcription, Real-time Polymerase Chain Reaction, Western Blot, Membrane, Concentration Assay, Molecular Weight, Recombinant

Journal: Progress in neurobiology

Article Title: Pathogenic Oligomeric Tau alters Neuronal RNA Processes through the Formation of Nuclear Heteromeric Amyloids with RNA-Binding Protein Musashi1

doi: 10.1016/j.pneurobio.2025.102742

Figure Lengend Snippet: ( A ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cytoplasm fraction of PCN P301S exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( B ) Quantification of cytoplasm T18 relative density as a function of β-actin. ( C ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cell membrane fraction of PCN P301S exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( D ) Quantification of cell membrane T18 relative density as a function of NMDAR1. ( E ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the nucleus fraction of PCN P301S exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( F ) Quantification of nucleus T18 relative density as a function of histone 3. ( G ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cytoskeleton fraction of PCN P301S exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( H ) Quantification of cytoskeleton T18 relative density as a function of β-III tubulin. ( I ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cytoplasm fraction of PCN WT exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( J ) Quantification of cytoplasm T18 relative density as a function of β-actin. ( K ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cell membrane fraction of PCN WT exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( L ) Quantification of cell membrane T18 relative density as a function of NMDAR1. ( M ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the nucleus fraction of PCN WT exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( N ) Quantification of nucleus T18 relative density as a function of histone 3. ( O ) Western blot of total Tau (anti-Tau-13 antibody, upper blot) and misfolded Tau aggregates (anti-T18 antibody, bottom blot) in the cytoskeleton fraction of PCN WT exposed to 0, 0.1, 0.25, or 0.5 μM rTauO. ( P ) Quantification of cytoskeleton T18 relative density as a function of β-III tubulin.Note: The loading controls for each fraction were β-actin for the cytoplasm, histone 3 for the nucleus, NMDAR1 for the cell membrane, and β-III tubulin for the cytoskeleton. Statistical differences in T18 relative density were evaluated with a one-way analysis of variance. Ordinary one-way ANOVA and Dunnett’s Multiple tests compared 0.1, 0.25, and 0.5 μM Tau oligomers vs untreated (0.0 μM) PCNs. All bar graphs with individual plots are represented as mean (SD). Abbreviations: NMDAR, N-methyl-D-aspartate receptor; NS, not significant; PCN, primary cortical neuron; rTauO, recombinant Tau oligomer; WT, wild type.

Article Snippet: P301S-Tau mice (B6;C3-Tg(Prnp-MAPT*P301S)PS19Vle/J; male hemizygous for Tg(Prnp-MAPT*P301S)PS19Vle; 008169, The Jackson Laboratory) overexpress a mutant form of human Tau (P301L mutation in MAPT , specifically the 4R/2N isoform) under the control of the neuron-specific murine prion protein promoter (Prnp).

Techniques: Western Blot, Membrane, Recombinant

Journal: Cell Reports Medicine

Article Title: Neuronal PPP2R5C in plasma is a potential biomarker for early diagnosis of Alzheimer’s disease

doi: 10.1016/j.xcrm.2026.102631

Figure Lengend Snippet: PPP2R5C interacts with Tau and attenuates its expression (A) Co-immunoprecipitation analysis demonstrating the interaction between PPP2R5C and Tau protein. (B) Representative western blots immunostained for t-Tau, p-Tau T181, p-Tau S202, and p-Tau S396, in HEK293 cell lysates following PPP2R5C overexpression. (C) Quantification of t-Tau, p-Tau T181, p-Tau S202, and p-Tau S396, normalized to vector ( n = 6). (D) Representative western blots showing t-tau, p-Tau T181, p-Tau S202, and p-Tau S396 in primary neurons from Tau P301S mice following PPP2R5C overexpression. (E) Quantification of t-Tau, p-Tau T181, p-Tau S202, and p-Tau S396 levels, normalized to vector ( n = 6). (F and G) Double-labeling immunofluorescence analysis of GFP (green) and t-Tau/p-Tau T181 (red) was conducted on primary Tau P301S neurons after PPP2R5C overexpression. Scale bars, 10 μm. (H and I) Quantification of t-tau and p-Tau T181 fluorescence intensities ( n = 6). (J) Representative DiI staining shows the difference in spine density in tau P301S neurons after PPP2R5C overexpression. Scale bar: 10 μm. (K) Quantification of the density of spines ( n = 10). All the western blot data are representative of three independent experiments. Quantification data are expressed as mean ± SEM (∗∗ p < 0.01 and ∗∗∗ p < 0.001 with Student’s t test).

Article Snippet: Tau P301S mice , Jackson Labs , Cat# 008169.

Techniques: Expressing, Immunoprecipitation, Western Blot, Over Expression, Plasmid Preparation, Labeling, Immunofluorescence, Fluorescence, Staining

Journal: Cell Reports Medicine

Article Title: Neuronal PPP2R5C in plasma is a potential biomarker for early diagnosis of Alzheimer’s disease

doi: 10.1016/j.xcrm.2026.102631

Figure Lengend Snippet: Overexpression of PPP2R5C in Tau P301S mice reduces AD-like pathogenesis and rescues cognitive function (A) Schematic representation of the experimental design. Two-month-old Tau P301S mice were injected with either AAV-hSyn-EGFP or AAV-hSyn-PPP2R5C-EGFP. Mice were sacrificed 6 months after AAV injection. (B and C) Morris water maze analysis as escape latency (s) and escape latency on day 4 (s). (D) Probe trial performance of Morris water maze test. (E) Swim speed of mice injected with AAVs encoding EGFP or PP2R5C-EGFP ( n = 8–10 mice per group). (F) Time spent in the novel arm in the Y-maze test ( n = 8–10 mice per group). (G, I, and K) Representative immunostaining images of t-Tau, p-Tau T181, and AT8 in the hippocampus of Tau P301S mice injected with AAVs encoding EGFP or PPP2R5C-EGFP. Scale bars: 200 μm for 4× images and 20 μm for magnified images. (H, J, and L) Quantification of immunoreactivity for t-Tau, p-Tau T181, and AT8 ( n = 5 mice per group). (M and N) Representative western blots showing Tau pathology in mouse brain tissue following PPP2R5C overexpression ( n = 6 mice per group). (O) Golgi staining revealed the dendritic spines in the apical dendritic layer of the CA1 region. Scale bar, 10 μm. (P) Quantification of spine density ( n = 6 mice per group). (Q) Representative electron microscopy of the synapse structures. Arrows indicate synapses. Scale bar, 1 μm. (R) Quantification of synaptic density ( n = 6 mice per group). All the western blot data are representative of three independent experiments. Quantification data are expressed as mean ± SEM (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and n.s., no statistics, Student’s t test).

Article Snippet: Tau P301S mice , Jackson Labs , Cat# 008169.

Techniques: Over Expression, Injection, Immunostaining, Western Blot, Staining, Electron Microscopy

Journal: Cell Reports Medicine

Article Title: Neuronal PPP2R5C in plasma is a potential biomarker for early diagnosis of Alzheimer’s disease

doi: 10.1016/j.xcrm.2026.102631

Figure Lengend Snippet: Knockdown of PPP2R5C in Tau P301S mice worsens cognitive dysfunctions (A) Schematic representation of the experimental design. Two-month-old Tau P301S mice were injected with either AAV-sh-Ctrl-EGFP or AAV-sh-PPP2R5C-EGFP. Mice were sacrificed 4 months after AAV injection. (B and C) Morris water maze analysis as escape latency (s) and escape latency on day 4 (s). (D) Probe trial performance of Morris water maze test. (E) Swim speed of mice injected with AAVs encoding sh-Ctrl-EGFP or sh-PPP2R5C-EGFP ( n = 8–10 mice per group). (F) Time spent in the novel arm in the Y-maze test ( n = 8–10 mice per group). (G, I, and K) Representative immunostaining images of t-Tau, p-Tau T181, and AT8 in the hippocampus of Tau P301S mice injected with AAVs encoding sh-Ctrl-EGFP or sh-PPP2R5C-EGFP. (H, J, and L) Quantifying immunoreactivity for t-Tau, p-Tau T181, and AT8 ( n = 4 mice per group). Scale bars: 200 μm for 4× images and 20 μm for magnified images. (M and N) Representative western blots showing Tau pathology in mouse brain tissue following PPP2R5C knockdown ( n = 6). (O) Golgi staining revealed the dendritic spines in the apical dendritic layer of the CA1 region. Scale bar, 10 μm. (P) Quantification of spine density ( n = 6 mice per group). (Q) Electron microscopy of synapses (left) and high magnification of synapses (right). Scale bar: 2 μm in the left panel, 200 μm in the right panel. (R) Quantification of synaptic density ( n = 6 mice per group). All the western blot data are representative of three independent experiments. Quantification data are expressed as mean ± SEM (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and n.s., no statistics, Student’s t test).

Article Snippet: Tau P301S mice , Jackson Labs , Cat# 008169.

Techniques: Knockdown, Injection, Immunostaining, Western Blot, Staining, Electron Microscopy

Journal: Cell Reports Medicine

Article Title: Neuronal PPP2R5C in plasma is a potential biomarker for early diagnosis of Alzheimer’s disease

doi: 10.1016/j.xcrm.2026.102631

Figure Lengend Snippet: PPP2R5C promotes Tau degradation and dephosphorylation by regulating autophagy and PP2A activity (A) Representative western blots show autophagy-lysosome inhibitors NH4Cl, Leu, and CQ prevent PPP2R5C-derived Tau degradation. (B) Quantifying relative Tau, p-Tau T181, p-Tau S202, and p-Tau S396 protein levels ( n = 6). (C) EM morphometric analysis of autophagic vacuoles in conditions of starvation combined with OA treatment and autophagic flux blockade combined with (PPP2R5C + LP) or without (PPP2R5C) treatment. Scale bar, 1 μm. (D) Representative IF images of AT8 and p62 after Tau P301S primary neurons infected with GFP-PPP2R5C/shPPP2R5C lentivirus. Scale bar, 10 μm. (E) Quantification of fluorescence density of p62 in neurons. ( n = 10). (F and H) Representative IF images of SH-SY5Y cells co-transfected with tandem mCherry-GFP-tagged autophagy marker LC3 plus empty vector or FLAG-PPP2R5C or siPPP2R5C. Autophagosomes were visualized with yellow dots (mCherry and GFP co-localization) and autolysosomes were identified as red dots (mCherry). Scale bars: 10 μm in normal and 2 μm in Enlargement. (G and I) Quantification of puncta ratio of yellow vs. red ( n = 10). (J) Enzymatic reaction kinetics of PP2A with different concentrations of pThr peptide. PP2A was isolated from HEK293 cells with the treatment of a PP2A inhibitor OA, FLAG-PPP2R5C, or siPPP2R5C ( n = 6). (K) Western blot confirms the changes in PPP2R5C levels. All the western blot data are representative of three independent experiments. Quantification data are expressed as mean ± SEM (∗∗ p < 0.01, ∗∗∗ p < 0.001, and n.s., no statistics, Student’s t test).

Article Snippet: Tau P301S mice , Jackson Labs , Cat# 008169.

Techniques: De-Phosphorylation Assay, Activity Assay, Western Blot, Derivative Assay, Infection, Fluorescence, Transfection, Marker, Plasmid Preparation, Isolation

Journal: Cell Reports Medicine

Article Title: Neuronal PPP2R5C in plasma is a potential biomarker for early diagnosis of Alzheimer’s disease

doi: 10.1016/j.xcrm.2026.102631

Figure Lengend Snippet: PPP2R5C triggers autophagy through ULK1-PPP2R5C direct binding activation (A) Western blot showing p -ULK1 Ser556 negatively correlated with PPP2R5C expression. (B) Binding positions and interaction mode analysis of proteins ULK1 and PPP2R5C. The binding interface was shown as a surface, and each protein was shown as a cartoon (right). The detailed molecular interactions of salt bridges, hydrogen bonds, and hydrophobic interactions were shown in the enlarged image, and residues on the protein interface are shown as sticks. (C) Co-immunoprecipitation assay to detect the interaction between PPP2R5C and ULK1 in HEK293 cells with FLAG-PPP2R5C or FLAG vector transfection. The co-precipitated ULK1 was subsequently detected by western blot analysis. (D) PPP2R5C and ULK1 interaction determined by co-immunoprecipitation and western blot in the cortex of WT and Tau P301S. (E) Immunofluorescence co-localization was used to observe the spatial location of PPP2R5C and ULK1 in the TauP301S and their WT littermates. Scale bars: 50 μm in normal and 20 μm in Enlargement. (F) Quantification of colocalization in (E) ( n = 5). (G) Mechanism diagram. In the early stages of AD, PPP2R5C protein levels begin to decrease. As a PP2A enzyme catalytic subunit B family member, PPP2R5C plays a role in AD pathology by influencing Tau protein phosphorylation. Additionally, the reduction of PPP2R5C affects the ULK1-PPP2R5C-autophagy pathway, resulting in elevated total Tau (t-Tau) protein levels, further contributing to AD progression. All the western blot data are representative of three independent experiments. Quantification data are expressed as mean ± SEM (∗∗ p < 0.01, Student’s t test).

Article Snippet: Tau P301S mice , Jackson Labs , Cat# 008169.

Techniques: Binding Assay, Activation Assay, Western Blot, Expressing, Co-Immunoprecipitation Assay, Plasmid Preparation, Transfection, Immunoprecipitation, Immunofluorescence, Phospho-proteomics