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StressMarq
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Sangon Biotech
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Elabscience Biotechnology
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Biofluids Inc
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Cell Signaling Technology Inc
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Peptide Institute
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Elan Drug Technologies
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Journal: Translational Psychiatry
Article Title: Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice
doi: 10.1038/s41398-026-04002-9
Figure Lengend Snippet: ( A - C ) Aβ40 and Aβ42 levels in the soluble TBS fractions ( A ), detergent soluble (TBS-X) fractions ( B ), and insoluble neutralized formic acid (FA) fractions ( C ) of cortical brain homogenates in the 5xFAD mice were measured by ELISA at 8 months of age, normalized to protein concentrations of each fraction. ( D ) Soluble oligomeric Aβ (oAβ) levels in the TBS-X fractions of cortical brain homogenates in the 5xFAD mice were measured by ELISA at 8 months of age, normalized to protein concentrations. ( E, F ) Amounts of full-length APP in the TBS-X fractions of mouse cortical lysates were measured by western blot at 8 months of age, normalized to those of β-actin (ACTB). Data are expressed as means ± SEM (GFP: N = 12; APOE3: N = 18; APOE3Ch: N = 13; Open circles: females, closed circles: males). Injection group differences were analyzed using two-way ANOVA, with Tukey’s multiple comparisons test, adjusting for sex. *, P < 0.05; **, P < 0.01.
Article Snippet:
Techniques: Enzyme-linked Immunosorbent Assay, Western Blot, Injection
Journal: Translational Psychiatry
Article Title: Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice
doi: 10.1038/s41398-026-04002-9
Figure Lengend Snippet: ( A ) Isogenic iPSC-derived astrocytes (iPSC-ACs) with homozygous APOE3 (left) and APOE3Ch (right) were immunostained for GFAP (green) and S100b (red). DAPI (blue) stains nuclei. Scale bars: 100 µm. ( B ) APOE mRNA levels in the iPSC-ACs were measured by RT-qPCR, normalized to those of β-actin ( ACTB ). ( C, D ) Amounts of APOE in the conditioned medium (CM) from iPSC-ACs were measured by western blot, normalized to protein amounts of cell lysates. ( E ) Effects of the CM from iPSC-ACs on Aβ42 aggregation was assessed by western blot using 6E10 antibody. ( F - G ) Populations of Aβ fibrils (F; > 150 kDa), oligomers (G; 37–150 kDa), and monomers ( H ; < 10 kDa) were quantified. Data expressed as means ± SEM (n = 3–5 independent differentiation batches). Group differences were analyzed using two-tailed student t-test or one-way ANOVA with Tukey’s multiple comparisons test. *, P < 0.05.
Article Snippet:
Techniques: Derivative Assay, Quantitative RT-PCR, Western Blot, Two Tailed Test
Journal: Alzheimer's & Dementia
Article Title: Bile acids are associated with baseline and longitudinal amyloid and tau pathology in patients with Alzheimer's disease
doi: 10.1002/alz.71307
Figure Lengend Snippet: LCA‐family BAs were associated with amyloid and tau pathologies. Heatmaps depicting the relationships between BAs levels and amyloid or tau pathology. Plasma Aβ42, Aβ42/40, p‐tau181, and amyloid PET centiloid were obtained from the CPAS cohort, and CSF Aβ42, CSF p‐tau, and amyloid PET centiloid levels were measured in the ADNI cohort. The colors of the dots/square indicate β coefficients (blue, negative; red, positive), and the symbol * indicates P FDR < 0.05. (A) BA–pathology associations at the population level, with the dot size reflecting ‐log 10 ( P FDR ). (B–E) Subgroup‐specific (B, CU group; C, CI group; D, A‐ group; E, A+ group) correlations between the levels of the LCA‐family and DA‐family BAs and pathological markers. (F–M) Logistic regression models assessing the ability of the LCA‐family and DCA‐family BAs to predict amyloid/tau pathology (adjusted for sex, age, and APOE genotype). ADNI, Alzheimer's Disease Neuroimaging Initiative; APOE, apolipoprotein E; BA, bile acid; CI, cognitively impaired; CPAS, Chinese Preclinical Alzheimer's Study; CSF, cerebrospinal fluid; CU, cognitively unimpaired; DCA, deoxycholic acid; LCA, lithocholic acid; PET, positron emission tomography.
Article Snippet: All samples were measured in duplicate on the
Techniques: Clinical Proteomics, Positron Emission Tomography
Journal: RSC Advances
Article Title: Graphene field-effect transistor based multiplexed sensing platform for simultaneous detection of multiple Alzheimer's disease biomarkers
doi: 10.1039/d5ra07384g
Figure Lengend Snippet: The electrical sensing results of GFET biosensor. (a) (PBASE: 5 mM; aptamer: 5 µM). (b) GFET transfer curves for Aβ42 detection under identical functionalization. (c) Four regions functionalized with Aβ42 and hsa-miR-125b aptamers in 1× PBS, with Aβ42 target added for measuring the average signal response at different concentrations. (d) Four regions functionalized with Aβ42 and hsa-miR-125b aptamers in 1× PBS, with hsa-miR-125b target added for measuring the average signal response at different concentrations. (e) The sensor response as a function 125b concentration, with mean, standard deviation, median, and a linear fitting curve. (f) The sensor response as a function Aβ42 concentration, with mean, standard deviation, median, and a linear fitting curve ( n ≥ 13, n is number of sensors used for each measurement) ( n ≥ 13, n is number of sensors used for each measurement).
Article Snippet: Aβ42 and Aβ40 peptides, hsa-miR-125b RNA sequence, the hsa-miR-125b complementary DNA probe and the
Techniques: Concentration Assay, Standard Deviation
Journal: RSC Advances
Article Title: Graphene field-effect transistor based multiplexed sensing platform for simultaneous detection of multiple Alzheimer's disease biomarkers
doi: 10.1039/d5ra07384g
Figure Lengend Snippet: Mixed sample detection results. (a) Higher concentration of Aβ42 biomarker vs. lower concentration of hsa-miR-125b biomarker. The absolute concentrations were (Aβ42 : 125b): 10 pM : 1 fM (10 000 : 1); 50 nM : 50 pM (1000 : 1); and 100 nM : 1 nM (100 : 1). (b) Higher concentration of hsa-miR-125b biomarker vs. lower concentration of Aβ42 biomarker. The absolute concentrations were (125b : Aβ42): 100 nM : 1 fM (10 8 : 1), 100 nM : 1 pM (10 6 : 1), and 50 nM : 50 pM (10 3 : 1). (c) Fixed concentration of Aβ40 biomarker and varying concentrations of hsa-miR-125b ( n ≥ 13, n is number of sensors used for each measurement).
Article Snippet: Aβ42 and Aβ40 peptides, hsa-miR-125b RNA sequence, the hsa-miR-125b complementary DNA probe and the
Techniques: Concentration Assay, Biomarker Discovery
Journal: bioRxiv
Article Title: Reduced LACTB expression in myeloid cells is associated with elevated succinylcarnitine levels and reduced Alzheimer’s disease risk
doi: 10.64898/2026.03.24.711053
Figure Lengend Snippet: A) Diagram summarizing the experimental design for xenotransplantation of human microglia precursors in mice. B) No differences in engraftment between human LACTB KO and WT microglia in hCSF1-5xFAD mice. C) Metabolomics in human LACTB KO or WT microglia isolated from the brains of hCSF1-5xFAD mice (n=2 clones per genotype, 2 mice injected per clone). D) Pathways enriched in GSEA analysis of bulk RNAseq data from human LACTB KO microglia isolated from the brain of hCSF1-5xFAD mice compared to human WT microglia (n=2 clones per genotype, 2 mice injected per clone). E-J) Immunostaining analysis of the number of human microglia (Ku80+Iba1+ cells) associated per plaque (Aβ42) (E), the area covered by plaques and the average plaque size (Aβ42) (F), the plaque compaction (ThioS/MOAB ratio) (G), and the area covered by active (LGALS3 (H), CD9 (I) markers) or antigen-presenting microglia (HLA marker (J)) microglia in hCSF1-5xFAD mice xenotransplanted with LACTB KO or WT human microglia (n=2 clones per genotype, 4-5 mice injected per clone). Graphs display individual data points (left) alongside estimated marginal means with 95% confidence intervals (right). For the raw data dot colors indicate distinct xenotransplanted microglia clones. Statistical details are provided in .
Article Snippet: For additional staining for amyloid pathology, sections were washed again in TBST buffer three times and incubated with the
Techniques: Isolation, Clone Assay, Injection, RNA sequencing, Immunostaining, Marker