Journal: Molecular Neurodegeneration

Article Title: A pharmacological chaperone improves memory by reducing Aβ and tau neuropathology in a mouse model with plaques and tangles

doi: 10.1186/s13024-019-0350-4

Figure Lengend Snippet: Antibodies used in the study

Article Snippet: PS1 , Rabbit , WB , Cell Signaling , 3622S.

Techniques:

Journal: Molecular Neurodegeneration

Article Title: A pharmacological chaperone improves memory by reducing Aβ and tau neuropathology in a mouse model with plaques and tangles

doi: 10.1186/s13024-019-0350-4

Figure Lengend Snippet: Pharmacological chaperone lowers Aβ levels and deposition in 3xTg mice. a Radioimmunoprecipitation assay (RIPA)-soluble and formic acid (FA)-extractable Aβ1–40 levels in cortex of 3xTg mice treated with TPT (3xTg/TPT) or controls (3xTg) were measured by sandwich enzyme-linked immunosorbent assay. Values represent mean ± standard error of the mean (* p < 0.05, n = 6). b RIPA-soluble and FA-extractable Aβ1–42 levels in cortex of 3xTg mice treated with TPT (3xTg/TPT) or controls (3xTg) were measured by sandwich enzyme-linked immunosorbent assay. Values represent mean ± standard error of the mean (* p < 0.05, n = 6). c Representative images of brain sections from 3xTg mice treated with TPT (3xTg/TPT) or control (3xTg) immuno-stained with 4G8 antibody to detect Aβ immunoreactivity (scale bar: 500 μm). d Quantification of the area occupied by Aβ immunoreactivity in brains of 3xTg mice treated with TPT or controls (3xTg). Values represent mean ± standard error of the mean (* p < 0.05, n = 4). e Representative Western blots of amyloid precursor protein (APP), sAPPα, sAPPβ, CTFs, BACE-1, ADAM10, APH-1, Nicastrin, Pen-2, PS1 and SorLA in cortex homogenates from 3xTg mice treated with TPT (3xTg/TPT) or controls (3xTg). f Densitometric analyses of the immunoreactivities to the antibodies shown in the previous panel. Values represent mean ± standard error of the mean (* p < 0.05, n = 3)

Article Snippet: PS1 , Rabbit , WB , Cell Signaling , 3622S.

Techniques: Radio Immunoprecipitation, Sandwich ELISA, Control, Staining, Western Blot

Journal: Frontiers in Immunology

Article Title: Novel prognostic signature unveils PSEN1 contributes to depression-induced lung adenocarcinoma progression

doi: 10.3389/fimmu.2026.1681306

Figure Lengend Snippet: PSEN1 induced by depression promotes LUAD proliferation. (A) Process of the animal experiment; (B) immobility times in the forced swimming test (FST) were compared between Con and CR mice (n=4); (C) total locomotion and central zone activity in OFT were compared between Con and CR mice (n=4); (D) total duration and migration to light box in LDBT were compared between Con and CR mice (n=4); (E) the LLC tumor growth curves and the end-point tumor weights and sizes were represented (n=4); (F) the mRNA levels of 14 DRGs in tumor tissues were tested by qRT-PCR (n=3); (G) immunofluorescence detection of PSEN1 protein expression in tumor tissues; (H) Validation of the overexpression of PSEN1 in A549 and H1299 cells by western blot; (I) validation of the overexpression of PSEN1 in A549 and H1299 cells by qRT-PCR; (J–L) determine the effect of PSEN1 overexpression on the proliferation of A549 and H1299 cells through CCK-8 (J) , colony formation assay (K) , and EdU (L) ; (M) survival curve of LUAD patients with low or high expression of PSEN1; (N) protein levels of PSEN1 in normal tissue and LUAD in CPATC database; (O) representative images ofimmunohistochemistry of PSEN1 in normal tissue and LUAD in HPA database. Data are represented as the mean ± standard error of the mean (SEM). *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001 by an unpaired Student’s t-test.

Article Snippet: After standard procedures for deparaffinization, rehydration, and blocking, the sections were subjected to overnight incubation at 4 °C with PSEN1 antibody (1:500, 16163-1-AP, Proteintech, China).

Techniques: Activity Assay, Migration, Quantitative RT-PCR, Immunofluorescence, Expressing, Biomarker Discovery, Over Expression, Western Blot, CCK-8 Assay, Colony Assay

Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

Article Title: TGF-β inhibits alveolar protein transport by promoting shedding, regulated intramembrane proteolysis, and transcriptional downregulation of megalin

doi: 10.1152/ajplung.00569.2016

Figure Lengend Snippet: Inhibition of γ-secretase and classical PKCs prevent the effect of TGF-β on megalin cell surface stability increasing megalin functionality. RLE-6TN cells were transfected with presenilin-1 (PS-1) or PKCα/β siRNA for 72 h and treated with TGF-β (20 ng/ml) for 10 h. Cells were then processed to detect megalin cell surface abundance by biotin-streptavidin pulldown assay (A and B) or to measure FITC-albumin binding and uptake (C). Results are shown as means ± SE. Two-way ANOVA and Šidák’s multiple comparisons, *P < 0.05; **P < 0.01; n = 5. D: RLE-6TN cells were co-transfected with PS-1 or PKC siRNA in the presence or absence of megalin (Meg) siRNA and FITC-albumin binding, and uptake were assessed. Boxes represent the median + quartiles; the ends of the whiskers show the minimum and maximum of all data. Two-way ANOVA and Tukey’s multiple comparisons, *P < 0.05; **P < 0.01; ****P < 0.0001 (compared with Scr control); §§§§P < 0.0001 (compared with Meg siRNA); ###P < 0.001; ####P < 0.0001 (compared with the corresponding single knockdown); n = 5. E: a representative Western blot of megalin knockdown in RLE-6TN cells. Scr, scrambled siRNA; PD, pulldown; KD, knockdown.

Article Snippet: Megalin antibody was obtained from Proteintech (Manchester, UK); MMP-2, MMP-9, PKCα/β, and presenilin-1 antibodies were from Santa Cruz Biotechnology; MMP-14 antibody was from Thermo Fisher (Schwerte, Germany); transferrin receptor antibody was purchased from Invitrogen (Karlsruhe, Germany), and Na, K-ATPase antibody was from Millipore (Darmstadt, Germany).

Techniques: Inhibition, Transfection, Binding Assay, Western Blot

Journal: Journal of Neuroinflammation

Article Title: Administration of anti-ERMAP antibody ameliorates Alzheimer’s disease in mice

doi: 10.1186/s12974-021-02320-x

Figure Lengend Snippet: Anti-ERMAP mAb does not alter the expression of APP expression and APP-processing enzymes. 3XTg-AD mice were injected with anti-ERMAP mAb, or control isotype Ab as in Fig. . Three and a half months later, the brains were harvested. A , B The expression levels of APP and PS-1 proteins as well as the APP cleavage products β-CTF and α-CTF were analyzed by Western blot. GAPDH was used as a loading control. A Representative Western blot images, B quantification of the expression levels of APP and PS-1 proteins. C qRT-PCR analysis of the relative expression levels of the genes for the APP-processing enzymes ADAM10, ADAM17, BACE1, and BACE2. D , E Western blot analysis of the expression levels of ADAM10, ADAM17 and BACE1 proteins. B , C , E The expression level of the protein or gene in control Ab-treated AD mice is defined as 1. The data are expressed as mean ± SD from one of three independent experiments with similar results (5 to 8 mice per group in each experiment)

Article Snippet: Primary antibodies include BACE1 (Santa Cruz), ADAM10 (Santa Cruz), ADAM17 (Millipore Sigma), Presenilin-1 (PS-1) (Novus Biologicals) and APP [to detect both full-length APP and C-terminal fragments (CTFs); CT695, ThermoFisher].

Techniques: Expressing, Injection, Control, Western Blot, Quantitative RT-PCR