Fig 1: The changes of mGluR5 and TSPO expression induced by LPS and KD in SN. The numbers of mGluR5+ microglia cells (a, c), TSPO+ microglia cells (b, d), and the levels of aceH3K9 in mGluR5 promoter region (e) and mGluR5 mRNA expression (f) were compared among multiple groups. Data were presented as the mean ± SEM. ***P < 0.001; **P < 0.01; *P < 0.05; LPS, lipopolysaccharide; KDp, preventive intervention with KD prior to the PD onset; KDt, therapeutic intervention with KD after the PD onset.
Fig 2: Brain TSPO and DAT PET imaging using 18F-DPA-714 and 18F-FP-CIT. The SUVs of 18F-DPA-714 (a) and 18F-FP-CIT (b) in substantia nigra, and those of 18F-FP-CIT in striatum (c) were compared among different groups. Data were presented as the mean ± SEM. ***P < 0.001; **P < 0.01; *P < 0.05; LPS, lipopolysaccharide; KDp, preventive intervention with KD prior to the PD onset; KDt, therapeutic intervention with KD after the PD onset.
Fig 3: Effect of TSPO deletion on the accumulation of esterified cholesterol in rat models.(A–J) ORO staining of adrenal glands from WT, HE, and HO rats. HO rats exhibited increased ORO staining of neutral lipids, which reflected esterified cholesterol in the steroidogenic tissues. (A–C) Male adrenal gland of Rat5; scale bar = 50 µm. (D–F) Male adrenal gland of Rat7; scale bar = 50 µm. (G–J) The distribution of esterified cholesterol in Rat5 and Rat7 testis. Esterified cholesterol was estimated using ORO staining of testis from Rat5 (G–H) and Rat7 (I–J). WT, HE, and HO rats are indicated, and the highlighted area is magnified below each panel. Lc, Leydig cell. Green arrows indicate lipid droplets; scale bar = 100 µm.
Fig 4: Effect of TSPO polymorphism on PK 11195/cholesterol binding in vitro.Saturation isotherms of [3H]-PK 11195 and [3H]-cholesterol binding to reconstituted mouse TSPO WT and mutant (Ala/Thr) proteins. (A) [3H]-PK 11195 and [3H]-cholesterol-specific binding studies were performed using 200 ng of mouse WT TSPO. Inset, electron micrographs of WT TSPO proteoliposomes stained with 2% uranyl acetate after SDS elimination using biobeads. (B) 200 ng of mouse Ala147Thr mutant reconstituted TSPO was used to study specific binding with [3H]-PK 11195 and [3H]-cholesterol. Inset, electron micrographs of mutant TSPO proteoliposomes stained with 2% uranyl acetate after SDS elimination using biobeads. [3H]-PK 11195 concentrations varied from 0.1 to 15 nM; [3H]-cholesterol concentrations varied from 0.1 to 30 nM. Values shown represent the mean (SE) from three independent experiments. The extra sum-of-squares F-test was used to compare the fitting curves and the P-values presented (values of P < 0.05 are statistically significant to reject the null hypothesis).
Fig 5: Effect of genome editing of rat Tspo on the PK 11195 binding and immunofluorescence staining.(A and B) Representative optical bright-field images were used as controls to show the morphology of adrenal sections used for the binding assay. (C and D) Autoradiographic localization of PK 11195 in the adrenal glands from WT, Rat5, and Rat7. (C) Autoradiographic images of tissue incubation with 1.2 nmol/l [3H]-PK 11195 in 50 mmol/l Tris–HCl (pH 7.4) for 30 min at room temperature (22°C). [3H]-PK 11195 binding was analyzed by digital autoradiography using a Beta-Imager 2000 (Biospace Laboratory, Paris, France). Binding intensities are presented in false color using the ImageJ look-up table ‘royal’. (D) Autoradiographic images of tissue incubation as in C but additionally with cold PK 11195 to show nonspecific binding. (E) Saturation isotherm of [3H]-PK 11195-specific binding studies using 15 µg of protein extracted from adrenal glands of WT1, WT2, and TSPO KO Rat5-1 and Rat5-2. The KD and Bmax of PK 11195 binding to WT1 adrenal protein extract were 3.84 ± 1.62 and 84.95 ± 11.86, respectively, and for WT2, adrenal protein extract was 3.04 ± 0.96 and 60.40 ± 5.67, respectively. (F and G) IF staining of cryosections of Rat5 adrenal gland using rabbit polyclonal anti-TSPO Ab (NP155). Images were obtained using laser scanning confocal microscopy (A) and epifluorescence imaging using an inverted microscope (B). The rat genotype (WT, HE, and HO) is indicated. Scale bar = 100 µm.
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