Journal: Frontiers in Oncology

Article Title: Inhibition of HSP90 as a Strategy to Radiosensitize Glioblastoma: Targeting the DNA Damage Response and Beyond

doi: 10.3389/fonc.2021.612354

Figure Lengend Snippet: HSP90i by NW457 leads to downregulation of DNA damage response factors, impaired DNA damage repair, and reduced clonogenic survival in response to ionizing irradiation in human glioblastoma cells. (A) Transcriptomic profiling of regulators of the DNA damage response (DDR) in LN229 and T98G cells. mRNA expression levels were determined by qRT-PCR, normalized to a matrix of 3 reference genes (18S rRNA, δ-amino-laevulinate-synthase, and β2-microglobulin), and calibrated to the results of untransformed human astrocytes. For both cell lines, three replicates were analyzed and are displayed as x-fold log2-values. (B) Time course analysis of DDR regulator protein expression in LN229 and T98G cells upon HSP90i by 10 nM NW457. Arrowheads indicate the bands that were used for quantification. Protein levels were normalized to a matrix comprising vinculin and α-tubulin and are depicted as x-fold log2-values compared to the 0 h controls. (C) Immunofluorescence microscopy of γH2AX and 53BP1 DNA damage repair foci in LN229 and T98G cells upon irradiation at 2 Gy ± HSP90i by NW457. Cells were treated with NW457 (10 nM) or DMSO for 24 h, irradiated, and fixed at the indicated times. Cells were stained for γH2AX, 53BP1, and DNA and subjected to deconvolution immunofluorescence microscopy. Scale bar depicts 10 µm. (D) Quantification of DNA damage repair kinetics from (C) . γH2AX and 53BP1 double-positive foci in at least 20 randomly picked nuclei were counted by hand. Individual data points with superimposed means ± 95% confidence intervals are displayed, and overall curve comparison was performed by two-way ANOVA. (E) Clonogenic survival of LN229 and T98G cells upon irradiation at 0–8 Gy ± HSP90i by NW457. Cells were pre-treated with 10 nM NW457 or DMSO for 24 h followed by irradiation at the indicated doses, and colony formation was allowed for 13 d ± continuous NW457 treatment. Individual data points of 4 independent experiments are shown, linear-quadratic regression lines are superimposed, and overall curve comparison was performed by two-way ANOVA.

Article Snippet: Cells were stained with monoclonal mouse anti-γH2AX (Merck Millipore) and polyclonal rabbit anti-53BP1 (Bio-Techne, Wiesbaden, Germany) antibodies diluted in 3% isotonic bovine serum albumin and 0.1% Triton X-100 for 2 h at room temperature.

Techniques: Irradiation, Expressing, Quantitative RT-PCR, Immunofluorescence, Microscopy, Staining, Comparison

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: Primer sequences used in q-PCR.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques:

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: Analysis of sMaf expressions in the hippocampus of AD patients. The mRNA expressions of (a) MafF, (b) MafG, and (c) MafK in the hippocampus of AD patient databases. The mRNA expressions of (d) MafF, (e) MafG, and (f) MafK in the hippocampus of AD patients under Braak stages III-IV and V-VI. The correlations between (h) MafF, (i) MafG, and (j) MafK and GCLC in the hippocampus of AD patient databases. All data were presented as mean ± SEM. ∗ p < 0.05 and ∗∗ p < 0.01 versus the control group or the Braak stage III-IV group.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques: Control

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: Constitutive expressions of sMafs in different tissues. The mRNA expressions of (a) MafF, (b) MafG, and (c) MafK in the brain (hippocampus, cerebral cortex, cerebellum, and brainstem), liver, lung, and kidney. The relative expressions of sMafs were normalized to GAPDH ( n = 3). All data were presented as mean ± SEM.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques:

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: MafF expression was increased in response to A β -induced oxidative injury. The protein expressions of MafF, MafG, and MafK in the (a) hippocampus from APP/PS1 mice and in the (b) hippocampus from SD rats after A β injection and in (c) SH-SY5Y cells treated with A β (20 μ M, 48 h) ( n = 3–5). The relative expressions of proteins were normalized to GAPDH. All data were presented as mean ± SEM; ∗ p < 0.05 and ∗∗ p < 0.01 versus the C57 group, the sham group, or the control group.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques: Expressing, Injection, Control

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: MafF expression participated in the oxidative stress caused by A β . The protein expressions of GCLC in the (a) hippocampus from APP/PS1 mice and in the (c) hippocampus from SD rats after A β injection and in (e) SH-SY5Y cells treated with A β (20 μ M, 48 h). The GSH levels in the (b) hippocampus from APP/PS1 mice and in the (d) hippocampus from SD rats after A β injection and in (f) SH-SY5Y cells treated with A β (20 μ M, 48 h). The protein expressions of MafF, MafG, and MafK in SH-SY5Y cells transfected with MafF siRNA for 48 h (g). GSH level in SH-SY5Y cells transfected with MafF siRNA (10 nM) for 48 h with or without A β (20 μ M) treatment (6 h) (h) ( n = 3–7). The relative expressions of proteins were normalized to GAPDH. All data were presented as mean ± SEM; ∗ p < 0.05 and ∗∗ p < 0.01 versus the C57 group, the sham group, the control group, or the NC group; # p < 0.05 versus the NC+A β group.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques: Expressing, Injection, Transfection, Control

Journal: Disease Markers

Article Title: Responsive Expression of MafF to β -Amyloid-Induced Oxidative Stress

doi: 10.1155/2020/8861358

Figure Lengend Snippet: The expressions of sMafs in basal or under A β /H 2 O 2 treatment in different cell lines. The constitutive expressions of (a) MafF, (b) MafG, and (c) MafK in SH-SY5Y cells, HepG2 cells, and A549 cells. The protein levels of MafF, MafG, and MafK in (f) SH-SY5Y cells, (d, g) HepG2 cells, and (e, h) A549 cells treated with A β for 48 h or H 2 O 2 for 24 h ( n = 3–5). The relative expressions of sMafs were normalized to β -actin/GAPDH. All data were presented as mean ± SEM; ∗ p < 0.05 and ∗∗ p < 0.01 versus the control group.

Article Snippet: The primary antibodies were as follows: rabbit anti-GCLC antibody (1 : 10000, Abcam, UK), rabbit anti-MafF antibody (1 : 1000, Proteintech Group, Rosemont, IL, USA), rabbit anti-MafG antibody (1 : 2000, Novus Biologicals, CO, USA), rabbit anti-MafK antibody (1 : 5000, Abcam), and mouse GAPDH monoclonal antibody (1 : 5000, Proteintech Group).

Techniques: Control

Journal: Oncotarget

Article Title: Immunohistochemical profiling of receptor tyrosine kinases, MED12, and TGF-βRII of surgically resected small cell lung cancer, and the potential of c-kit as a prognostic marker

doi: 10.18632/oncotarget.14410

Figure Lengend Snippet: Distribution of RTKs, MED12, and TGF-βRII stratified by IHC total score in SCLC tumors as shown in Figure 2 (n=125)

Article Snippet: Rabbit anti-human polyclonal MED12 antibody (NB100-2357, Novus Biologicals, Littleton, CO, USA), rabbit anti-human polyclonal TGF-βRII antibody (NB100-91994, Novus Biologicals), rabbit anti-human polyclonal c-kit antibody (A4502, Dako, Glostrup, Denmark), rabbit anti-human polyclonal HER2 antibody (A0485, Dako), rabbit anti-human monoclonal c-Met antibody (EP1454Y, Abcam, Cambridge, UK), rabbit anti-human monoclonal VEGFRII antibody (#2479, CST, Danvers, MA, USA), mouse anti-human monoclonal EGFR antibody (31G7, Nichirei Biosciences, Tokyo, Japan), and mouse anti-human monoclonal ALK antibody (5A4, ab17127, Abcam) were used as first antibodies.

Techniques:

Journal: Oncotarget

Article Title: Immunohistochemical profiling of receptor tyrosine kinases, MED12, and TGF-βRII of surgically resected small cell lung cancer, and the potential of c-kit as a prognostic marker

doi: 10.18632/oncotarget.14410

Figure Lengend Snippet: Univariate analysis of the association between molecular expression and OS (n=107)

Article Snippet: Rabbit anti-human polyclonal MED12 antibody (NB100-2357, Novus Biologicals, Littleton, CO, USA), rabbit anti-human polyclonal TGF-βRII antibody (NB100-91994, Novus Biologicals), rabbit anti-human polyclonal c-kit antibody (A4502, Dako, Glostrup, Denmark), rabbit anti-human polyclonal HER2 antibody (A0485, Dako), rabbit anti-human monoclonal c-Met antibody (EP1454Y, Abcam, Cambridge, UK), rabbit anti-human monoclonal VEGFRII antibody (#2479, CST, Danvers, MA, USA), mouse anti-human monoclonal EGFR antibody (31G7, Nichirei Biosciences, Tokyo, Japan), and mouse anti-human monoclonal ALK antibody (5A4, ab17127, Abcam) were used as first antibodies.

Techniques: Expressing

Journal: Digestive diseases and sciences

Article Title: Inappropriate Angiogenic Response as a Novel Mechanism of Duodenal Ulceration and Impaired Healing

doi: 10.1007/s10620-011-1753-4

Figure Lengend Snippet: Increased levels of anti-angiogenic factors endostatin and angiostatin. Levels of anti-angiogenic factors endostatin (19 kDa) and angiostatin (50 kDa) measured by Western blot (a) and ELISA (b) in the duodenal mucosa after administration of cysteamine or propionitrile to rats. Ctrl: control. *P < 0.05

Article Snippet: The blot was blocked with a 5% solution of dry milk for 2 h, and incubated with antibodies against endostatin (Lab Vision, Fremont, CA, USA) and angiostatin (Novus Biologicals, Littleton, CO, USA) at 1:200 dilutions, VEGF (Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 1:200 dilution, and MMP2, MMP9, TIMP-1 and TIMP-2 (Santa Cruz Biotechnology) at 1:500 dilution.

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Control

Journal: Digestive diseases and sciences

Article Title: Inappropriate Angiogenic Response as a Novel Mechanism of Duodenal Ulceration and Impaired Healing

doi: 10.1007/s10620-011-1753-4

Figure Lengend Snippet: Effect of MMP2 inhibition on cysteamine-induced duodenal ulcer and expression of MMP2, TIMP-1, endostatin, and angiostatin. Inhibition of MMP2 by selective MMP2 inhibitor I attenuated cysteamine-induced duodenal ulceration (a), reduced protein expression and proteolytic activity of MMP2 (b), reduced levels of endostatin and angiostatin (c), and increased levels of VEGF (d) and TIMP-1 (e) in duodenal mucosa. *P < 0.05

Article Snippet: The blot was blocked with a 5% solution of dry milk for 2 h, and incubated with antibodies against endostatin (Lab Vision, Fremont, CA, USA) and angiostatin (Novus Biologicals, Littleton, CO, USA) at 1:200 dilutions, VEGF (Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 1:200 dilution, and MMP2, MMP9, TIMP-1 and TIMP-2 (Santa Cruz Biotechnology) at 1:500 dilution.

Techniques: Inhibition, Expressing, Activity Assay

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Relation of CXCR5 expression with clinicopathological parameters in 158 cases of SACC.

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Clinical significance of CXCR5 expression in SACC patients. ( A ) Immunohistochemical staining of CXCR5 in normal salivary gland (NSG), SACC without PNI (No-PNI), far away from nerve of SACC with PNI (Far-nerve), nerve invasion front of SACC with PNI (Nerve-front). ‘N’ represented nerve. (Bar: upper, 50 μm; lower, 20 μm) ( ** p < 0.01, *** p < 0.001). ( B ) Kaplan-Meier survival analysis on SACC patients with different expression status of CXCR5. The overall survival time for patients without or with low CXCR5 expression was longer than those with high CXCR5 expression (log-rank test, p < 0.0001).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing, Immunohistochemical staining, Staining

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Cox multivariate regression analysis of overall survival in SACC patients.

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: The expression of CXCR5 in normal salivary gland and SACC with different PNI status.

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Silencing CXCR5 attenuates migration, invasion and PNI in SACC cells. ( A ) Immunofluorescence and qRT-PCR analysis showed that CXCR5 expression was dramatically inhibited by siRNA treatment. ( B – D ) CXCR5 silence with siRNA or CXCR5 blockade with anti-CXCR5 antibody impeded migration, invasion and PNI of SACC-LM cells, (Bar: 100 μm). ( E ) Immunofluorescence and qRT-PCR analysis showed that CXCR5 level was significantly increased by CXCR5-overexpressing plasmid. ( F – H ) CXCR5 overexpression enhanced migration, invasion and PNI capacity of SACC-LM cells, (Bar: 100 μm) ( * p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Migration, Immunofluorescence, Quantitative RT-PCR, Expressing, Plasmid Preparation, Over Expression

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Schwann-like cell differentiation is involved in CXCR5 induced PNI in SACC cells. ( A ) CXCR5 silence with siRNA or CXCR5 blockade with anti-CXCR5 antibody downregulated the expression of Schwann cell markers, including S100A4, p75NTR, GFAP by qRT-PCR analyses. ( B ) CXCR5 overexpression upregulated the expression of S100A4, p75NTR, GFAP in SACC-LM cells. ( C ) CXCR5 silence with siRNA or CXCR5 blockade with anti-CXCR5 antibody resulted in the transformation of SACC-LM cells from spindle-like fibroblastic cellular morphology to epithelial plasticity with little pseudopodia, (Bar: 50 μm). ( D ) The heatmap of 8 differentially expressed miRNAs in SACC-LM cells transfected with control or si-CXCR5 on a scale from blue (low) to red (high). ‘Blue’ represents low expression, and ‘red’ represents high expression. ( E ) The microarray data of 8 differentially expressed miRNAs in the si-CXCR5 and control SACC-LM cells was confirmed by qRT-PCR. For qRT-PCR, U6 was used to normalize the Ct values. ( F ) CXCR5 overexpression upregulated the expression of miR-187 in SACC-LM cells, ( * p < 0.05, ** p < 0.01).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Cell Differentiation, Expressing, Quantitative RT-PCR, Over Expression, Transformation Assay, Transfection, Control, Microarray

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: CXCR5 promotes the expression of Schwann cell markers by inhibiting miR-187. ( A ) An RNA-FISH assay was conducted to determine the level of miR-187 in normal salivary gland (NSG), SACC without PNI (No-PNI), far away from nerve of SACC with PNI (Far-nerve), nerve invasion front of SACC with PNI (Nerve-front). ‘N’ represented nerve, (Bar: 50 μm). ( B ) The binding sites on S100A4 3′UTR for miR-187 and the mutant sites. ( C ) Luciferase reporter analysis was carried out to determine the interaction of miR-187 with S100A4. ( D ) qRT-PCR analysis showed that reduced expression of Schwann cell hallmarks mediated by CXCR5 silence could be partially reversed by miR-187 inhibitor. ( E ) Inhibitory migratory, invasive and PNI ability in SACC-LM cells mediated by CXCR5 silence could be reversed by S100A4 overexpression. ( F ) Repressive migratory, invasive and PNI ability in SACC-LM cells induced miR-187 overexpression was alleviated by S100A4 overexpression, ( * p < 0.05, ** p < 0.01).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing, Binding Assay, Mutagenesis, Luciferase, Quantitative RT-PCR, Over Expression

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: Inhibition of CXCR5 suppresses PNI in SACC xenograft model. ( A ) Representative images on hindlimb function of the mouse and HE staining were presented. ( B ) qRT-PCR analysis showed that anti-CXCR5 antibody group mice showed reduced expression of S100A4, p75NTR and GFAP compared with saline group mice. ( C ) Immunohistochemical staining showed that anti-CXCR5 antibody group mice showed reduced expression of S100A4, p75NTR and GFAP compared with saline group mice. The expression of S100A4, p75NTR, GFAP was higher at nerve invasion frontier than that in tumors far away from nerve in PNI groups, ‘N’ represented nerve, (Bar: 50 μm) ( ** p < 0.01, *** p < 0.001).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Inhibition, Staining, Quantitative RT-PCR, Expressing, Saline, Immunohistochemical staining

Journal: Aging (Albany NY)

Article Title: CXCR5 induces perineural invasion of salivary adenoid cystic carcinoma by inhibiting microRNA-187

doi: 10.18632/aging.203097

Figure Lengend Snippet: CXCR5 expression intrinsically connects with the level of Schwann cell markers in SACC specimens. ( A ) Immunohistochemical staining of Schwann cell markers, including S100A4, p75NTR and GFAP in normal salivary gland (NSG), SACC without PNI (No-PNI), far away nerve of SACC with PNI (Far-nerve), nerve invasion front of SACC with PNI (Nerve-front). ‘N’ represented nerve, (Bar: 20 μm). ( B ) Correlation of CXCR5 with Schwann cell markers at nerve invasion frontier of SACC patients. CXCR5 expression was positively correlated with the expression of S100A4, p75NTR and GFAP at nerve invasion frontier of SACC ( ** p < 0.01).

Article Snippet: 1.0 μg/ml of anti-human CXCR5 antibody (R&D Systems) was added to 6-well plates after SACC cells were seeded [ ].

Techniques: Expressing, Immunohistochemical staining, Staining

Journal: International Journal of Molecular Sciences

Article Title: Reduced VDAC1, Maintained Mitochondrial Dynamics and Enhanced Mitochondrial Biogenesis in a Transgenic Tau Mouse Model of Alzheimer’s Disease

doi: 10.3390/ijms23158561

Figure Lengend Snippet: Western Blot, immunofluorescence, and quantification analysis of mitochondrial biogenesis proteins in the hippocampal fields of 6-month-old WT, VDAC1 +/− , TAU, and VDAC1 +/− /TAU mice. ( A ) Representative immunoblots. ( B ) Quantitative densitometry analysis of mitochondrial biogenesis PGC1A (* p < 0.05), NRF1 (**** p < 0.0001), NRF2 (** p < 0.01), and TFAM (**** p < 0.0001) proteins were significantly increased in VDAC1 +/− /TAU mice compared to TAU mice. Forty micrograms (g) of total protein were put into each lane. The loading control was carried out with the help of the housekeeping protein beta-actin. Data are from three independent experiments with similar results (N = 3). ( C ) Representative immunofluorescence images of 10-micron coronal sections (10×). ( D ) fluorescence intensity analysis of mitochondrial biogenesis PGC1A (*** p < 0.001), NRF1 (**** p < 0.0001), NRF2 (**** p < 0.0001), and TFAM (**** p < 0.0001) proteins were significantly increased in VDAC1 +/− /TAU mice compared to TAU mice. The data are from three separate experiments, all of which yielded comparable findings (N = 3), and each mouse was exposed to 10–15 fields. Scale bar: 200 μm. The results were presented as the mean accompanied by the standard error of the mean; ns denotes that the difference did not reach statistical significance; * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001; one-way ANOVA followed by Turkey’s test for multiple comparisons.

Article Snippet: After that, the sections were incubated with the appropriate primary antibodies [DRP1 (NB110-55288, Rabbit Polyclonal 1:100; Novus Biologicals), FIS1 (NB100-56646, Rabbit Polyclonal 1:100; Novus Biologicals), fusion proteins: MFN1: (13798-1-AP, Rabbit Polyclonal 1:100; Protein Tech Group), MFN2 (9482, Rabbit Polyclonal 1:100; Cell Signaling Technology), OPA1 (NBP2-59770, Rabbit Polyclonal 1:100; Novus Biologicals), PGC1A (NBP1-04676, Rabbit Polyclonal 1:100; Novus Biologicals), NRF1 (ab34682, Rabbit Polyclonal 1:100; Abcam), NRF2 (NBP1-32822, Rabbit Polyclonal 1:100; Novus Biologicals), TFAM (NBP2-19437, Rabbit Polyclonal 1:100; Novus Biologicals)] for a whole night at 4 degrees Celsius.

Techniques: Western Blot, Immunofluorescence, Control, Fluorescence