7 ethoxyresorufin er  (Millipore)


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    Structured Review

    Millipore 7 ethoxyresorufin er
    Confirmation of the CYP1A1 inhibitory properties of Ulva fasciata extract by (a) Dixon plot and (b) Y-intercept of the Linewaver-Burk plot versus inhibitor's concentration. Each plot was obtained from independent reactions containing the desired concentration of <t>ethoxyresorufin</t> (0.31–5.00 μ M), 1 pM Supersome protein, 50 mM NADPH, and different concentrations of the extract in a final volume of 200 μ L. Each reaction was followed for 10 min, with the fluorescence signal being recorded every 15 s. Each point in (a) represents the mean ± SD obtained from three independent experiments. Slope of each plot in (a) was obtained and plotted versus the inverse of the concentration of ethoxyresorufin (b).
    7 Ethoxyresorufin Er, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 5775 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 5775 article reviews
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    7 ethoxyresorufin er - by Bioz Stars, 2020-07
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    Images

    1) Product Images from "Gas Chromatography-Mass Spectrometry Analysis of Ulva fasciata (Green Seaweed) Extract and Evaluation of Its Cytoprotective and Antigenotoxic Effects"

    Article Title: Gas Chromatography-Mass Spectrometry Analysis of Ulva fasciata (Green Seaweed) Extract and Evaluation of Its Cytoprotective and Antigenotoxic Effects

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2015/520598

    Confirmation of the CYP1A1 inhibitory properties of Ulva fasciata extract by (a) Dixon plot and (b) Y-intercept of the Linewaver-Burk plot versus inhibitor's concentration. Each plot was obtained from independent reactions containing the desired concentration of ethoxyresorufin (0.31–5.00 μ M), 1 pM Supersome protein, 50 mM NADPH, and different concentrations of the extract in a final volume of 200 μ L. Each reaction was followed for 10 min, with the fluorescence signal being recorded every 15 s. Each point in (a) represents the mean ± SD obtained from three independent experiments. Slope of each plot in (a) was obtained and plotted versus the inverse of the concentration of ethoxyresorufin (b).
    Figure Legend Snippet: Confirmation of the CYP1A1 inhibitory properties of Ulva fasciata extract by (a) Dixon plot and (b) Y-intercept of the Linewaver-Burk plot versus inhibitor's concentration. Each plot was obtained from independent reactions containing the desired concentration of ethoxyresorufin (0.31–5.00 μ M), 1 pM Supersome protein, 50 mM NADPH, and different concentrations of the extract in a final volume of 200 μ L. Each reaction was followed for 10 min, with the fluorescence signal being recorded every 15 s. Each point in (a) represents the mean ± SD obtained from three independent experiments. Slope of each plot in (a) was obtained and plotted versus the inverse of the concentration of ethoxyresorufin (b).

    Techniques Used: Concentration Assay, Fluorescence

    2) Product Images from "Inflammation and Proliferation Act Together to Mediate Intestinal Cell Fusion"

    Article Title: Inflammation and Proliferation Act Together to Mediate Intestinal Cell Fusion

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0006530

    Increased epithelial proliferation correlates with increased cell fusion. (A) Schematic representation of experimental design. AhCre + ;Apc fl/fl mice were transplanted with GFP-expressing whole bone marrow (WBM) on day 0. Two days later, Cre recombinase was induced by β-naphthoflavone (β-NF) administration for 4 consecutive days (days 2–5). Mice were sacrificed on day 7 and the distal small intestine analyzed for fusion (B–E). The intestinal-specific deletion of Apc resulted in an extensive hyperproliferation of crypt cells compared to wild-type (WT) mice, as seen by H E stain (C vs. B) and Ki67 staining (red, indicated by yellow brackets; E vs. D). (F–K) Detection of GFP-expressing cells (green; yellow arrowheads mark examples) denoting cell fusion was increased in the AhCre + ;Apc −/− mice compared to mock-injected WT mice. Three patterns of cell fusion were observed: (G) crypt-only, (H) villus-only, (I) both crypt and villus regions in one crypt/villus unit. Panel (J) is a higher magnification of the red box in panel (I) demonstrating that the Paneth cell region at the base of the crypt remained GFP-negative. Solid white lines denote epithelial/luminal border; dashed white lines indicate epithelial/mesenchymal border. Bars = 25 µm. (K) A significant increase in fusion was observed in villus only ( P = 0.011) and crypt/villus ( P = 0.009) AhCre + ;Apc −/− mice (gray bars) compared to mock-injected WT mice (black bars).
    Figure Legend Snippet: Increased epithelial proliferation correlates with increased cell fusion. (A) Schematic representation of experimental design. AhCre + ;Apc fl/fl mice were transplanted with GFP-expressing whole bone marrow (WBM) on day 0. Two days later, Cre recombinase was induced by β-naphthoflavone (β-NF) administration for 4 consecutive days (days 2–5). Mice were sacrificed on day 7 and the distal small intestine analyzed for fusion (B–E). The intestinal-specific deletion of Apc resulted in an extensive hyperproliferation of crypt cells compared to wild-type (WT) mice, as seen by H E stain (C vs. B) and Ki67 staining (red, indicated by yellow brackets; E vs. D). (F–K) Detection of GFP-expressing cells (green; yellow arrowheads mark examples) denoting cell fusion was increased in the AhCre + ;Apc −/− mice compared to mock-injected WT mice. Three patterns of cell fusion were observed: (G) crypt-only, (H) villus-only, (I) both crypt and villus regions in one crypt/villus unit. Panel (J) is a higher magnification of the red box in panel (I) demonstrating that the Paneth cell region at the base of the crypt remained GFP-negative. Solid white lines denote epithelial/luminal border; dashed white lines indicate epithelial/mesenchymal border. Bars = 25 µm. (K) A significant increase in fusion was observed in villus only ( P = 0.011) and crypt/villus ( P = 0.009) AhCre + ;Apc −/− mice (gray bars) compared to mock-injected WT mice (black bars).

    Techniques Used: Mouse Assay, Expressing, Staining, Injection

    3) Product Images from "Characterization of Maternal and Fetal CYP3A-Mediated Progesterone Metabolism"

    Article Title: Characterization of Maternal and Fetal CYP3A-Mediated Progesterone Metabolism

    Journal: Fetal and pediatric pathology

    doi: 10.1080/15513815.2017.1354411

    Effect of CYP450 Inhibitors on 16α-OHP (A) and 6β-OHP (B) formation following incubation of progesterone (30 μM) with human liver microsomes (0.5 mg/mL) for 30 minutes in the absence (control) and presences of known isoform-selective CYP inhibitors: ketoconazole (CYP3A4), α-naphthoflavone (CYP1A2), letrozole (CYP2A6), omeprazole (CYP2C19), pilocarpine (CYP2A6), quecertin (CYP2C8), quinidine (CYP2D6), or sulfaphenazole (CYP2C9). Data is presented as mean ± SD of duplicate experiments. * indicates p
    Figure Legend Snippet: Effect of CYP450 Inhibitors on 16α-OHP (A) and 6β-OHP (B) formation following incubation of progesterone (30 μM) with human liver microsomes (0.5 mg/mL) for 30 minutes in the absence (control) and presences of known isoform-selective CYP inhibitors: ketoconazole (CYP3A4), α-naphthoflavone (CYP1A2), letrozole (CYP2A6), omeprazole (CYP2C19), pilocarpine (CYP2A6), quecertin (CYP2C8), quinidine (CYP2D6), or sulfaphenazole (CYP2C9). Data is presented as mean ± SD of duplicate experiments. * indicates p

    Techniques Used: Incubation

    4) Product Images from "Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene"

    Article Title: Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene

    Journal: Biochemical Journal

    doi: 10.1042/BJ20051518

    Xenobiotics increased the binding of Nrf2–protein complexes to the ARE - 1 sequence ( A ) EMSA was performed using nuclear extracts (5 μg) obtained from control HepG2 cells or those treated with 25 μM β-NF or 250 μM BHA for 3 h and the radiolabelled probe containing the ARE - 1 or ARE - 2 sequence. For competition experiments, the unlabelled (cold) probe was included at a 50-fold molar excess. ( B ) A supershift assay was performed using nuclear extracts (15 μg) from HepG2 cells (control) or those treated with BHA and the radiolabelled probe containing the ARE - 1 sequence in the presence or absence of anti-Nrf2 antibody (Ab). The shifted bands are denoted by lines, and supershifted bands are denoted by the bracket.
    Figure Legend Snippet: Xenobiotics increased the binding of Nrf2–protein complexes to the ARE - 1 sequence ( A ) EMSA was performed using nuclear extracts (5 μg) obtained from control HepG2 cells or those treated with 25 μM β-NF or 250 μM BHA for 3 h and the radiolabelled probe containing the ARE - 1 or ARE - 2 sequence. For competition experiments, the unlabelled (cold) probe was included at a 50-fold molar excess. ( B ) A supershift assay was performed using nuclear extracts (15 μg) from HepG2 cells (control) or those treated with BHA and the radiolabelled probe containing the ARE - 1 sequence in the presence or absence of anti-Nrf2 antibody (Ab). The shifted bands are denoted by lines, and supershifted bands are denoted by the bracket.

    Techniques Used: Binding Assay, Sequencing

    Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.
    Figure Legend Snippet: Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.

    Techniques Used: Northern Blot, Incubation

    Activity of the Mrp2 reporter gene constructs induced by xenobiotics ( A ) Hepa 1-6 cells were transfected with constructs containing either both ARE sequences (p−1895/+99-CAT) or only the ARE - 1 -like sequence (p−185/+99-CAT). CAT activity was measured after treatment with 250 μM BHA, 500 μM 2,4,5-T or 25 μM β-NF for 24 h. ( B ) Results expressed as the induction relative to the activity of the construct treated with vehicle (0.1% DMSO). Results are means±S.D. for three independent experiments.
    Figure Legend Snippet: Activity of the Mrp2 reporter gene constructs induced by xenobiotics ( A ) Hepa 1-6 cells were transfected with constructs containing either both ARE sequences (p−1895/+99-CAT) or only the ARE - 1 -like sequence (p−185/+99-CAT). CAT activity was measured after treatment with 250 μM BHA, 500 μM 2,4,5-T or 25 μM β-NF for 24 h. ( B ) Results expressed as the induction relative to the activity of the construct treated with vehicle (0.1% DMSO). Results are means±S.D. for three independent experiments.

    Techniques Used: Activity Assay, Construct, Transfection, Sequencing

    5) Product Images from "Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene"

    Article Title: Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene

    Journal: Biochemical Journal

    doi: 10.1042/BJ20051518

    Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.
    Figure Legend Snippet: Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.

    Techniques Used: Northern Blot, Incubation

    6) Product Images from "Telmisartan directly ameliorates the neuronal inflammatory response to IL-1? partly through the JNK/c-Jun and NADPH oxidase pathways"

    Article Title: Telmisartan directly ameliorates the neuronal inflammatory response to IL-1? partly through the JNK/c-Jun and NADPH oxidase pathways

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-9-102

    The nuclear factor-kappa B (NF-κB) pathway is not involved in the neuroprotective effect of telmisartan in SK-N-SH neuroblasts. (A) Telmisartan does not prevent time-dependent IκB-α protein degradation in cells in response to interleukin-1 beta (IL-1β). Cells were pretreated for 2 hours with 10 μmol/l telmisartan (Telm) before exposure to 10 ng/ml IL-1β for the indicated time intervals. IκB-α protein levels were determined in whole-cell extracts, and normalized to β-actin. (B) Neither telmisartan nor diphenyleneiodonium (DPI) modified IL-1β-induced expression of IκB-α mRNA. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 3 hours to 10 ng/ml IL-1β to determine IκB-α mRNA expression. (C) Neither telmisartan nor DPI affected IL-1β-induced nuclear translocation of the NF-κB p65 subunit. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 30 minutes to 10 ng/ml IL-1β. The NF-κB p65 subunit protein was determined in nuclear extracts and normalized to the level of the nuclear protein histone H4. Representative western blots are shown below the corresponding bar graphs. Results are presented as means ± SEM from three independent experiments. # P
    Figure Legend Snippet: The nuclear factor-kappa B (NF-κB) pathway is not involved in the neuroprotective effect of telmisartan in SK-N-SH neuroblasts. (A) Telmisartan does not prevent time-dependent IκB-α protein degradation in cells in response to interleukin-1 beta (IL-1β). Cells were pretreated for 2 hours with 10 μmol/l telmisartan (Telm) before exposure to 10 ng/ml IL-1β for the indicated time intervals. IκB-α protein levels were determined in whole-cell extracts, and normalized to β-actin. (B) Neither telmisartan nor diphenyleneiodonium (DPI) modified IL-1β-induced expression of IκB-α mRNA. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 3 hours to 10 ng/ml IL-1β to determine IκB-α mRNA expression. (C) Neither telmisartan nor DPI affected IL-1β-induced nuclear translocation of the NF-κB p65 subunit. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 30 minutes to 10 ng/ml IL-1β. The NF-κB p65 subunit protein was determined in nuclear extracts and normalized to the level of the nuclear protein histone H4. Representative western blots are shown below the corresponding bar graphs. Results are presented as means ± SEM from three independent experiments. # P

    Techniques Used: Modification, Expressing, Translocation Assay, Western Blot

    7) Product Images from "ZINC NUTRITIONAL STATUS MODULATES EXPRESSION OF AHR-RESPONSIVE P450 ENZYMES IN VASCULAR ENDOTHELIAL CELLS"

    Article Title: ZINC NUTRITIONAL STATUS MODULATES EXPRESSION OF AHR-RESPONSIVE P450 ENZYMES IN VASCULAR ENDOTHELIAL CELLS

    Journal: Environmental toxicology and pharmacology

    doi: 10.1016/j.etap.2007.10.016

    Zinc deficiency compromises β-naphthoflavone-induced CYP1A1 protein expression in vascular endothelial cells Cells were exposed to vehicle control, TPEN, β- NF (1.0 µM), TPEN plus β- NF, or TPEN with zinc supplementation plus β- NF for 24 hours. The values are ratios of the densitometric units of CYP1A1 over those of β-Actin. Bars with different letters (a, b, c) are statistically different from each other (p
    Figure Legend Snippet: Zinc deficiency compromises β-naphthoflavone-induced CYP1A1 protein expression in vascular endothelial cells Cells were exposed to vehicle control, TPEN, β- NF (1.0 µM), TPEN plus β- NF, or TPEN with zinc supplementation plus β- NF for 24 hours. The values are ratios of the densitometric units of CYP1A1 over those of β-Actin. Bars with different letters (a, b, c) are statistically different from each other (p

    Techniques Used: Expressing

    8) Product Images from "Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells"

    Article Title: Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells

    Journal: Particle and Fibre Toxicology

    doi: 10.1186/1743-8977-7-41

    Effects of siRNA against NF-κB (p65) on DEP-induced mRNA expression of genes . Effects of siRNA against NF-κB (p65) on DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA. Successful transfection was verified by Western analysis of p65-levels (E). Human bronchial epithelial BEAS-2B cells were exposed to DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells detected in separate experiments (n = 4). * p
    Figure Legend Snippet: Effects of siRNA against NF-κB (p65) on DEP-induced mRNA expression of genes . Effects of siRNA against NF-κB (p65) on DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA. Successful transfection was verified by Western analysis of p65-levels (E). Human bronchial epithelial BEAS-2B cells were exposed to DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells detected in separate experiments (n = 4). * p

    Techniques Used: Expressing, Transfection, Western Blot, Quantitative RT-PCR

    Effect of inhibitors of p38 and CYP1A1 on DEP-induced mRNA expression of genes . Effect of inhibitors of p38 (A-D) and CYP1A1 (E-H) on DEP-induced expression of IL-6 (A, E), IL-8 (B, F), COX-2 (C, G) and CYP1A1 (D, H) mRNA in cultures of human bronchial epithelial BEAS-2B cells. Cells were incubated with the p38 inhibitor (SB202190, 5 μM) or the CYP1A1 inhibitor (α-naphthoflavone, 25 μM) for 1 h, prior to addition of DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of mRNA levels performed by QRT-PCR. Bars represent fold increase in mRNA relative to unexposed cells not treated with inhibitor detected in separate replicate experiments (means ± SEM, n = 4). * p
    Figure Legend Snippet: Effect of inhibitors of p38 and CYP1A1 on DEP-induced mRNA expression of genes . Effect of inhibitors of p38 (A-D) and CYP1A1 (E-H) on DEP-induced expression of IL-6 (A, E), IL-8 (B, F), COX-2 (C, G) and CYP1A1 (D, H) mRNA in cultures of human bronchial epithelial BEAS-2B cells. Cells were incubated with the p38 inhibitor (SB202190, 5 μM) or the CYP1A1 inhibitor (α-naphthoflavone, 25 μM) for 1 h, prior to addition of DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of mRNA levels performed by QRT-PCR. Bars represent fold increase in mRNA relative to unexposed cells not treated with inhibitor detected in separate replicate experiments (means ± SEM, n = 4). * p

    Techniques Used: Expressing, Incubation, Quantitative RT-PCR

    Proposed model for DEP-induced expression of IL-8, COX-2 and CYP1A1, based on the presented findings . DEP-induced mRNA expression of CYP1A1 in BEAS-2B cells occurs at much lower DEP-concentrations than the concentrations necessary to induce mRNA expression of IL-8 and COX-2. Activation of AhR and expression of CYP1A1 mRNA seem essential in facilitating the DEP-induced expression of IL-8 and COX-2 mRNA via a permissive pathway (required, but not decisive for the strength of the response), not involving p38 and NF-κB/p-65. However, the p38 and p65 pathways seem crucial in DEP-induced expression of COX-2 and IL-8 mRNA, via a major pathway.
    Figure Legend Snippet: Proposed model for DEP-induced expression of IL-8, COX-2 and CYP1A1, based on the presented findings . DEP-induced mRNA expression of CYP1A1 in BEAS-2B cells occurs at much lower DEP-concentrations than the concentrations necessary to induce mRNA expression of IL-8 and COX-2. Activation of AhR and expression of CYP1A1 mRNA seem essential in facilitating the DEP-induced expression of IL-8 and COX-2 mRNA via a permissive pathway (required, but not decisive for the strength of the response), not involving p38 and NF-κB/p-65. However, the p38 and p65 pathways seem crucial in DEP-induced expression of COX-2 and IL-8 mRNA, via a major pathway.

    Techniques Used: Expressing, Activation Assay

    Time-dependent DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA . Human bronchial epithelial BEAS-2B cells were exposed to 0 or 100 μg/ml DEPs for 0, 2, 4 or 8 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells at 0 h, detected in separate experiments (n≥3). * p
    Figure Legend Snippet: Time-dependent DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA . Human bronchial epithelial BEAS-2B cells were exposed to 0 or 100 μg/ml DEPs for 0, 2, 4 or 8 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells at 0 h, detected in separate experiments (n≥3). * p

    Techniques Used: Expressing, Quantitative RT-PCR

    Concentration-dependent DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA . Human bronchial epithelial BEAS-2B cells were exposed to increasing concentrations of DEPs (0-200 μg/ml) for 4 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells detected in separate experiments (n = 3). Experiments with very low concentrations (0.025, 0.05 and 0.1 μg/ml) were only repeated twice. * p
    Figure Legend Snippet: Concentration-dependent DEP-induced expression of IL-6 (A), IL-8 (B), COX-2 (C) and CYP1A1 (D) mRNA . Human bronchial epithelial BEAS-2B cells were exposed to increasing concentrations of DEPs (0-200 μg/ml) for 4 h. Relative quantification of cytokine mRNA levels was performed by QRT-PCR. Bars represent means ± SEM of fold increase relative to unexposed cells detected in separate experiments (n = 3). Experiments with very low concentrations (0.025, 0.05 and 0.1 μg/ml) were only repeated twice. * p

    Techniques Used: Concentration Assay, Expressing, Quantitative RT-PCR

    9) Product Images from "Detection of Cytochrome P450 mRNA in Tissue Sections and Cell Lines Using Enzyme-Labeled Fluorescence In Situ Hybridization"

    Article Title: Detection of Cytochrome P450 mRNA in Tissue Sections and Cell Lines Using Enzyme-Labeled Fluorescence In Situ Hybridization

    Journal: In vitro toxicology

    doi:

    Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM beta-napthoflavone (β-NF)-induced H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.
    Figure Legend Snippet: Enzyme-labeled fluorescence (ELF) in situ hybridization control experiments utilizing cultured rat hepatoma cells and formalin-fixed, paraffin-embedded human tissue sections. (A) 22-μM beta-napthoflavone (β-NF)-induced H4IIE rat cells hybridized with rat biotin-conjugated CYP1A1 oligomer. (B) 22-μM β-NF-treated H4IIe rat cells probed with the rat biotin-labeled CYP1A1 20-mer and pretreated with 150 μ/ml of RNase A. (C) 22-μM β-NF-exposed H4IIE rat cells hybridized with rat biotinylated CYP1A1 2Gmer plus 60-fold excess nonbiotinylated rat CYP1A1 probe. (D) Poorly differentiated squamous cell carcinoma of human oral epithelium probed with human CYP1A1 biotin-labeled 20-mer. (E) Poorly differentiated squamous cell carcinoma of human oral epithelium hybridized with the partially homologous rat CYP1A1 biotin-conjugated oligomer probe. (F) Poorly differentiated squamous cell carcinoma of human oral epithelium without the addition of a biotinylated oligomer to the hybridization buffer. Magnification 400×.

    Techniques Used: Labeling, Fluorescence, In Situ Hybridization, Cell Culture, Formalin-fixed Paraffin-Embedded, Hybridization

    Enzyme-labeled fluorescence (ELF) in situ hybridization using a rat biotin-conjugated CYP1A1 oligomer probe with cultured rat hepatoma cells. (A9 untreated H4IIE cells probed with biotinylated CYP1A1 oligomer. (B) 22-μM beta-naphoflavone (β-NF)-treated H4IIE cells hybridized with biotin-labeled CYP1A1 oligomer (C) 22-μM β-NF exposed H4IIE cells lacking the biotinylated CYP1A1 probe from the hybridization solution. (D) Unexposed Fao cells probed with biotinylated CYP1A1 oligomer. (E) 22-μM β-NF-treated Fao cells hybridized with biotin-labeled CYP1A1 oligomer (F) 22-μM β-NF-exposed Fao cells without the biotinylated CYP1A1 probe. Magnification 400×.
    Figure Legend Snippet: Enzyme-labeled fluorescence (ELF) in situ hybridization using a rat biotin-conjugated CYP1A1 oligomer probe with cultured rat hepatoma cells. (A9 untreated H4IIE cells probed with biotinylated CYP1A1 oligomer. (B) 22-μM beta-naphoflavone (β-NF)-treated H4IIE cells hybridized with biotin-labeled CYP1A1 oligomer (C) 22-μM β-NF exposed H4IIE cells lacking the biotinylated CYP1A1 probe from the hybridization solution. (D) Unexposed Fao cells probed with biotinylated CYP1A1 oligomer. (E) 22-μM β-NF-treated Fao cells hybridized with biotin-labeled CYP1A1 oligomer (F) 22-μM β-NF-exposed Fao cells without the biotinylated CYP1A1 probe. Magnification 400×.

    Techniques Used: Labeling, Fluorescence, In Situ Hybridization, Cell Culture, Hybridization

    10) Product Images from ""

    Article Title:

    Journal: Molecular Pharmacology

    doi: 10.1124/mol.114.093369

    Hit compound characterization led to selection of lead compound, CB7993113. H1G1.1c3 cells were treated with vehicle (0.1% DMSO) or 10 −9 to 10 −5 M AHR antagonists immediately prior to stimulation with 10 −7 M β -NF. Fluorescence
    Figure Legend Snippet: Hit compound characterization led to selection of lead compound, CB7993113. H1G1.1c3 cells were treated with vehicle (0.1% DMSO) or 10 −9 to 10 −5 M AHR antagonists immediately prior to stimulation with 10 −7 M β -NF. Fluorescence

    Techniques Used: Selection, Fluorescence

    11) Product Images from "Comparative gene responses to collected ambient particles in vitro: endothelial responses"

    Article Title: Comparative gene responses to collected ambient particles in vitro: endothelial responses

    Journal: Physiological Genomics

    doi: 10.1152/physiolgenomics.00051.2011

    α-Napthoflavone (α-NF) and resveratrol suppressed sum06 APM-induced gene expression. RT-PCR analysis demonstrates α-NF significantly suppressed sum06 APM-induced CYP1A1 gene expression compared with control DMSO (35%). Resveratrol suppressed Sum06 APM-induced CYP1A1, TIPARP, PTGS2, and CCL-2 gene expression compared with control (87, 17, 33, 38%). n = 3; * P ≤ 0.05, Sum06 APM compared with control; # P ≤ 0.05, Sum06 APM with α-NF or resveratrol compared with Sum06 APM.
    Figure Legend Snippet: α-Napthoflavone (α-NF) and resveratrol suppressed sum06 APM-induced gene expression. RT-PCR analysis demonstrates α-NF significantly suppressed sum06 APM-induced CYP1A1 gene expression compared with control DMSO (35%). Resveratrol suppressed Sum06 APM-induced CYP1A1, TIPARP, PTGS2, and CCL-2 gene expression compared with control (87, 17, 33, 38%). n = 3; * P ≤ 0.05, Sum06 APM compared with control; # P ≤ 0.05, Sum06 APM with α-NF or resveratrol compared with Sum06 APM.

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    12) Product Images from "Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells"

    Article Title: Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells

    Journal: Particle and Fibre Toxicology

    doi: 10.1186/1743-8977-7-41

    Effect of inhibitors of p38 and CYP1A1 on DEP-induced mRNA expression of genes . Effect of inhibitors of p38 (A-D) and CYP1A1 (E-H) on DEP-induced expression of IL-6 (A, E), IL-8 (B, F), COX-2 (C, G) and CYP1A1 (D, H) mRNA in cultures of human bronchial epithelial BEAS-2B cells. Cells were incubated with the p38 inhibitor (SB202190, 5 μM) or the CYP1A1 inhibitor (α-naphthoflavone, 25 μM) for 1 h, prior to addition of DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of mRNA levels performed by QRT-PCR. Bars represent fold increase in mRNA relative to unexposed cells not treated with inhibitor detected in separate replicate experiments (means ± SEM, n = 4). * p
    Figure Legend Snippet: Effect of inhibitors of p38 and CYP1A1 on DEP-induced mRNA expression of genes . Effect of inhibitors of p38 (A-D) and CYP1A1 (E-H) on DEP-induced expression of IL-6 (A, E), IL-8 (B, F), COX-2 (C, G) and CYP1A1 (D, H) mRNA in cultures of human bronchial epithelial BEAS-2B cells. Cells were incubated with the p38 inhibitor (SB202190, 5 μM) or the CYP1A1 inhibitor (α-naphthoflavone, 25 μM) for 1 h, prior to addition of DEPs (0 and 100 μg/ml) for 4 h. Relative quantification of mRNA levels performed by QRT-PCR. Bars represent fold increase in mRNA relative to unexposed cells not treated with inhibitor detected in separate replicate experiments (means ± SEM, n = 4). * p

    Techniques Used: Expressing, Incubation, Quantitative RT-PCR

    13) Product Images from "Receptor Heterodimerization and Co-Receptor Engagement in TLR2 Activation Induced by MIC1 and MIC4 from Toxoplasma gondii"

    Article Title: Receptor Heterodimerization and Co-Receptor Engagement in TLR2 Activation Induced by MIC1 and MIC4 from Toxoplasma gondii

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms20205001

    rMIC1 and rMIC4 induce IL-12 production by macrophages through activation of TGF-β activated kinase 1 (TAK1), p38, and nuclear factor-kappa B (NF-κB). ( A ) RAW264.7- luc  murine macrophages were stimulated with the following preparations of  Toxoplasma gondii  microneme proteins: rMIC1 (5 µg/mL), rMIC4 (5 µg/mL), and the native Lac+ fraction (5 µg/mL), which contains MIC1 and MIC4. LPS (500 ng/mL) and medium were used as the positive and negative controls, respectively. Cells were lysed 4 h post-stimulation, and NF-κB activation was inferred from the luminescence measurements. Data are expressed as the mean ± SD of triplicate wells, and data from three independent experiments yielding similar results. ( B ) Total lysates of bone marrow-derived macrophages (BMDMs) was were 30 min after stimulation with rMIC1 (5 µg/mL), rMIC4 (5 µg/mL), or LPS (1 µg/mL). As controls, cells were also incubated with medium (i.e., unstimulated cells [US]) or sampled at time zero (i.e., T0), as indicated at the top of the panels. Immunoblotting was performed to assess total p38 and the p65 subunit of NF-κB, as well as their phosphorylated forms (p-p38 and p-NF-κB). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used as a loading control. ( C , D ) Densitometric analysis to quantify the p38 and NF-κB bands in the Western blot (panel B). ( E , F ) IL-12 concentrations in the supernatant of BMDM cultures that were pretreated with vehicle (-) or pharmacological inhibitors of AKT (Wortmannin, 100 nM), TAK1 (5Z-7-oxozeaenol, 100 nM), ERK (PD9805, 20 μM), JNK (SP600125, 20 μM), p38 (SB202190, 20 μM), or NF-κB (Caffeic acid, 15 µg/mL) for 3 h, and subsequently stimulated with ( E ) rMIC1 (5 µg/mL) or ( F ) rMIC4 (5 µg/mL) for 24 h as assessed by ELISA. LPS (1 µg/mL) and medium were used as the positive and negative controls, respectively. ( G ) Viability of BMDMs pretreated with pharmacological inhibitors of signaling molecules. Statistical analysis comparing the viability of cells (%) that were pretreated with each inhibitor and stimulated with rMIC1 or rMIC4 to that of cells stimulated with rMICs but not pretreated with pharmacological inhibitors (vehicle). Staurosporine (2 µM) and Triton X-100 (1%  v / v ) were used to induce in vitro apoptosis. The data are from two independent experiments yielding similar results. (*)  p
    Figure Legend Snippet: rMIC1 and rMIC4 induce IL-12 production by macrophages through activation of TGF-β activated kinase 1 (TAK1), p38, and nuclear factor-kappa B (NF-κB). ( A ) RAW264.7- luc murine macrophages were stimulated with the following preparations of Toxoplasma gondii microneme proteins: rMIC1 (5 µg/mL), rMIC4 (5 µg/mL), and the native Lac+ fraction (5 µg/mL), which contains MIC1 and MIC4. LPS (500 ng/mL) and medium were used as the positive and negative controls, respectively. Cells were lysed 4 h post-stimulation, and NF-κB activation was inferred from the luminescence measurements. Data are expressed as the mean ± SD of triplicate wells, and data from three independent experiments yielding similar results. ( B ) Total lysates of bone marrow-derived macrophages (BMDMs) was were 30 min after stimulation with rMIC1 (5 µg/mL), rMIC4 (5 µg/mL), or LPS (1 µg/mL). As controls, cells were also incubated with medium (i.e., unstimulated cells [US]) or sampled at time zero (i.e., T0), as indicated at the top of the panels. Immunoblotting was performed to assess total p38 and the p65 subunit of NF-κB, as well as their phosphorylated forms (p-p38 and p-NF-κB). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used as a loading control. ( C , D ) Densitometric analysis to quantify the p38 and NF-κB bands in the Western blot (panel B). ( E , F ) IL-12 concentrations in the supernatant of BMDM cultures that were pretreated with vehicle (-) or pharmacological inhibitors of AKT (Wortmannin, 100 nM), TAK1 (5Z-7-oxozeaenol, 100 nM), ERK (PD9805, 20 μM), JNK (SP600125, 20 μM), p38 (SB202190, 20 μM), or NF-κB (Caffeic acid, 15 µg/mL) for 3 h, and subsequently stimulated with ( E ) rMIC1 (5 µg/mL) or ( F ) rMIC4 (5 µg/mL) for 24 h as assessed by ELISA. LPS (1 µg/mL) and medium were used as the positive and negative controls, respectively. ( G ) Viability of BMDMs pretreated with pharmacological inhibitors of signaling molecules. Statistical analysis comparing the viability of cells (%) that were pretreated with each inhibitor and stimulated with rMIC1 or rMIC4 to that of cells stimulated with rMICs but not pretreated with pharmacological inhibitors (vehicle). Staurosporine (2 µM) and Triton X-100 (1% v / v ) were used to induce in vitro apoptosis. The data are from two independent experiments yielding similar results. (*) p

    Techniques Used: Activation Assay, Derivative Assay, Incubation, Western Blot, Enzyme-linked Immunosorbent Assay, In Vitro

    14) Product Images from "Real-time Monitoring of Non-specific Toxicity Using a Saccharomyces cerevisiae Reporter System"

    Article Title: Real-time Monitoring of Non-specific Toxicity Using a Saccharomyces cerevisiae Reporter System

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s8106433

    a. Bioluminescence response to 5,6-benzoflavone in real-time monitoring during exposure of 4 h. Squares (0.75 nM), diamonds (7.5 nM), circles (75 nM) and triangles (750 nM) denote for concentration of 5,6-benzoflavone used, respectively. The error bars are shown for triplicate parallel measurements. b. Bioluminescence response to rapamycin in real-time monitoring during an exposure of 4h. Rapamycin reveals totally different bioluminescence response. The error bars are shown for triplicate parallel measurements and the symbols are diamonds (0.05 μM), Squares (0.5 μM), and circles (5 μM) denote for concentration of rapamycin used, respectively.
    Figure Legend Snippet: a. Bioluminescence response to 5,6-benzoflavone in real-time monitoring during exposure of 4 h. Squares (0.75 nM), diamonds (7.5 nM), circles (75 nM) and triangles (750 nM) denote for concentration of 5,6-benzoflavone used, respectively. The error bars are shown for triplicate parallel measurements. b. Bioluminescence response to rapamycin in real-time monitoring during an exposure of 4h. Rapamycin reveals totally different bioluminescence response. The error bars are shown for triplicate parallel measurements and the symbols are diamonds (0.05 μM), Squares (0.5 μM), and circles (5 μM) denote for concentration of rapamycin used, respectively.

    Techniques Used: Concentration Assay

    15) Product Images from "Ganoderic Acid A Metabolites and Their Metabolic Kinetics"

    Article Title: Ganoderic Acid A Metabolites and Their Metabolic Kinetics

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2017.00101

    Effect of CYP inhibitors on the formation of GAA metabolites M2 and M4 in pooled RLMs (A) or HLMs (B) . GAA was incubated with pooled RLMs or HLMs with and without α-naphthoflavone (NAP), ticlopidine (TIC), quinidine (QND), ketoconazole (KET), fluconazole (FLU) and diethyldithiocarbamate (DIE). * p
    Figure Legend Snippet: Effect of CYP inhibitors on the formation of GAA metabolites M2 and M4 in pooled RLMs (A) or HLMs (B) . GAA was incubated with pooled RLMs or HLMs with and without α-naphthoflavone (NAP), ticlopidine (TIC), quinidine (QND), ketoconazole (KET), fluconazole (FLU) and diethyldithiocarbamate (DIE). * p

    Techniques Used: Incubation

    16) Product Images from "Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene"

    Article Title: Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene

    Journal: Biochemical Journal

    doi: 10.1042/BJ20051518

    Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.
    Figure Legend Snippet: Dose-dependence and time course of the induction of Mrp2 and GCLC mRNAs by xenobiotics in hepatoma cell lines Mouse Hepa 1-6 cells ( A ) and human HepG2 cells ( B ) were exposed to different concentrations of xenobiotics (BHA, 2,4,5-T, 2AAF or β-NF) for 24 h. Total RNA (10 μg) from control (DMSO) and treated cells was subjected to Northern blot analysis using specific probes for mouse or human genes. In order to determinate the time course of the induction of Mrp2 ( C ) and GCLC ( D ) mRNAs, Hepa 1-6 cells were incubated in medium containing 0.1% DMSO (control), 25 μM β-NF, 250 μM BHA, 500 μM 2,4,5-T or 200 μM 2AAF. At various intervals up to 24 h, RNA was harvested, and the specific mRNA levels were determined by Northern blotting. The relative contents of Mrp2 and GCLC were determined using the PhosphorImager system. The mRNA levels were normalized to values observed in control cells, and are plotted as the relative amounts of mRNA. Results are means±S.D. for four independent experiments.

    Techniques Used: Northern Blot, Incubation

    Activity of the Mrp2 reporter gene constructs induced by xenobiotics ( A ) Hepa 1-6 cells were transfected with constructs containing either both ARE sequences (p−1895/+99-CAT) or only the ARE - 1 -like sequence (p−185/+99-CAT). CAT activity was measured after treatment with 250 μM BHA, 500 μM 2,4,5-T or 25 μM β-NF for 24 h. ( B ) Results expressed as the induction relative to the activity of the construct treated with vehicle (0.1% DMSO). Results are means±S.D. for three independent experiments.
    Figure Legend Snippet: Activity of the Mrp2 reporter gene constructs induced by xenobiotics ( A ) Hepa 1-6 cells were transfected with constructs containing either both ARE sequences (p−1895/+99-CAT) or only the ARE - 1 -like sequence (p−185/+99-CAT). CAT activity was measured after treatment with 250 μM BHA, 500 μM 2,4,5-T or 25 μM β-NF for 24 h. ( B ) Results expressed as the induction relative to the activity of the construct treated with vehicle (0.1% DMSO). Results are means±S.D. for three independent experiments.

    Techniques Used: Activity Assay, Construct, Transfection, Sequencing

    17) Product Images from "Cytochrome P450-mediated metabolism of N-(2-methoxyphenyl)-hydroxylamine, a human metabolite of the environmental pollutants and carcinogens o-anisidine and o-nitroanisole"

    Article Title: Cytochrome P450-mediated metabolism of N-(2-methoxyphenyl)-hydroxylamine, a human metabolite of the environmental pollutants and carcinogens o-anisidine and o-nitroanisole

    Journal: Interdisciplinary Toxicology

    doi: 10.2478/v10102-010-0045-8

    HPLC elution profiles of metabolites of 1 mM o -anisidine incubated with rabbit microsomes ( A ), of 1.0 mM N -(2-methoxyphenyl)hydroxylamine incubated with rabbit ( B ) and rat ( C ) hepatic microsomes. ( D ) synthetic N -(2-methoxyphenyl)hydroxylamine and o -anisidine. ( E ) o -aminophenol. ( F ) o -nitrosoanisole. For incubation conditions see Materials and methods . Peaks eluting between 2.0 and 5.5 min, solvent front, NADPH and protein components of microsomes and NADPH-generation system.
    Figure Legend Snippet: HPLC elution profiles of metabolites of 1 mM o -anisidine incubated with rabbit microsomes ( A ), of 1.0 mM N -(2-methoxyphenyl)hydroxylamine incubated with rabbit ( B ) and rat ( C ) hepatic microsomes. ( D ) synthetic N -(2-methoxyphenyl)hydroxylamine and o -anisidine. ( E ) o -aminophenol. ( F ) o -nitrosoanisole. For incubation conditions see Materials and methods . Peaks eluting between 2.0 and 5.5 min, solvent front, NADPH and protein components of microsomes and NADPH-generation system.

    Techniques Used: High Performance Liquid Chromatography, Incubation

    18) Product Images from "Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells"

    Article Title: Diesel exhaust particles induce CYP1A1 and pro-inflammatory responses via differential pathways in human bronchial epithelial cells

    Journal: Particle and Fibre Toxicology

    doi: 10.1186/1743-8977-7-41

    DEP-induced phosphorylation of p38 (A), phosphorylation of p65 (B) and degradation of IκBα (C) . Human bronchial epithelial BEAS-2B cells were exposed to increasing concentrations of DEPs (0, 100, 200 μg/ml) for 2 or 4 h before Western analysis. Each figure displays a representative blot and optical quantification of the protein bands from separate replicate experiments. Detected levels of phosphorylated p38 and p65 and the levels of IκBα are respectively normalised against total p38, p65, or β-actin, and are presented as fold increase (mean ± SEM, n≥3) compared to unexposed cells.
    Figure Legend Snippet: DEP-induced phosphorylation of p38 (A), phosphorylation of p65 (B) and degradation of IκBα (C) . Human bronchial epithelial BEAS-2B cells were exposed to increasing concentrations of DEPs (0, 100, 200 μg/ml) for 2 or 4 h before Western analysis. Each figure displays a representative blot and optical quantification of the protein bands from separate replicate experiments. Detected levels of phosphorylated p38 and p65 and the levels of IκBα are respectively normalised against total p38, p65, or β-actin, and are presented as fold increase (mean ± SEM, n≥3) compared to unexposed cells.

    Techniques Used: Western Blot

    19) Product Images from "Aryl hydrocarbon receptor activity modulates prolactin expression in the pituitary"

    Article Title: Aryl hydrocarbon receptor activity modulates prolactin expression in the pituitary

    Journal: Toxicology and applied pharmacology

    doi: 10.1016/j.taap.2012.08.026

    β-naphthoflavone alone and with α-naphthoflavone activated Cyp1a1 and suppressed AhR expression
    Figure Legend Snippet: β-naphthoflavone alone and with α-naphthoflavone activated Cyp1a1 and suppressed AhR expression

    Techniques Used: Expressing

    20) Product Images from ""

    Article Title:

    Journal: Molecular Pharmacology

    doi: 10.1124/mol.114.093369

    CB7993113 directly binds murine AHR protein and blocks AHR nuclear translocation. In vitro-expressed murine AHR (mAHR) (A) or human AHR (hAHR) (B) protein was incubated with 2 nM [ 3 H]TCDD in the presence of vehicle (DMSO), 10 μ M CH223191, or 10
    Figure Legend Snippet: CB7993113 directly binds murine AHR protein and blocks AHR nuclear translocation. In vitro-expressed murine AHR (mAHR) (A) or human AHR (hAHR) (B) protein was incubated with 2 nM [ 3 H]TCDD in the presence of vehicle (DMSO), 10 μ M CH223191, or 10

    Techniques Used: Translocation Assay, In Vitro, Incubation

    21) Product Images from "Asian Dust Particles Induce Macrophage Inflammatory Responses via Mitogen-Activated Protein Kinase Activation and Reactive Oxygen Species Production"

    Article Title: Asian Dust Particles Induce Macrophage Inflammatory Responses via Mitogen-Activated Protein Kinase Activation and Reactive Oxygen Species Production

    Journal: Journal of Immunology Research

    doi: 10.1155/2014/856154

    Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- κ B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of SN50, a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P
    Figure Legend Snippet: Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- κ B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of SN50, a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P

    Techniques Used: Enzyme-linked Immunosorbent Assay

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    Millipore rabbit polyclonal anti nuclear factor kappa b nf κb p65 antibody
    The nuclear factor-kappa B (NF-κB) pathway is not involved in the neuroprotective effect of telmisartan in SK-N-SH neuroblasts. (A) Telmisartan does not prevent time-dependent IκB-α protein degradation in cells in response to interleukin-1 beta (IL-1β). Cells were pretreated for 2 hours with 10 μmol/l telmisartan (Telm) before exposure to 10 ng/ml IL-1β for the indicated time intervals. IκB-α protein levels were determined in whole-cell extracts, and normalized to β-actin. (B) Neither telmisartan nor diphenyleneiodonium (DPI) modified IL-1β-induced expression of IκB-α mRNA. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 3 hours to 10 ng/ml IL-1β to determine IκB-α mRNA expression. (C) Neither telmisartan nor DPI affected IL-1β-induced nuclear translocation of the NF-κB <t>p65</t> subunit. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 30 minutes to 10 ng/ml IL-1β. The NF-κB p65 subunit protein was determined in nuclear extracts and normalized to the level of the nuclear protein histone H4. Representative western blots are shown below the corresponding bar graphs. Results are presented as means ± SEM from three independent experiments. # P
    Rabbit Polyclonal Anti Nuclear Factor Kappa B Nf κb P65 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore nuclear factor κ b
    Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- <t>κ</t> B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of <t>SN50,</t> a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P
    Nuclear Factor κ B, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore nf κ b
    Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- <t>κ</t> B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of <t>SN50,</t> a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P
    Nf κ B, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The nuclear factor-kappa B (NF-κB) pathway is not involved in the neuroprotective effect of telmisartan in SK-N-SH neuroblasts. (A) Telmisartan does not prevent time-dependent IκB-α protein degradation in cells in response to interleukin-1 beta (IL-1β). Cells were pretreated for 2 hours with 10 μmol/l telmisartan (Telm) before exposure to 10 ng/ml IL-1β for the indicated time intervals. IκB-α protein levels were determined in whole-cell extracts, and normalized to β-actin. (B) Neither telmisartan nor diphenyleneiodonium (DPI) modified IL-1β-induced expression of IκB-α mRNA. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 3 hours to 10 ng/ml IL-1β to determine IκB-α mRNA expression. (C) Neither telmisartan nor DPI affected IL-1β-induced nuclear translocation of the NF-κB p65 subunit. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 30 minutes to 10 ng/ml IL-1β. The NF-κB p65 subunit protein was determined in nuclear extracts and normalized to the level of the nuclear protein histone H4. Representative western blots are shown below the corresponding bar graphs. Results are presented as means ± SEM from three independent experiments. # P

    Journal: Journal of Neuroinflammation

    Article Title: Telmisartan directly ameliorates the neuronal inflammatory response to IL-1? partly through the JNK/c-Jun and NADPH oxidase pathways

    doi: 10.1186/1742-2094-9-102

    Figure Lengend Snippet: The nuclear factor-kappa B (NF-κB) pathway is not involved in the neuroprotective effect of telmisartan in SK-N-SH neuroblasts. (A) Telmisartan does not prevent time-dependent IκB-α protein degradation in cells in response to interleukin-1 beta (IL-1β). Cells were pretreated for 2 hours with 10 μmol/l telmisartan (Telm) before exposure to 10 ng/ml IL-1β for the indicated time intervals. IκB-α protein levels were determined in whole-cell extracts, and normalized to β-actin. (B) Neither telmisartan nor diphenyleneiodonium (DPI) modified IL-1β-induced expression of IκB-α mRNA. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 3 hours to 10 ng/ml IL-1β to determine IκB-α mRNA expression. (C) Neither telmisartan nor DPI affected IL-1β-induced nuclear translocation of the NF-κB p65 subunit. The cells were pretreated for 2 hours with 10 μmol/l Telm or 5 μmol/l DPI before exposure for 30 minutes to 10 ng/ml IL-1β. The NF-κB p65 subunit protein was determined in nuclear extracts and normalized to the level of the nuclear protein histone H4. Representative western blots are shown below the corresponding bar graphs. Results are presented as means ± SEM from three independent experiments. # P

    Article Snippet: Primary antibodies used for western blot analysis were: rabbit polyclonal anti-nuclear factor-kappa B (NF-κB)-p65 antibody (1:2000, Millipore, Billerica, MA, USA); mouse polyclonal anti-cyclooxygenase-2 (COX-2) (1:1000, Cayman Chemical, Ann Arbor, MI, USA); rabbit anti-phospho-p38 mitogen-activated protein kinase (MAPK) (1:1000), rabbit anti-phospho-extracellular signal-regulated kinases (ERK)1/2 (1:1000), rabbit anti-phospho-JNK (1:1000), rabbit anti-phospho-c-Jun (1:1000), rabbit anti-IκB-α (1:1000), rabbit anti-β-actin (1:1000), and rabbit anti-histone H4 (1:1000), all from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Modification, Expressing, Translocation Assay, Western Blot

    Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- κ B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of SN50, a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P

    Journal: Journal of Immunology Research

    Article Title: Asian Dust Particles Induce Macrophage Inflammatory Responses via Mitogen-Activated Protein Kinase Activation and Reactive Oxygen Species Production

    doi: 10.1155/2014/856154

    Figure Lengend Snippet: Asian dust particles-induced tumor necrosis factor- α (TNF- α ) production is dependent on mitogen-activated protein kinase and nuclear factor- κ B signaling pathways. RAW264.7 cells were pretreated for 30 min with (a) 50 μ M of SP600125, an inhibitor of c-Jun N-terminal kinase; (b) 30 μ M of U0126, an extracellular signal-regulated kinase (ERK) inhibitor; or (c) 50 μ M of SN50, a nuclear factor- κ B (NF- κ B) inhibitor and then treated for 6 h with 100 μ g/mL of ADP1 or ADP2 or 1.5 μ g/mL of LPS. Dimethyl sulfoxide (0.1%) vehicle was used as control (Cont.). The level of TNF- α in the culture supernatants was assessed by means of an enzyme-linked immunosorbent assay. Results are expressed as mean ± SD; n = 6; * P

    Article Snippet: SN50, a nuclear factor-κ B (NF-κ B) inhibitor, was purchased from Calbiochem (La Jolla, CA).

    Techniques: Enzyme-linked Immunosorbent Assay