fatty acid free bovine serum albumin bsa  (Millipore)


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    Bovine Serum Albumin
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    a9306
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    Structured Review

    Millipore fatty acid free bovine serum albumin bsa
    Bovine Serum Albumin

    https://www.bioz.com/result/fatty acid free bovine serum albumin bsa/product/Millipore
    Average 99 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    fatty acid free bovine serum albumin bsa - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Intrarenal renin-angiotensin system mediates fatty acid-induced ER stress in the kidney"

    Article Title: Intrarenal renin-angiotensin system mediates fatty acid-induced ER stress in the kidney

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00223.2015

    Valsartan or aliskiren prevented palmitic acid (PA; 0.8 mM)-induced endoplasmic reticulum (ER) stress in cultured human proximal tubule epithelial cells (HK2) cells after a 24-h treatment. A and B : protein abundance of binding immunoglobulin protein (BiP) and C/EBP homologous protein (CHOP) was unchanged in HK2 cells treated with BSA (2 and 10 mg/ml) and with or without valsartan (10 −6 M) or aliskiren (10 −7 M). C : MTT assays of HK2 cells. HK2 cells were incubated with PA at different concentrations for 24 h. After the cells were incubated with tetrazolium salt solution for 2 h, the quantity of formazan product was determined from the absorbance at 560 nm. * P
    Figure Legend Snippet: Valsartan or aliskiren prevented palmitic acid (PA; 0.8 mM)-induced endoplasmic reticulum (ER) stress in cultured human proximal tubule epithelial cells (HK2) cells after a 24-h treatment. A and B : protein abundance of binding immunoglobulin protein (BiP) and C/EBP homologous protein (CHOP) was unchanged in HK2 cells treated with BSA (2 and 10 mg/ml) and with or without valsartan (10 −6 M) or aliskiren (10 −7 M). C : MTT assays of HK2 cells. HK2 cells were incubated with PA at different concentrations for 24 h. After the cells were incubated with tetrazolium salt solution for 2 h, the quantity of formazan product was determined from the absorbance at 560 nm. * P

    Techniques Used: Cell Culture, Binding Assay, MTT Assay, Incubation

    2) Product Images from "Effects of Fatty Acids on Benzo[a]pyrene Uptake and Metabolism in Human Lung Adenocarcinoma A549 Cells"

    Article Title: Effects of Fatty Acids on Benzo[a]pyrene Uptake and Metabolism in Human Lung Adenocarcinoma A549 Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0090908

    Glutathionation in A549 cells supplemented with BSA-conjugated fatty acids (LA, DHA, BSA carrier control). Cells were treated with BSO or GSH in combination with each of the fatty acids for 48 µM BaP for 24 h. Data represents mean normalized intensity ± SEM of at least 30 images per treatment and 30 cells per image. * indicates significant difference from the corresponding control using Tukey test at p
    Figure Legend Snippet: Glutathionation in A549 cells supplemented with BSA-conjugated fatty acids (LA, DHA, BSA carrier control). Cells were treated with BSO or GSH in combination with each of the fatty acids for 48 µM BaP for 24 h. Data represents mean normalized intensity ± SEM of at least 30 images per treatment and 30 cells per image. * indicates significant difference from the corresponding control using Tukey test at p

    Techniques Used:

    3) Product Images from "The “long tail” of the protein tumbling correlation function: observation by 1H NMR relaxometry in a wide frequency and concentration range"

    Article Title: The “long tail” of the protein tumbling correlation function: observation by 1H NMR relaxometry in a wide frequency and concentration range

    Journal: Journal of Biomolecular Nmr

    doi: 10.1007/s10858-015-0001-1

    Dispersion profiles of ( a ) LYZ and ( b ) BSA at different concentrations. For direct visual comparison of R 1ρ ( triangles ) and R 1 ( circles ), R 1ρ data were multiplied by 10/3 (see ESM, Eqs. S1–S5). R 2 ’s ( squares ) were measured at 20 MHz and are shown in a separate column of each plot. Solid lines provide the best fit result. Uncertain data points (BSA at ω 0 /2π
    Figure Legend Snippet: Dispersion profiles of ( a ) LYZ and ( b ) BSA at different concentrations. For direct visual comparison of R 1ρ ( triangles ) and R 1 ( circles ), R 1ρ data were multiplied by 10/3 (see ESM, Eqs. S1–S5). R 2 ’s ( squares ) were measured at 20 MHz and are shown in a separate column of each plot. Solid lines provide the best fit result. Uncertain data points (BSA at ω 0 /2π

    Techniques Used:

    Order parameter \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ S_{\text{rot}}^{2} $$\end{document} S rot 2 and correlation time of the slow component \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ \tau_{\text{S}} $$\end{document} τ S (T = 20 °C) of rotational diffusion as a function of protein concentration of LYZ ( circles ) and BSA ( squares and diamonds ). For BSA, two sets of data are shown corresponding to the analyses using the simple and the more complicated form of the correlation function that includes oligomers (see ESM, Table S2). At the lowest concentration (65 g/L), the upper and lower boundaries of \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ S_{\text{rot}}^{2} $$\end{document} S rot 2 and \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ \tau_{\text{S}} , $$\end{document} τ S , respectively, are shown (indicated by arrows ). The minimum (65 g/L) and maximum (260 g/L) concentrations correspond to 4.5 and 18.2 mM for LYZ and 1 and 3.9 mM for BSA, respectively
    Figure Legend Snippet: Order parameter \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ S_{\text{rot}}^{2} $$\end{document} S rot 2 and correlation time of the slow component \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ \tau_{\text{S}} $$\end{document} τ S (T = 20 °C) of rotational diffusion as a function of protein concentration of LYZ ( circles ) and BSA ( squares and diamonds ). For BSA, two sets of data are shown corresponding to the analyses using the simple and the more complicated form of the correlation function that includes oligomers (see ESM, Table S2). At the lowest concentration (65 g/L), the upper and lower boundaries of \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ S_{\text{rot}}^{2} $$\end{document} S rot 2 and \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ \tau_{\text{S}} , $$\end{document} τ S , respectively, are shown (indicated by arrows ). The minimum (65 g/L) and maximum (260 g/L) concentrations correspond to 4.5 and 18.2 mM for LYZ and 1 and 3.9 mM for BSA, respectively

    Techniques Used: Diffusion-based Assay, Protein Concentration, Concentration Assay

    Size-exclusion chromatogram of LYZ and BSA ( top ) and blue native (BN) PAGE of BSA performed on the elution volume of different peaks of the size-exclusion chromatography ( bottom )
    Figure Legend Snippet: Size-exclusion chromatogram of LYZ and BSA ( top ) and blue native (BN) PAGE of BSA performed on the elution volume of different peaks of the size-exclusion chromatography ( bottom )

    Techniques Used: Polyacrylamide Gel Electrophoresis, Size-exclusion Chromatography

    4) Product Images from "Proteomic Identification of Betaig-h3 as a Lysophosphatidic Acid-Induced Secreted Protein of Human Mesenchymal Stem Cells: Paracrine Activation of A549 Lung Adenocarcinoma Cells by Betaig-h3 *"

    Article Title: Proteomic Identification of Betaig-h3 as a Lysophosphatidic Acid-Induced Secreted Protein of Human Mesenchymal Stem Cells: Paracrine Activation of A549 Lung Adenocarcinoma Cells by Betaig-h3 *

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M111.012385

    Role of LPA 1 in the LPA-induced expression of βig-h3. A , hASCs were treated with indicated concentrations of LPA for 4 days. B , hASCs were treated with serum-free medium containing 10 μ m LPA or vehicles (0.1% BSA) for the indicated time.
    Figure Legend Snippet: Role of LPA 1 in the LPA-induced expression of βig-h3. A , hASCs were treated with indicated concentrations of LPA for 4 days. B , hASCs were treated with serum-free medium containing 10 μ m LPA or vehicles (0.1% BSA) for the indicated time.

    Techniques Used: Expressing

    5) Product Images from "Sphingosine-1-Phosphate Induces Dose-Dependent Chemotaxis or Fugetaxis of T-ALL Blasts through S1P1 Activation"

    Article Title: Sphingosine-1-Phosphate Induces Dose-Dependent Chemotaxis or Fugetaxis of T-ALL Blasts through S1P1 Activation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0148137

    S1P3 is not involved in S1P-driven chemotactic responses of CEM cells. (A) CEM cells were serum-starved for 2 h and pre-treated or not with W146 (100 μM) and/or BM-241 (100 μM). Cells were applied in Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Black bars correspond to pre-treatment with RPMI-BSA 0.1%; white bars correspond to pre-treatment with W146; grid bars correspond to pre-treatment with BML-241; and chess bars correspond to pre-treatment with W146 plus BML-241. Results were analyzed by Two-way ANOVA, followed by Bonferroni post-test (n = 3). (B) S1P receptors mRNA expression were analyzed by real time quantitative PCR, compared with the control Abelson (Abl) gene (2 -ΔCt ) in SU-DHL-1 cells (n = 4). (C) S1P1 and S1P3 mRNA expression was analyzed by real time quantitative PCR, compared with the control Abelson (Abl). Fold change analysis were done using HPB-ALL as calibrator to normalize the expression of S1P1 and S1P3 on SU-DHL-1 cells. Statistical analysis was made with ΔCt values and significant differences are related to HPB-ALL cells. Results were analyzed by Student’s t test (n = 4). (D) SU-DHL-1 cells were serum-starved for 2 h, applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Results were analyzed by One-way ANOVA, followed by Tukey post-test (n = 3). (E) SU-DHL-1 cells were serum-starved for 2 h and treated or not with W146 (100 μM). Cells were applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Values correspond to specific migration after subtracting the numbers of migrating cells in culture medium only. Black bars correspond to pre-treatment with RPMI-BSA 0.1% alone and white bars correspond to pre-treatment with W146. Results were analyzed by unpaired Student’s t test (n = 3). Results are expressed as mean ± SEM and differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.
    Figure Legend Snippet: S1P3 is not involved in S1P-driven chemotactic responses of CEM cells. (A) CEM cells were serum-starved for 2 h and pre-treated or not with W146 (100 μM) and/or BM-241 (100 μM). Cells were applied in Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Black bars correspond to pre-treatment with RPMI-BSA 0.1%; white bars correspond to pre-treatment with W146; grid bars correspond to pre-treatment with BML-241; and chess bars correspond to pre-treatment with W146 plus BML-241. Results were analyzed by Two-way ANOVA, followed by Bonferroni post-test (n = 3). (B) S1P receptors mRNA expression were analyzed by real time quantitative PCR, compared with the control Abelson (Abl) gene (2 -ΔCt ) in SU-DHL-1 cells (n = 4). (C) S1P1 and S1P3 mRNA expression was analyzed by real time quantitative PCR, compared with the control Abelson (Abl). Fold change analysis were done using HPB-ALL as calibrator to normalize the expression of S1P1 and S1P3 on SU-DHL-1 cells. Statistical analysis was made with ΔCt values and significant differences are related to HPB-ALL cells. Results were analyzed by Student’s t test (n = 4). (D) SU-DHL-1 cells were serum-starved for 2 h, applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Results were analyzed by One-way ANOVA, followed by Tukey post-test (n = 3). (E) SU-DHL-1 cells were serum-starved for 2 h and treated or not with W146 (100 μM). Cells were applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. Values correspond to specific migration after subtracting the numbers of migrating cells in culture medium only. Black bars correspond to pre-treatment with RPMI-BSA 0.1% alone and white bars correspond to pre-treatment with W146. Results were analyzed by unpaired Student’s t test (n = 3). Results are expressed as mean ± SEM and differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.

    Techniques Used: Incubation, Expressing, Real-time Polymerase Chain Reaction, Migration

    High S1P concentrations induce S1P1-dependent fugetaxis of CEM cells. (A) CEM cells were serum-starved for 2 h, applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. S1P was added to the upper chamber to evaluate fugetaxis; only RPMI-BSA 0.1% was added to the bottom chambers. Results were analyzed by One-way ANOVA, followed by Tukey post-test (n = 3). (B) CEM cells were serum-starved for 2 h and pre-treated or not with W146 (100 μM). Cells were then applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. S1P was added to the upper chamber to evaluate repulsive responses. Black bars correspond to T-ALL blasts pre-treated with RPMI-BSA 0.1% alone and white bars correspond to T-ALL blasts pre-treated with W146. Results were analyzed by unpaired Student’s t test. Results are expressed as mean ± SEM and differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001 (n = 3).
    Figure Legend Snippet: High S1P concentrations induce S1P1-dependent fugetaxis of CEM cells. (A) CEM cells were serum-starved for 2 h, applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. S1P was added to the upper chamber to evaluate fugetaxis; only RPMI-BSA 0.1% was added to the bottom chambers. Results were analyzed by One-way ANOVA, followed by Tukey post-test (n = 3). (B) CEM cells were serum-starved for 2 h and pre-treated or not with W146 (100 μM). Cells were then applied to Transwell™ chambers containing different S1P concentrations and incubated for 4 hours. S1P was added to the upper chamber to evaluate repulsive responses. Black bars correspond to T-ALL blasts pre-treated with RPMI-BSA 0.1% alone and white bars correspond to T-ALL blasts pre-treated with W146. Results were analyzed by unpaired Student’s t test. Results are expressed as mean ± SEM and differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001 (n = 3).

    Techniques Used: Incubation

    S1P1 is involved in S1P-driven chemotactic responses of T-ALL blasts. T-ALL blasts were serum-starved for 2 h and pre-treated or not with W146 (100 μM). (A) Cells were applied to Transwell™ chambers with S1P 1, 10, 100, 500 or 1000 nM and incubated for 4 hours (n = 3). (B) Migratory response of CEM cells toward S1P 100, 2500, 5000 and 10000 nM (n = 3). Values correspond to a specific migration after subtracting the numbers of migrating cells obtained in wells with culture medium only. Black bars correspond to T-ALL blasts pre-treated with RPMI-BSA 0.1% and white bars correspond to T-ALL blasts pre-treated with W146. Results are expressed as mean ± SEM and were analyzed by unpaired Student’s t test. Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.
    Figure Legend Snippet: S1P1 is involved in S1P-driven chemotactic responses of T-ALL blasts. T-ALL blasts were serum-starved for 2 h and pre-treated or not with W146 (100 μM). (A) Cells were applied to Transwell™ chambers with S1P 1, 10, 100, 500 or 1000 nM and incubated for 4 hours (n = 3). (B) Migratory response of CEM cells toward S1P 100, 2500, 5000 and 10000 nM (n = 3). Values correspond to a specific migration after subtracting the numbers of migrating cells obtained in wells with culture medium only. Black bars correspond to T-ALL blasts pre-treated with RPMI-BSA 0.1% and white bars correspond to T-ALL blasts pre-treated with W146. Results are expressed as mean ± SEM and were analyzed by unpaired Student’s t test. Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.

    Techniques Used: Incubation, Migration

    S1P modulates F-actin polymerization, AKT, ERK and Rac1 activity. (A) Modulation of the actin cytoskeleton after stimulation by different S1P concentrations in CEM cells pre-treated or not with W146 (100 μM). Results are represented as [(MFI after addition of the ligand) / (MFI before addition of the ligand)] x 100. The MFI values obtained before the addition of S1P were arbitrarily set as 100% and correspond to the time zero. White circles correspond to cells previously treated with W146 (100 μM) and the black circles correspond to cells treated with RPMI-BSA 0.1%. Results are expressed by mean ± SEM and were analyzed by unpaired Student’s t test (n = 3). Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001 (B) AKT and (C) ERK1/2 activation after stimulation of CEM cells, with different S1P concentrations, being pre-treated or not with W146 (100 μM). Protein extracts were analyzed by Western-blot with AKT, phosphorylated-AKT, ERK1/2 and phosphorylated-ERK-1/2 specific antibodies. Representative western-blots images are shown (n = 3). (D) Rac1 activity after stimulation of CEM cells, pre-treated or not with W146 (100 μM), with different S1P concentrations was accessed by G-LISA. Optical density (OD) was detected in 490 nm. Results are represented as [(OD after addition of the ligand) / (OD before addition of the ligand)] x 100. OD values obtained before the addition of S1P were arbitrarily set as 100% and correspond to the time zero. Black circles correspond pre-treatment with RPMI-BSA 0.1% and white circles correspond to pre-treatment with W146 (100 μM). Results and are expressed as mean ± SEM. Differences between distinct time points and control (time zero) were analyzed by One-way ANOVA, followed by Dunnett post-test and were considered statistically significant when # p˂0.05, ## p ˂0.01 or ### p ˂0.001. Differences between pre-treatment with RPMI-BSA 0.1% and pre-treatment with W146 (100 μM) were analyzed by unpaired Student T test (n = 1, with 2 biological replicates in duplicate). Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.
    Figure Legend Snippet: S1P modulates F-actin polymerization, AKT, ERK and Rac1 activity. (A) Modulation of the actin cytoskeleton after stimulation by different S1P concentrations in CEM cells pre-treated or not with W146 (100 μM). Results are represented as [(MFI after addition of the ligand) / (MFI before addition of the ligand)] x 100. The MFI values obtained before the addition of S1P were arbitrarily set as 100% and correspond to the time zero. White circles correspond to cells previously treated with W146 (100 μM) and the black circles correspond to cells treated with RPMI-BSA 0.1%. Results are expressed by mean ± SEM and were analyzed by unpaired Student’s t test (n = 3). Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001 (B) AKT and (C) ERK1/2 activation after stimulation of CEM cells, with different S1P concentrations, being pre-treated or not with W146 (100 μM). Protein extracts were analyzed by Western-blot with AKT, phosphorylated-AKT, ERK1/2 and phosphorylated-ERK-1/2 specific antibodies. Representative western-blots images are shown (n = 3). (D) Rac1 activity after stimulation of CEM cells, pre-treated or not with W146 (100 μM), with different S1P concentrations was accessed by G-LISA. Optical density (OD) was detected in 490 nm. Results are represented as [(OD after addition of the ligand) / (OD before addition of the ligand)] x 100. OD values obtained before the addition of S1P were arbitrarily set as 100% and correspond to the time zero. Black circles correspond pre-treatment with RPMI-BSA 0.1% and white circles correspond to pre-treatment with W146 (100 μM). Results and are expressed as mean ± SEM. Differences between distinct time points and control (time zero) were analyzed by One-way ANOVA, followed by Dunnett post-test and were considered statistically significant when # p˂0.05, ## p ˂0.01 or ### p ˂0.001. Differences between pre-treatment with RPMI-BSA 0.1% and pre-treatment with W146 (100 μM) were analyzed by unpaired Student T test (n = 1, with 2 biological replicates in duplicate). Differences were considered statistically significant when * p˂0.05, ** p ˂0.01 or *** p ˂0.001.

    Techniques Used: Activity Assay, Activation Assay, Western Blot

    6) Product Images from "Astragalus Polysaccharide Suppresses Skeletal Muscle Myostatin Expression in Diabetes: Involvement of ROS-ERK and NF-κB Pathways"

    Article Title: Astragalus Polysaccharide Suppresses Skeletal Muscle Myostatin Expression in Diabetes: Involvement of ROS-ERK and NF-κB Pathways

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2013/782497

    Effect of APS on glucose uptake and myostatin expression in C2C12 cells exposure to palmitate. C2C12 cells were incubated for 24 h in DMEM containing 5% BSA in either the presence (FFA-treated cells) or absence (control cells) of 0.5 mmol/L FFAs. Cells treated with APS were incubated with additional APS at the final concentration of 200 μ g/mL. (a) Glucose uptake was assayed using [3H]2-deoxyglucose in the presence or in the absence of 100 nM insulin. # P
    Figure Legend Snippet: Effect of APS on glucose uptake and myostatin expression in C2C12 cells exposure to palmitate. C2C12 cells were incubated for 24 h in DMEM containing 5% BSA in either the presence (FFA-treated cells) or absence (control cells) of 0.5 mmol/L FFAs. Cells treated with APS were incubated with additional APS at the final concentration of 200 μ g/mL. (a) Glucose uptake was assayed using [3H]2-deoxyglucose in the presence or in the absence of 100 nM insulin. # P

    Techniques Used: Expressing, Incubation, Concentration Assay

    7) Product Images from "Fetuin‐A aggravates lipotoxicity in podocytes via interleukin‐1 signaling. Fetuin‐A aggravates lipotoxicity in podocytes via interleukin‐1 signaling"

    Article Title: Fetuin‐A aggravates lipotoxicity in podocytes via interleukin‐1 signaling. Fetuin‐A aggravates lipotoxicity in podocytes via interleukin‐1 signaling

    Journal: Physiological Reports

    doi: 10.14814/phy2.13287

    Antagonization of IL ‐1 attenuates FetA or LPS exacerbated palmitic acid‐induced podocyte death. (A) Graph shows podocytes treated with 200 μ mol/L palmitic acid (palm) or bovine serum albumin ( BSA ) (control) alone or in combination with 200 μ g/mL bovine FetA for 48 h, and preincubated for 1 h with 1 ng/mL TAK ‐242, or 3.3 μ g/ mL anti‐ IL ‐1 β antibody, or 1 μ g/ mL IL ‐1Ra (Anakinra). Bar graph represents the mean percentages ± SD of Annexin V‐positive/ PI ‐negative (early apoptotic) and Annexin V‐positive/ PI ‐positive (late apoptotic/necrotic) podocytes ( n = 3, ** P
    Figure Legend Snippet: Antagonization of IL ‐1 attenuates FetA or LPS exacerbated palmitic acid‐induced podocyte death. (A) Graph shows podocytes treated with 200 μ mol/L palmitic acid (palm) or bovine serum albumin ( BSA ) (control) alone or in combination with 200 μ g/mL bovine FetA for 48 h, and preincubated for 1 h with 1 ng/mL TAK ‐242, or 3.3 μ g/ mL anti‐ IL ‐1 β antibody, or 1 μ g/ mL IL ‐1Ra (Anakinra). Bar graph represents the mean percentages ± SD of Annexin V‐positive/ PI ‐negative (early apoptotic) and Annexin V‐positive/ PI ‐positive (late apoptotic/necrotic) podocytes ( n = 3, ** P

    Techniques Used:

    TLR 4 blockage attenuates bovine FetA or LPS exacerbated palmitic acid‐induced podocyte death. (A) Graph shows podocytes treated with 200 μ mol/L palmitic acid (palm) or bovine serum albumin ( BSA ) (control) alone or in combination with 200 μ g/mL bovine FetA for 48 h and preincubated with 1 ng/mL TAK ‐242 for 1 h. Bar graph represents the mean percentages ± SD of Annexin V‐positive/ PI ‐negative (early apoptotic) and Annexin V‐positive/ PI ‐positive (late apoptotic/necrotic) podocytes ( n = 3, ** P
    Figure Legend Snippet: TLR 4 blockage attenuates bovine FetA or LPS exacerbated palmitic acid‐induced podocyte death. (A) Graph shows podocytes treated with 200 μ mol/L palmitic acid (palm) or bovine serum albumin ( BSA ) (control) alone or in combination with 200 μ g/mL bovine FetA for 48 h and preincubated with 1 ng/mL TAK ‐242 for 1 h. Bar graph represents the mean percentages ± SD of Annexin V‐positive/ PI ‐negative (early apoptotic) and Annexin V‐positive/ PI ‐positive (late apoptotic/necrotic) podocytes ( n = 3, ** P

    Techniques Used:

    8) Product Images from "Distinct regulation of stearoyl-CoA desaturase 1 gene expression by cis and trans C18:1 fatty acids in human aortic smooth muscle cells"

    Article Title: Distinct regulation of stearoyl-CoA desaturase 1 gene expression by cis and trans C18:1 fatty acids in human aortic smooth muscle cells

    Journal: Genes & Nutrition

    doi: 10.1007/s12263-011-0258-2

    HASMC growth in the presence of C18:1 fatty acid isomers. a HASMC were pre-treated for 24 h in DMEM with 0.5% BSA and then exposed to control medium (ctr), 50 and 100 μM of oleic acid (OA) for 48 h. Protein lysates were prepared for the analysis of scd1 protein expression by Western blotting. b HASMC were pre-treated for 24 h in DMEM with 0.5% BSA and then treated with 100 μM of oleic acid. Cells were collected at various time points for analysis of scd1 protein expression by Western blotting. c HASMC were pre-treated for 24 h in DMEM with 0.5% BSA. At day 0, cells were treated with oleic acid (OA), trans vaccenic acid (VA) and elaidic acid (ELA) at 100 μM. Proliferation control cells were maintained in DMEM with 10% FBS. Cell number was determined by Cyquant ® kit. Values represent the mean ± SEM ( n = 3)
    Figure Legend Snippet: HASMC growth in the presence of C18:1 fatty acid isomers. a HASMC were pre-treated for 24 h in DMEM with 0.5% BSA and then exposed to control medium (ctr), 50 and 100 μM of oleic acid (OA) for 48 h. Protein lysates were prepared for the analysis of scd1 protein expression by Western blotting. b HASMC were pre-treated for 24 h in DMEM with 0.5% BSA and then treated with 100 μM of oleic acid. Cells were collected at various time points for analysis of scd1 protein expression by Western blotting. c HASMC were pre-treated for 24 h in DMEM with 0.5% BSA. At day 0, cells were treated with oleic acid (OA), trans vaccenic acid (VA) and elaidic acid (ELA) at 100 μM. Proliferation control cells were maintained in DMEM with 10% FBS. Cell number was determined by Cyquant ® kit. Values represent the mean ± SEM ( n = 3)

    Techniques Used: Expressing, Western Blot, CyQUANT Assay

    9) Product Images from "Reversible Nuclear-Lipid-Droplet Morphology Induced by Oleic Acid: A Link to Cellular-Lipid Metabolism"

    Article Title: Reversible Nuclear-Lipid-Droplet Morphology Induced by Oleic Acid: A Link to Cellular-Lipid Metabolism

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0170608

    Experimental protocol for the different treatments used with rat primary hepatocytes and HepG2 cells. Cells treated with the respective vehicle of OA or Triacsin C, ethanol+BSA or methanol, constituted the controls for the different experimental groups.
    Figure Legend Snippet: Experimental protocol for the different treatments used with rat primary hepatocytes and HepG2 cells. Cells treated with the respective vehicle of OA or Triacsin C, ethanol+BSA or methanol, constituted the controls for the different experimental groups.

    Techniques Used:

    10) Product Images from "Lipid-bound apolipoproteins in tyrosyl radical-oxidized HDL stabilize ABCA1 like lipid-free apolipoprotein A-I"

    Article Title: Lipid-bound apolipoproteins in tyrosyl radical-oxidized HDL stabilize ABCA1 like lipid-free apolipoprotein A-I

    Journal: BMC Biochemistry

    doi: 10.1186/1471-2091-13-1

    tyrHDL increases cellular ABCA1 in the presence of ALLN . Cholesterol-loaded fibroblasts were incubated with BSA and 10 μg/ml apoA-I, HDL, or tyrHDL with or without protease inhibitor ALLN (50 μM) to inhibit endogenous calpain for 16 h. ABCA1 was determined by immunoblotting as in Figure 3. The data are representative of three experiments with similar results.
    Figure Legend Snippet: tyrHDL increases cellular ABCA1 in the presence of ALLN . Cholesterol-loaded fibroblasts were incubated with BSA and 10 μg/ml apoA-I, HDL, or tyrHDL with or without protease inhibitor ALLN (50 μM) to inhibit endogenous calpain for 16 h. ABCA1 was determined by immunoblotting as in Figure 3. The data are representative of three experiments with similar results.

    Techniques Used: Incubation, Protease Inhibitor

    Crosslinking of tyrHDL to ABCA1 . Cholesterol-loaded fibroblasts were equilibrated in the presence of 5 μM T0901317 for 24 h to upregulate ABCA1 expression. The cells were then treated with BSA alone or plus 10 μg/ml apoA-I, HDL and tyrHDL for 2 h, washed, and then incubated with 250 mM of DSP for 1 h. Whole cell lysates were isolated, run on a 5-15% SDS-PAGE gradient gel and probed for the presence of ABCA1 and apoA-I by immunoblot. 5% beta mercaptoethanol (β-ME) was used as a reducing agent to cleave crosslinks formed by DSP. Results are representative of three separate experiments with similar results.
    Figure Legend Snippet: Crosslinking of tyrHDL to ABCA1 . Cholesterol-loaded fibroblasts were equilibrated in the presence of 5 μM T0901317 for 24 h to upregulate ABCA1 expression. The cells were then treated with BSA alone or plus 10 μg/ml apoA-I, HDL and tyrHDL for 2 h, washed, and then incubated with 250 mM of DSP for 1 h. Whole cell lysates were isolated, run on a 5-15% SDS-PAGE gradient gel and probed for the presence of ABCA1 and apoA-I by immunoblot. 5% beta mercaptoethanol (β-ME) was used as a reducing agent to cleave crosslinks formed by DSP. Results are representative of three separate experiments with similar results.

    Techniques Used: Expressing, Incubation, Isolation, SDS Page

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  • 99
    Millipore fatty acid free bsa
    Analysis of de novo sphingolipid biosynthesis in RAW264.7 cells by [ 13 C]palmitate labeling. RAW264.7 cells were incubated with 0.1 m m [U- 13 C]palmitic acid (as the <t>BSA</t> complex) with vehicle control (PBS), KLA (100 ng/ml), <t>ISP1</t> (1 μ m ), or KLA+ ISP1. For cells treated with KLA + ISP1, ISP1 was added 1 h prior to the addition of KLA for the times shown. The appearance of 13 C in newly synthesized sphingolipids was quantified by mass spectrometry as described under supplemental “Materials and Methods” . A , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer subspecies. Data represent the means ± S.E. ( n = 3). B , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species in cells treated with control ( left ) or KLA ( right ), Data represent the means ( n = 3). Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (7.6 pmol/μg DNA); C18 (0.7 pmol/μg DNA); C20 (0.3 pmol/μg DNA); C22 (3.2 pmol/μg DNA); C24:1 (6 pmol/μg DNA); C24 (6.4 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); C26 (0.1 pmol/μg DNA). C , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species ( left ) and 12 C (unlabeled) Cer species ( right ) in cells treated with KLA + ISP1. Data represent the means ( n = 3).
    Fatty Acid Free Bsa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 509 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ffa bsa
    Effects of OF and CM on the mRNA expressions of lipogenesis-related genes. Real-time RT-PCR analysis of sterol regulatory element-binding protein-1 ( SREBP-1c ) (a) and glycerol-3-phosphate acyltransferase ( GPAT ) (b) mRNA levels in 1 mM <t>FFA/BSA-treated</t> HepG2 cells. All data were normalized to GAPDH mRNA, and the fold changes in expression were calculated relative to control cells (treated with 1% BSA). Each experiment was independently performed three times. Data were presented as the mean ± SD. Values not sharing common superscripts are significantly different ( p
    Ffa Bsa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Analysis of de novo sphingolipid biosynthesis in RAW264.7 cells by [ 13 C]palmitate labeling. RAW264.7 cells were incubated with 0.1 m m [U- 13 C]palmitic acid (as the BSA complex) with vehicle control (PBS), KLA (100 ng/ml), ISP1 (1 μ m ), or KLA+ ISP1. For cells treated with KLA + ISP1, ISP1 was added 1 h prior to the addition of KLA for the times shown. The appearance of 13 C in newly synthesized sphingolipids was quantified by mass spectrometry as described under supplemental “Materials and Methods” . A , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer subspecies. Data represent the means ± S.E. ( n = 3). B , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species in cells treated with control ( left ) or KLA ( right ), Data represent the means ( n = 3). Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (7.6 pmol/μg DNA); C18 (0.7 pmol/μg DNA); C20 (0.3 pmol/μg DNA); C22 (3.2 pmol/μg DNA); C24:1 (6 pmol/μg DNA); C24 (6.4 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); C26 (0.1 pmol/μg DNA). C , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species ( left ) and 12 C (unlabeled) Cer species ( right ) in cells treated with KLA + ISP1. Data represent the means ( n = 3).

    Journal: The Journal of Biological Chemistry

    Article Title: Kdo2-Lipid A, a TLR4-specific Agonist, Induces de Novo Sphingolipid Biosynthesis in RAW264.7 Macrophages, Which Is Essential for Induction of Autophagy *

    doi: 10.1074/jbc.M110.170621

    Figure Lengend Snippet: Analysis of de novo sphingolipid biosynthesis in RAW264.7 cells by [ 13 C]palmitate labeling. RAW264.7 cells were incubated with 0.1 m m [U- 13 C]palmitic acid (as the BSA complex) with vehicle control (PBS), KLA (100 ng/ml), ISP1 (1 μ m ), or KLA+ ISP1. For cells treated with KLA + ISP1, ISP1 was added 1 h prior to the addition of KLA for the times shown. The appearance of 13 C in newly synthesized sphingolipids was quantified by mass spectrometry as described under supplemental “Materials and Methods” . A , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer subspecies. Data represent the means ± S.E. ( n = 3). B , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species in cells treated with control ( left ) or KLA ( right ), Data represent the means ( n = 3). Because of the difficulties in visualization, the quantities of ceramide subspecies in control treated cells at the 24-h time point are as follows: C16 (7.6 pmol/μg DNA); C18 (0.7 pmol/μg DNA); C20 (0.3 pmol/μg DNA); C22 (3.2 pmol/μg DNA); C24:1 (6 pmol/μg DNA); C24 (6.4 pmol/μg DNA); C26:1 (0.2 pmol/μg DNA); C26 (0.1 pmol/μg DNA). C , summation of base (backbone)-labeled and dual (backbone and fatty acid)-labeled Cer species ( left ) and 12 C (unlabeled) Cer species ( right ) in cells treated with KLA + ISP1. Data represent the means ( n = 3).

    Article Snippet: Materials The suppliers for the reagents were as follows: Kdo2 -lipid A and the internal standard mixture for SL analysis by LC ESI-MS/MS (ceramide/sphingoid internal standard mixture II, LM-6005) (Avanti Polar Lipids, Alabaster, AL); [U-13 C]palmitic acid (98%) (Cambridge Isotopes, Andover, MA); fatty acid-free BSA (Calbiochem) ; Hoechst 33342 (Invitrogen); ISP1 (Biomol, Plymouth Meeting, PA); mouse monoclonal antibody to SPT1 (anti-LCB1), anti-BiP/GRP78, and anti-GM130 (BD Biosciences); rabbit monoclonal anti-HA tag and rabbit polyclonal LC3B antibody (Cell Signaling Technology, Boston); mouse monoclonal anti-Cer antibody clone 15B4 (Alexis Biochemicals, San Diego) This antibody clone has been successfully used in immunocytochemistry applications with no indication of nonspecific reactions with other lipids ( ) The secondary Alexa Fluor-conjugated F(ab)2 fragment goat anti-mouse antibody and goat anti-rabbit antibody were from Molecular Probes, Inc. (Eugene, OR.).

    Techniques: Labeling, Incubation, Synthesized, Mass Spectrometry

    PA-induced lipotoxicity and DHA neuroprotective action on primary rat cortical cells (RCC). A : Cellular morphology of control and treated (PA/BSA, 2:1, 48 hr) RCC. B : Nuclear morphology of control and treated RCC. Arrows indicate fragmented nuclei. C : Viability of RCC treated for 48 hr with PA/BSA (2:1 ratio; PA) or in cotreatment with DHA (PA + DHA). Viability was determined using the WST-1 assay. Data represent mean ± SEM of three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: PA-induced lipotoxicity and DHA neuroprotective action on primary rat cortical cells (RCC). A : Cellular morphology of control and treated (PA/BSA, 2:1, 48 hr) RCC. B : Nuclear morphology of control and treated RCC. Arrows indicate fragmented nuclei. C : Viability of RCC treated for 48 hr with PA/BSA (2:1 ratio; PA) or in cotreatment with DHA (PA + DHA). Viability was determined using the WST-1 assay. Data represent mean ± SEM of three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: WST-1 Assay

    Palmitic acid-induced lipotoxicity in NGFDPC12 cells. A : NGFDPC12 cells were exposed to PA/BSA (2:1 ratio), and viability was determined using WST-1 assay at the indicated times. B : NGFDPC12 cells were exposed to different PA/BSA ratios (0.25:1, 0.5:1, 1:1, and 2:1 with BSA at a concentration of 0.150 mM) for 24 hr. Cell viability was measured by the WST-1 assay. C : NGFDPC12 cells were exposed to 0.150 mM BSA without PA (control) or PA/BSA (2:1; PA) for 12 hr. Cells were stained with Hoechst (10 ng/liter), and nuclei were visualized under fluorescent microscopy. Arrows indicate nuclei showing chromatin condensation and fragmentation. D : Regulation of apoptosis-asociated genes in NGFDPC12 cultures exposed to PA/BSA (2:1). Quantitative RT-PCR experiments show the time-dependent mRNA expression of Bim, Bad, AIF, BNIP-3, 14.3.3, and FAS-R. GAPDH mRNA expression was used as the internal control. Data represent mean 6 SEM of three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: Palmitic acid-induced lipotoxicity in NGFDPC12 cells. A : NGFDPC12 cells were exposed to PA/BSA (2:1 ratio), and viability was determined using WST-1 assay at the indicated times. B : NGFDPC12 cells were exposed to different PA/BSA ratios (0.25:1, 0.5:1, 1:1, and 2:1 with BSA at a concentration of 0.150 mM) for 24 hr. Cell viability was measured by the WST-1 assay. C : NGFDPC12 cells were exposed to 0.150 mM BSA without PA (control) or PA/BSA (2:1; PA) for 12 hr. Cells were stained with Hoechst (10 ng/liter), and nuclei were visualized under fluorescent microscopy. Arrows indicate nuclei showing chromatin condensation and fragmentation. D : Regulation of apoptosis-asociated genes in NGFDPC12 cultures exposed to PA/BSA (2:1). Quantitative RT-PCR experiments show the time-dependent mRNA expression of Bim, Bad, AIF, BNIP-3, 14.3.3, and FAS-R. GAPDH mRNA expression was used as the internal control. Data represent mean 6 SEM of three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: WST-1 Assay, Concentration Assay, Staining, Microscopy, Quantitative RT-PCR, Expressing

    DNA fragmentation and caspase-3 activity of NGFDPC12 cells exposed to PA. A : Representative experimental results of BRDU-FITC plots (apoptotic cells) vs. PI (total DNA marker) for controls and cells exposed to PA/BSA (2:1) for 12 hr. The R2 quadrant shows cells exhibiting increased BrdU-FITC fluorescence (green). Nonapoptotic cells are indicated in red. B : Representative distribution diagram of positive apoptotic NGFDPC12 cells. Cells were treated with BSA for negative control (green), PA/BSA (2:1) for 12 hr (red) or 24 hr (blue), or staurosporine for positive control (orange). C : Quantitative analysis of positive apoptotic NGFDPC12 cells as shown in B. The data represent the mean ± SEM of three independent experiments done in triplicate. D : Caspase-3 activity in cell extracts was determined in control or NGFDPC12 cells treated with PA/BSA for 12 hr. E : Early posttreatment with BSA protects NGFDPC12 cells from PA-induced lipotoxicity. Additional BSA (0.6 mM final concentration) was added to NGFDPC-12 cells at 2 or 6 hr after initial PA/BSA (2:1 ratio) treatment. Percentage of viable cells was measured by the WST-1 assay at the end of a 24-hr incubation period. Nuclei in bottom panel were visualized with Hoechst staining. Data represent mean ± SEM of three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: DNA fragmentation and caspase-3 activity of NGFDPC12 cells exposed to PA. A : Representative experimental results of BRDU-FITC plots (apoptotic cells) vs. PI (total DNA marker) for controls and cells exposed to PA/BSA (2:1) for 12 hr. The R2 quadrant shows cells exhibiting increased BrdU-FITC fluorescence (green). Nonapoptotic cells are indicated in red. B : Representative distribution diagram of positive apoptotic NGFDPC12 cells. Cells were treated with BSA for negative control (green), PA/BSA (2:1) for 12 hr (red) or 24 hr (blue), or staurosporine for positive control (orange). C : Quantitative analysis of positive apoptotic NGFDPC12 cells as shown in B. The data represent the mean ± SEM of three independent experiments done in triplicate. D : Caspase-3 activity in cell extracts was determined in control or NGFDPC12 cells treated with PA/BSA for 12 hr. E : Early posttreatment with BSA protects NGFDPC12 cells from PA-induced lipotoxicity. Additional BSA (0.6 mM final concentration) was added to NGFDPC-12 cells at 2 or 6 hr after initial PA/BSA (2:1 ratio) treatment. Percentage of viable cells was measured by the WST-1 assay at the end of a 24-hr incubation period. Nuclei in bottom panel were visualized with Hoechst staining. Data represent mean ± SEM of three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: Activity Assay, Marker, Fluorescence, Negative Control, Positive Control, Concentration Assay, WST-1 Assay, Incubation, Staining

    ROS generation and changes in mitochondrial membrane permeability in NGFDPC12 cells undergoing PA-induced lipotoxicity. A : ROS generation in NGFDPC12 cells was detected by the 2′,7′ -dichlorofluorescein diacetate (DCF) method at 12 hr after the initial exposure to PA using flow cytometry. NGFDPC12 cells were treated with no DCF (light green), DCF (dark green), PA + DCF (blue), or hydrogen peroxide + DCF (red). B : Quantification of ROS production in NGFDPC12 cells at 3, 6, 9, and 12 hr after PA/BSA treatment. C : ROS modulation after addition of DHA, MCI-186, or BSA to NCGDPC12 cells treated with PA for 6 hr. D: Mitochondrial depolarization in NGFDPC12 cells, control or PA/BSA treated, detected by JC-1 flow cytometric analysis. JC-1 was detected in the FL1 or FL2 channel depending on its aggregation status (see Mqaterials and Methods). The R2 quadrant defines cells with leaky mitochondria showing reduced FL2 readings (green). Cells with intact mitochondria are indicated in R1 (red). Data represent mean ± SEM sent of at least three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: ROS generation and changes in mitochondrial membrane permeability in NGFDPC12 cells undergoing PA-induced lipotoxicity. A : ROS generation in NGFDPC12 cells was detected by the 2′,7′ -dichlorofluorescein diacetate (DCF) method at 12 hr after the initial exposure to PA using flow cytometry. NGFDPC12 cells were treated with no DCF (light green), DCF (dark green), PA + DCF (blue), or hydrogen peroxide + DCF (red). B : Quantification of ROS production in NGFDPC12 cells at 3, 6, 9, and 12 hr after PA/BSA treatment. C : ROS modulation after addition of DHA, MCI-186, or BSA to NCGDPC12 cells treated with PA for 6 hr. D: Mitochondrial depolarization in NGFDPC12 cells, control or PA/BSA treated, detected by JC-1 flow cytometric analysis. JC-1 was detected in the FL1 or FL2 channel depending on its aggregation status (see Mqaterials and Methods). The R2 quadrant defines cells with leaky mitochondria showing reduced FL2 readings (green). Cells with intact mitochondria are indicated in R1 (red). Data represent mean ± SEM sent of at least three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: Permeability, Flow Cytometry, Cytometry

    Inhibition of fatty acid-induced lipotoxicity by DHA. A : DHA inhibits induction of cell death by PA in NGFDPC12 cells. Cell viability was determined after treatment for 24 hr as follows: 0.150 mM BSA alone (control), PA/BSA 2:1 ratio (PA), PA/BSA 2:1 cotreated with DHA followed by an increase in BSA final concentration to 0.6 mM at 6 hr (PA + DHA + BSA at 6 hr), and DHA pretreatment for 12 hr followed by treatment with PA/BSA 2:1 (DHA 12 hr pre + PA). B : DHA treatment inhibits apoptotic features of NGFDPC12 cells treated with PA/BSA. Morphology of NGFDPC12 cells treated with BSA alone (control), PA/BSA 2:1 cotreated with DHA, or PA/BSA 2:1 for 24 hr. C : Nuclear morphology of NGFDPC12 cells treated with BSA alone (control), PA/BSA 2:1 cotreated with DHA or PA/BSA 2:1 for 24 hr. Arrows indicate nuclei exhibiting fragmentation. D : DHA cotreatment produced a significant inhibitory effect of caspase-3 activity in cellular extracts of NGFDPC12 cells exposed to PA/BSA (2:1). E : Cleavage of PARP and lamin B in NGFDPC-12 cells exposed to PA/BSA (2:1), as assessed by Western blotting. PA treatment induced the appearance of the signature apoptotic fragments of PARP (85 kDa) or lamin B (46 kDa). DHA inhibited PARP and lamin B cleavage. Data in A and D represent mean ± SEM of three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: Inhibition of fatty acid-induced lipotoxicity by DHA. A : DHA inhibits induction of cell death by PA in NGFDPC12 cells. Cell viability was determined after treatment for 24 hr as follows: 0.150 mM BSA alone (control), PA/BSA 2:1 ratio (PA), PA/BSA 2:1 cotreated with DHA followed by an increase in BSA final concentration to 0.6 mM at 6 hr (PA + DHA + BSA at 6 hr), and DHA pretreatment for 12 hr followed by treatment with PA/BSA 2:1 (DHA 12 hr pre + PA). B : DHA treatment inhibits apoptotic features of NGFDPC12 cells treated with PA/BSA. Morphology of NGFDPC12 cells treated with BSA alone (control), PA/BSA 2:1 cotreated with DHA, or PA/BSA 2:1 for 24 hr. C : Nuclear morphology of NGFDPC12 cells treated with BSA alone (control), PA/BSA 2:1 cotreated with DHA or PA/BSA 2:1 for 24 hr. Arrows indicate nuclei exhibiting fragmentation. D : DHA cotreatment produced a significant inhibitory effect of caspase-3 activity in cellular extracts of NGFDPC12 cells exposed to PA/BSA (2:1). E : Cleavage of PARP and lamin B in NGFDPC-12 cells exposed to PA/BSA (2:1), as assessed by Western blotting. PA treatment induced the appearance of the signature apoptotic fragments of PARP (85 kDa) or lamin B (46 kDa). DHA inhibited PARP and lamin B cleavage. Data in A and D represent mean ± SEM of three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: Inhibition, Concentration Assay, Produced, Activity Assay, Western Blot

    DHA reduces mitochondrial depolarization of NGFDPC12 cells undergoing PA-induced lipotoxicity. A : NGFDPC12 cells were treated with PA/BSA alone (PA) or in the presence DHA (PA + DHA) for 9 or 12 hr, and mitochondrial depolarization was determined by JC-1 flow cytometry assays. Representative flow cytometric plots are shown. B : Quantification of mitochondria depolarization (R2 in JC-1 flow cytometry) in NGFDPC12 cells undergoing PA-induced lipotoxicity. Data represent mean ± SEM of three independent experiments. ★ P

    Journal: Journal of neuroscience research

    Article Title: Activation and Reversal of Lipotoxicity in PC12 and Rat Cortical Cells Following Exposure to Palmitic Acid

    doi: 10.1002/jnr.21918

    Figure Lengend Snippet: DHA reduces mitochondrial depolarization of NGFDPC12 cells undergoing PA-induced lipotoxicity. A : NGFDPC12 cells were treated with PA/BSA alone (PA) or in the presence DHA (PA + DHA) for 9 or 12 hr, and mitochondrial depolarization was determined by JC-1 flow cytometry assays. Representative flow cytometric plots are shown. B : Quantification of mitochondria depolarization (R2 in JC-1 flow cytometry) in NGFDPC12 cells undergoing PA-induced lipotoxicity. Data represent mean ± SEM of three independent experiments. ★ P

    Article Snippet: PA and/or DHA (Sigma, St. Louis, MO) was first dissolved/diluted in 100% ethanol and further diluted in warm low-serum medium for NGFDPC12 cells, or serum-free medium for RCC, with fatty acid-free BSA (EMD Biosciences, La Jolla, CA).

    Techniques: Flow Cytometry, Cytometry

    Anti-glycan IgG in the sera of lambs vaccinated with Haemonchus contortus excretory/secretory (ES) products analyzed by ELISA. The amount of IgG against Galα1-3GalNAc-polyacrylamide (PAA), GalNAcβ1-4(Fucα1-3)GlcNAc-BSA (LDNF) and

    Journal: International journal for parasitology

    Article Title: Vaccination-induced IgG response to Gal?1-3GalNAc glycan epitopes in lambs protected against Haemonchus contortus challenge infection

    doi: 10.1016/j.ijpara.2009.07.009

    Figure Lengend Snippet: Anti-glycan IgG in the sera of lambs vaccinated with Haemonchus contortus excretory/secretory (ES) products analyzed by ELISA. The amount of IgG against Galα1-3GalNAc-polyacrylamide (PAA), GalNAcβ1-4(Fucα1-3)GlcNAc-BSA (LDNF) and

    Article Snippet: After blocking (60 min 37°C) with 1% ELISA-grade BSA (Fraction V, fatty acid free; Calbiochem, San Diego, USA) in TSM (20 mM Tris-HCl, pH 7.4, 150 mM NaCl, 2 mM CaCl2 , 2 mM MgCl2 ) and washing with TSM containing 0.1% Tween-20, glycan-specific antibodies or biotinylated GSI-B4 were added for 60 min at 37°C.

    Techniques: Enzyme-linked Immunosorbent Assay

    Effects of OF and CM on the mRNA expressions of lipogenesis-related genes. Real-time RT-PCR analysis of sterol regulatory element-binding protein-1 ( SREBP-1c ) (a) and glycerol-3-phosphate acyltransferase ( GPAT ) (b) mRNA levels in 1 mM FFA/BSA-treated HepG2 cells. All data were normalized to GAPDH mRNA, and the fold changes in expression were calculated relative to control cells (treated with 1% BSA). Each experiment was independently performed three times. Data were presented as the mean ± SD. Values not sharing common superscripts are significantly different ( p

    Journal: Mediators of Inflammation

    Article Title: Antilipotoxicity Activity of Osmanthus fragrans and Chrysanthemum morifolium Flower Extracts in Hepatocytes and Renal Glomerular Mesangial Cells

    doi: 10.1155/2017/4856095

    Figure Lengend Snippet: Effects of OF and CM on the mRNA expressions of lipogenesis-related genes. Real-time RT-PCR analysis of sterol regulatory element-binding protein-1 ( SREBP-1c ) (a) and glycerol-3-phosphate acyltransferase ( GPAT ) (b) mRNA levels in 1 mM FFA/BSA-treated HepG2 cells. All data were normalized to GAPDH mRNA, and the fold changes in expression were calculated relative to control cells (treated with 1% BSA). Each experiment was independently performed three times. Data were presented as the mean ± SD. Values not sharing common superscripts are significantly different ( p

    Article Snippet: The FFA/BSA or oleic acid (OA)/BSA complex solution was sterile-filtered through 0.22 μ m sterile filters (Millipore S.A.S., Molsheim, France) and then stored at −20°C until use.

    Techniques: Quantitative RT-PCR, Binding Assay, Expressing

    Effect of OF and CM on FFA-induced ROS production. HepG2 cells were incubated with 1 mM FFAs/BSA for 24 h in the presence of OF or CM. Vehicle cells were incubated with 0.1% DMSO in the presence of FFAs/BSA. Control cells were incubated with 1% BSA. Intracellular ROS production was quantified using the fluorescent probe DCFDA. Data were presented as mean ± SD of three independent experiments. Values not sharing common superscripts are significantly different ( p

    Journal: Mediators of Inflammation

    Article Title: Antilipotoxicity Activity of Osmanthus fragrans and Chrysanthemum morifolium Flower Extracts in Hepatocytes and Renal Glomerular Mesangial Cells

    doi: 10.1155/2017/4856095

    Figure Lengend Snippet: Effect of OF and CM on FFA-induced ROS production. HepG2 cells were incubated with 1 mM FFAs/BSA for 24 h in the presence of OF or CM. Vehicle cells were incubated with 0.1% DMSO in the presence of FFAs/BSA. Control cells were incubated with 1% BSA. Intracellular ROS production was quantified using the fluorescent probe DCFDA. Data were presented as mean ± SD of three independent experiments. Values not sharing common superscripts are significantly different ( p

    Article Snippet: The FFA/BSA or oleic acid (OA)/BSA complex solution was sterile-filtered through 0.22 μ m sterile filters (Millipore S.A.S., Molsheim, France) and then stored at −20°C until use.

    Techniques: Incubation

    Effects of OF and CM on lipid accumulation in free fatty acid-overloaded HepG2 cells. HepG2 cells were incubated with 1 mM FFAs/BSA and cotreated with various concentrations of OF and CM for 24 h. Vehicle cells were incubated with 0.1% DMSO in the presence of FFAs/BSA. Control cells were incubated with 1% BSA. Cell viability was measured by the MTT assay (a). Quantitative analysis of lipid deposition in cells by the OD 500 nm values using Oil Red O staining (b). Intracellular triglyceride (c) and cholesterol (d) contents were determined in cell lysates by an enzymatic colorimetric method using a commercially available kit. Total cholesterol and TG levels of the control cells were 25.3 ± 7.1 and 28.7 ± 2.7 μ g/mg of cellular protein, respectively. Data were presented as mean ± SD of three independent experiments. Values not sharing common superscripts are significantly different ( p

    Journal: Mediators of Inflammation

    Article Title: Antilipotoxicity Activity of Osmanthus fragrans and Chrysanthemum morifolium Flower Extracts in Hepatocytes and Renal Glomerular Mesangial Cells

    doi: 10.1155/2017/4856095

    Figure Lengend Snippet: Effects of OF and CM on lipid accumulation in free fatty acid-overloaded HepG2 cells. HepG2 cells were incubated with 1 mM FFAs/BSA and cotreated with various concentrations of OF and CM for 24 h. Vehicle cells were incubated with 0.1% DMSO in the presence of FFAs/BSA. Control cells were incubated with 1% BSA. Cell viability was measured by the MTT assay (a). Quantitative analysis of lipid deposition in cells by the OD 500 nm values using Oil Red O staining (b). Intracellular triglyceride (c) and cholesterol (d) contents were determined in cell lysates by an enzymatic colorimetric method using a commercially available kit. Total cholesterol and TG levels of the control cells were 25.3 ± 7.1 and 28.7 ± 2.7 μ g/mg of cellular protein, respectively. Data were presented as mean ± SD of three independent experiments. Values not sharing common superscripts are significantly different ( p

    Article Snippet: The FFA/BSA or oleic acid (OA)/BSA complex solution was sterile-filtered through 0.22 μ m sterile filters (Millipore S.A.S., Molsheim, France) and then stored at −20°C until use.

    Techniques: Incubation, MTT Assay, Staining