lipoprotein depleted serum lpds  (Thermo Fisher)


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    Name:
    TaqMan Array Mouse Lipoprotein Signaling Cholesterol Metabolism 96 well plate fast Configurable
    Description:
    The Lipoprotein Signaling Cholesterol Metabolism array profiles the range of genes involved in lipoprotein transport and cholesterol metabolism including LDL and HDL receptors as well as their associated proteins
    Catalog Number:
    RPWCWDX
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    None
    Category:
    GX
    Format:
    Format 96 Fast
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    Structured Review

    Thermo Fisher lipoprotein depleted serum lpds
    Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in <t>AML12</t> cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum <t>(LPDS)</t> medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P
    The Lipoprotein Signaling Cholesterol Metabolism array profiles the range of genes involved in lipoprotein transport and cholesterol metabolism including LDL and HDL receptors as well as their associated proteins
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    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Images

    1) Product Images from "Integrating mouse and human genetic data to move beyond GWAS and identify causal genes in cholesterol metabolism"

    Article Title: Integrating mouse and human genetic data to move beyond GWAS and identify causal genes in cholesterol metabolism

    Journal: Cell metabolism

    doi: 10.1016/j.cmet.2020.02.015

    Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in AML12 cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum (LPDS) medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P
    Figure Legend Snippet: Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in AML12 cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum (LPDS) medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P

    Techniques Used: Mouse Assay, Expressing, Incubation

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: Quercetin-3-glucoside increases low-density lipoprotein receptor (LDLR) expression, attenuates proprotein convertase subtilisin/kexin 9 (PCSK9) secretion, and stimulates LDL uptake by Huh7 human hepatocytes in culture
    Article Snippet: The following antibodies were from commercial sources: anti-human LDLR (R & D Systems), anti-β-actin (Sigma), anti-SREBP-2 (Santa Cruz), anti-HMG-CoAR (Millipore), and anti-sortilin (Abcam), Horseradish peroxidase (HRP)-conjugated anti-rabbit or mouse immunoglobulins (Ig) (GE HealthCare) or anti-goat Ig (Santa Cruz). .. The chemiluminescence revelation kit was from PerkinElmer; the PCSK9 ELISA kit from Circulex; the RNeasy extraction kit from Qiagen; the Superscript II RNase H– Reverse Transcriptase, bodipy-LDL, non-conjugated LDL and Alexa Fluor 488™ were from Invitrogen; lipoprotein-depleted serum (LPDS), Q3G and simvastatin from Sigma; the FastStart TaqMan ProbeMaster-Rox master mix, primer pairs, and Universal Probe Library (UPL) fluorescent probes, and the Protease Inhibitor Cocktail (PIC) from Roche; the Amplify fluor solution from Amersham Biosciences, the Vectashield mounting medium with 4′,6-diamidino-2-phenylindole (DAPI) from Vector Laboratories. .. 2.2 Cell culture and lysis Unless otherwise specified, all Huh7 cell incubations were carried out at 37 °C in a humidified 5% CO2 –95% air atmosphere.

    Protease Inhibitor:

    Article Title: Quercetin-3-glucoside increases low-density lipoprotein receptor (LDLR) expression, attenuates proprotein convertase subtilisin/kexin 9 (PCSK9) secretion, and stimulates LDL uptake by Huh7 human hepatocytes in culture
    Article Snippet: The following antibodies were from commercial sources: anti-human LDLR (R & D Systems), anti-β-actin (Sigma), anti-SREBP-2 (Santa Cruz), anti-HMG-CoAR (Millipore), and anti-sortilin (Abcam), Horseradish peroxidase (HRP)-conjugated anti-rabbit or mouse immunoglobulins (Ig) (GE HealthCare) or anti-goat Ig (Santa Cruz). .. The chemiluminescence revelation kit was from PerkinElmer; the PCSK9 ELISA kit from Circulex; the RNeasy extraction kit from Qiagen; the Superscript II RNase H– Reverse Transcriptase, bodipy-LDL, non-conjugated LDL and Alexa Fluor 488™ were from Invitrogen; lipoprotein-depleted serum (LPDS), Q3G and simvastatin from Sigma; the FastStart TaqMan ProbeMaster-Rox master mix, primer pairs, and Universal Probe Library (UPL) fluorescent probes, and the Protease Inhibitor Cocktail (PIC) from Roche; the Amplify fluor solution from Amersham Biosciences, the Vectashield mounting medium with 4′,6-diamidino-2-phenylindole (DAPI) from Vector Laboratories. .. 2.2 Cell culture and lysis Unless otherwise specified, all Huh7 cell incubations were carried out at 37 °C in a humidified 5% CO2 –95% air atmosphere.

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  • 99
    Thermo Fisher dmem medium
    25HC does not directly affect bacterial infectivity or host viability. 25HC could inhibit L. monocytogenes infection through different mechanisms. For example, it may (1) directly reduce bacterial viability, (2) inhibit the expression or function of bacterial virulence factors, (3) induce host cell death, or (4) regulate host cellular processes that limit bacterial infection. a , To determine whether 25HC directly reduced bacterial viability, a starting bacterial culture was back-diluted in <t>DMEM</t> (10% FBS) supplemented with vehicle (EtOH) or 25HC (5 μM). Bacterial cultures were incubated at 37°C while shaking at 200 rpm, and OD 600 was measured for each sample at the indicated time points. Mean values from 3 independent experiments are plotted, and error bars show s.d. b , To determine whether 25HC directly modifies bacterial virulence, GFP-expressing L. monocytogenes were cultured overnight in BHI supplemented with vehicle (EtOH) or 25HC (5 μM) and <t>HEK293A</t> cells were then infected with bacteria from either culture (MOI = 20, 6 hours). Infection was analysed by flow cytometry. Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined by student’s unpaired t-test (two-tailed). c-d , Host cell viability was assessed in cells treated with 25HC (c) or in cells virally transduced with CH25H (d). HEK293A cells were treated with 25HC (5 μM) or vehicle (EtOH) for 6, 16, or 24 hours (c) or transduced with Fluc or CH25H for 72 hours (d). Cell viability was evaluated by measuring ATP production using CellTiter-Glo assays. Data are normalized to vehicle (EtOH) in (c), and Fluc in (d). Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined before normalization by student’s unpaired t-test (two-tailed).
    Dmem Medium, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher lpds
    ATGL expression in macrophages and foam cells. Mouse peritoneal macrophages, human THP-1, and human monocyte-derived macrophages ( HMDM ) were cultivated in <t>DMEM,</t> 10% <t>LPDS</t> in the absence (control) or presence of 100 μg of acLDL/ml. Total RNA was isolated and reverse-transcribed, and mRNA expression of ATGL ( A and C ) and hormone-sensitive lipase ( HSL ) was determined by real time PCR, including murine hypoxanthine-guanine phosphoribosyltransferase or human ( hu ) porphobilinogen deaminase normalization ( A ). Untreated macrophages were arbitrarily set to 1. Data are expressed as mean values ( n = 3) ± S.E. of triplicate repeats. ***, p ≤ 0.001. B , cell extracts of macrophages, foam cells (40 μg per lane), and white adipose tissue ( WAT ) (10 and 40 μg per lane) were resolved by SDS-PAGE. Protein expression of ATGL and hormone-sensitive lipase were analyzed by Western blotting relative to the expression of β-actin. STD , standard.
    Lpds, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher lipoprotein depleted serum lpds
    Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in <t>AML12</t> cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum <t>(LPDS)</t> medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P
    Lipoprotein Depleted Serum Lpds, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lipoprotein depleted serum lpds/product/Thermo Fisher
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    97
    Thermo Fisher lpd specific raph1 small interfering rna sirna
    Depletion of <t>Lpd</t> in HeLa cells using <t>RAPH1</t> <t>siRNA</t> interference significantly reduced the number of plaques formed by L. monocytogenes . The results of Western blot analysis using anti-Lpd antibody against the cell lysate of HeLa cells either transformed with Lpd-expressing plasmid or transfected with 1 nM nonspecific Luc siRNA as a control with RAPH1 individual or mixed siRNAs for 3 days are shown. Tubulin was used as the control. The relative intensity of the band of each sample against HeLa cell lysate was measured using ImageJ. The number of plaques was significantly lower in HeLa cell knockdown of Lpd expression using a RAPH1 siRNA mixture and three of the individual siRNAs. Error bars indicate standard errors. Stars indicate statistically significant differences. *, P
    Lpd Specific Raph1 Small Interfering Rna Sirna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    25HC does not directly affect bacterial infectivity or host viability. 25HC could inhibit L. monocytogenes infection through different mechanisms. For example, it may (1) directly reduce bacterial viability, (2) inhibit the expression or function of bacterial virulence factors, (3) induce host cell death, or (4) regulate host cellular processes that limit bacterial infection. a , To determine whether 25HC directly reduced bacterial viability, a starting bacterial culture was back-diluted in DMEM (10% FBS) supplemented with vehicle (EtOH) or 25HC (5 μM). Bacterial cultures were incubated at 37°C while shaking at 200 rpm, and OD 600 was measured for each sample at the indicated time points. Mean values from 3 independent experiments are plotted, and error bars show s.d. b , To determine whether 25HC directly modifies bacterial virulence, GFP-expressing L. monocytogenes were cultured overnight in BHI supplemented with vehicle (EtOH) or 25HC (5 μM) and HEK293A cells were then infected with bacteria from either culture (MOI = 20, 6 hours). Infection was analysed by flow cytometry. Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined by student’s unpaired t-test (two-tailed). c-d , Host cell viability was assessed in cells treated with 25HC (c) or in cells virally transduced with CH25H (d). HEK293A cells were treated with 25HC (5 μM) or vehicle (EtOH) for 6, 16, or 24 hours (c) or transduced with Fluc or CH25H for 72 hours (d). Cell viability was evaluated by measuring ATP production using CellTiter-Glo assays. Data are normalized to vehicle (EtOH) in (c), and Fluc in (d). Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined before normalization by student’s unpaired t-test (two-tailed).

    Journal: Nature microbiology

    Article Title: Oxysterols provide innate immunity to bacterial infection by mobilizing cell surface accessible cholesterol

    doi: 10.1038/s41564-020-0701-5

    Figure Lengend Snippet: 25HC does not directly affect bacterial infectivity or host viability. 25HC could inhibit L. monocytogenes infection through different mechanisms. For example, it may (1) directly reduce bacterial viability, (2) inhibit the expression or function of bacterial virulence factors, (3) induce host cell death, or (4) regulate host cellular processes that limit bacterial infection. a , To determine whether 25HC directly reduced bacterial viability, a starting bacterial culture was back-diluted in DMEM (10% FBS) supplemented with vehicle (EtOH) or 25HC (5 μM). Bacterial cultures were incubated at 37°C while shaking at 200 rpm, and OD 600 was measured for each sample at the indicated time points. Mean values from 3 independent experiments are plotted, and error bars show s.d. b , To determine whether 25HC directly modifies bacterial virulence, GFP-expressing L. monocytogenes were cultured overnight in BHI supplemented with vehicle (EtOH) or 25HC (5 μM) and HEK293A cells were then infected with bacteria from either culture (MOI = 20, 6 hours). Infection was analysed by flow cytometry. Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined by student’s unpaired t-test (two-tailed). c-d , Host cell viability was assessed in cells treated with 25HC (c) or in cells virally transduced with CH25H (d). HEK293A cells were treated with 25HC (5 μM) or vehicle (EtOH) for 6, 16, or 24 hours (c) or transduced with Fluc or CH25H for 72 hours (d). Cell viability was evaluated by measuring ATP production using CellTiter-Glo assays. Data are normalized to vehicle (EtOH) in (c), and Fluc in (d). Bars represent mean values. Error bars show s.d. from three independent experiments and statistical significance was determined before normalization by student’s unpaired t-test (two-tailed).

    Article Snippet: For the BMDM medium-transfer infection assays ( , and ), 15,000 HEK293A cells were seeded per well of a 96-well plate in DMEM medium (containing 5% LPDS, 1×NEAA).

    Techniques: Infection, Expressing, Incubation, Cell Culture, Flow Cytometry, Two Tailed Test, Transduction

    ATGL expression in macrophages and foam cells. Mouse peritoneal macrophages, human THP-1, and human monocyte-derived macrophages ( HMDM ) were cultivated in DMEM, 10% LPDS in the absence (control) or presence of 100 μg of acLDL/ml. Total RNA was isolated and reverse-transcribed, and mRNA expression of ATGL ( A and C ) and hormone-sensitive lipase ( HSL ) was determined by real time PCR, including murine hypoxanthine-guanine phosphoribosyltransferase or human ( hu ) porphobilinogen deaminase normalization ( A ). Untreated macrophages were arbitrarily set to 1. Data are expressed as mean values ( n = 3) ± S.E. of triplicate repeats. ***, p ≤ 0.001. B , cell extracts of macrophages, foam cells (40 μg per lane), and white adipose tissue ( WAT ) (10 and 40 μg per lane) were resolved by SDS-PAGE. Protein expression of ATGL and hormone-sensitive lipase were analyzed by Western blotting relative to the expression of β-actin. STD , standard.

    Journal: The Journal of Biological Chemistry

    Article Title: Efficient Phagocytosis Requires Triacylglycerol Hydrolysis by Adipose Triglyceride Lipase *

    doi: 10.1074/jbc.M110.107854

    Figure Lengend Snippet: ATGL expression in macrophages and foam cells. Mouse peritoneal macrophages, human THP-1, and human monocyte-derived macrophages ( HMDM ) were cultivated in DMEM, 10% LPDS in the absence (control) or presence of 100 μg of acLDL/ml. Total RNA was isolated and reverse-transcribed, and mRNA expression of ATGL ( A and C ) and hormone-sensitive lipase ( HSL ) was determined by real time PCR, including murine hypoxanthine-guanine phosphoribosyltransferase or human ( hu ) porphobilinogen deaminase normalization ( A ). Untreated macrophages were arbitrarily set to 1. Data are expressed as mean values ( n = 3) ± S.E. of triplicate repeats. ***, p ≤ 0.001. B , cell extracts of macrophages, foam cells (40 μg per lane), and white adipose tissue ( WAT ) (10 and 40 μg per lane) were resolved by SDS-PAGE. Protein expression of ATGL and hormone-sensitive lipase were analyzed by Western blotting relative to the expression of β-actin. STD , standard.

    Article Snippet: Macrophages were cultured in DMEM, 10% LPDS (Invitrogen) supplemented with 1% penicillin, 1% streptomycin for 2 h. Thereafter, cells were washed twice with PBS, and if not stated otherwise, the adherent macrophages were cultured in high glucose (25 mm ) DMEM containing 4 mm glutamine, 1 mm pyruvate, and 10% LPDS.

    Techniques: Expressing, Derivative Assay, Isolation, Real-time Polymerase Chain Reaction, SDS Page, Western Blot

    mRNA levels of mitochondrial genes in Atgl −/− and WT macrophages and foam cells. MPM were cultivated in DMEM, 10% LPDS in the absence or presence of 100 μg of acLDL/ml (foam cells). Total RNA was isolated from cells and reverse-transcribed, and mRNA levels of carnitine palmitoyltransferase ( CPT )1a ( A ) and long chain acyl-CoA dehydrogenase ( LCAD ) ( B ) were determined by real time PCR, including normalization to hypoxanthine-guanine phosphoribosyltransferase ( HPRT ) levels. Untreated MPM were arbitrarily set to 1. Data are expressed as mean values ± S.E. of triplicate repeats. C , long chain acyl-CoA. D , carnitine ester concentrations were determined in macrophages of Atgl −/− and WT mice. Data are expressed as mean values ( n = 4–5) ± S.E. correlated to protein concentrations. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Efficient Phagocytosis Requires Triacylglycerol Hydrolysis by Adipose Triglyceride Lipase *

    doi: 10.1074/jbc.M110.107854

    Figure Lengend Snippet: mRNA levels of mitochondrial genes in Atgl −/− and WT macrophages and foam cells. MPM were cultivated in DMEM, 10% LPDS in the absence or presence of 100 μg of acLDL/ml (foam cells). Total RNA was isolated from cells and reverse-transcribed, and mRNA levels of carnitine palmitoyltransferase ( CPT )1a ( A ) and long chain acyl-CoA dehydrogenase ( LCAD ) ( B ) were determined by real time PCR, including normalization to hypoxanthine-guanine phosphoribosyltransferase ( HPRT ) levels. Untreated MPM were arbitrarily set to 1. Data are expressed as mean values ± S.E. of triplicate repeats. C , long chain acyl-CoA. D , carnitine ester concentrations were determined in macrophages of Atgl −/− and WT mice. Data are expressed as mean values ( n = 4–5) ± S.E. correlated to protein concentrations. *, p

    Article Snippet: Macrophages were cultured in DMEM, 10% LPDS (Invitrogen) supplemented with 1% penicillin, 1% streptomycin for 2 h. Thereafter, cells were washed twice with PBS, and if not stated otherwise, the adherent macrophages were cultured in high glucose (25 mm ) DMEM containing 4 mm glutamine, 1 mm pyruvate, and 10% LPDS.

    Techniques: Isolation, Cycling Probe Technology, Real-time Polymerase Chain Reaction, Mouse Assay

    Phagocytosis in Atgl −/− and WT macrophages. A , MPM from Atgl −/− and WT mice were cultivated in DMEM, 10% LPDS with 0, 6, and 25 m m glucose for 1 and 8 h, respectively. Phagocytosis of fluorescein-labeled E. coli particles is presented as mean values ( n = 6) ± S.E. of two independent experiments. Phagocytosis of WT cells was arbitrarily set to 100%. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Efficient Phagocytosis Requires Triacylglycerol Hydrolysis by Adipose Triglyceride Lipase *

    doi: 10.1074/jbc.M110.107854

    Figure Lengend Snippet: Phagocytosis in Atgl −/− and WT macrophages. A , MPM from Atgl −/− and WT mice were cultivated in DMEM, 10% LPDS with 0, 6, and 25 m m glucose for 1 and 8 h, respectively. Phagocytosis of fluorescein-labeled E. coli particles is presented as mean values ( n = 6) ± S.E. of two independent experiments. Phagocytosis of WT cells was arbitrarily set to 100%. *, p

    Article Snippet: Macrophages were cultured in DMEM, 10% LPDS (Invitrogen) supplemented with 1% penicillin, 1% streptomycin for 2 h. Thereafter, cells were washed twice with PBS, and if not stated otherwise, the adherent macrophages were cultured in high glucose (25 mm ) DMEM containing 4 mm glutamine, 1 mm pyruvate, and 10% LPDS.

    Techniques: Mouse Assay, Labeling

    ATP concentrations and ADP/ATP ratios in Atgl −/− and WT macrophages. A , ATP levels in Atgl −/− and WT MPM were measured after cultivating the cells for 24 h in DMEM, 10% LPDS containing 0, 6, and 25 m m glucose. Oligomycin (0.5 μ m ) was used as an ATP-depletion control. Data are presented as mean values ( n = 4) ± S.E. ***, p ≤ 0.001. B , ADP/ATP ratios in Atgl −/− and WT MPM were determined using the EnzyLight TM ADP/ATP ratio assay kit. Data are expressed as mean values ( n = 4) ± S.E. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Efficient Phagocytosis Requires Triacylglycerol Hydrolysis by Adipose Triglyceride Lipase *

    doi: 10.1074/jbc.M110.107854

    Figure Lengend Snippet: ATP concentrations and ADP/ATP ratios in Atgl −/− and WT macrophages. A , ATP levels in Atgl −/− and WT MPM were measured after cultivating the cells for 24 h in DMEM, 10% LPDS containing 0, 6, and 25 m m glucose. Oligomycin (0.5 μ m ) was used as an ATP-depletion control. Data are presented as mean values ( n = 4) ± S.E. ***, p ≤ 0.001. B , ADP/ATP ratios in Atgl −/− and WT MPM were determined using the EnzyLight TM ADP/ATP ratio assay kit. Data are expressed as mean values ( n = 4) ± S.E. *, p

    Article Snippet: Macrophages were cultured in DMEM, 10% LPDS (Invitrogen) supplemented with 1% penicillin, 1% streptomycin for 2 h. Thereafter, cells were washed twice with PBS, and if not stated otherwise, the adherent macrophages were cultured in high glucose (25 mm ) DMEM containing 4 mm glutamine, 1 mm pyruvate, and 10% LPDS.

    Techniques:

    Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in AML12 cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum (LPDS) medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P

    Journal: Cell metabolism

    Article Title: Integrating mouse and human genetic data to move beyond GWAS and identify causal genes in cholesterol metabolism

    doi: 10.1016/j.cmet.2020.02.015

    Figure Lengend Snippet: Sesn1 regulates cellular and plasma cholesterol content independent of LDLR and SREBP2 signaling. (A) Liver PCSK9 and LDLR protein levels in mice after 0.2% cholesterol diet feeding for three days. n = 4. (B) Plasma total cholesterol levels in Ldlr −/− Sesn1 +/+ (black) and Ldlr −/− Sesn1 +/− (red) male mice after 4 and 12 weeks of cholesterol diet feeding. n > 9. (C) Liver mRNA expression levels of cholesterol and lipid genes in male Sesn1 +/+ (black) and Sesn1 −/− (red) mice fed a cholesterol diet for three days. n = 4. (D) Cellular cholesterol levels in AML12 cells after Sesn1 silencing (red) or control (black) incubated in FBS or lipoprotein depleted serum (LPDS) medium. n = 4. (E) LDLR protein levels in Sesn1 siRNA or control siRNA treated AML12 cells with FBS, n = 4. (F) mRNA expression levels of cholesterol and lipid metabolism genes in AML12 cells after Sesn1 silencing with FBS or LPDS medium. n = 3. Data represented is mean ± SE, ** P

    Article Snippet: AML12 cells were incubated with lipoprotein depleted serum (LPDS) (Alfa Aesar, Havervill, MA) medium for additional 24 hours before harvest.

    Techniques: Mouse Assay, Expressing, Incubation

    Depletion of Lpd in HeLa cells using RAPH1 siRNA interference significantly reduced the number of plaques formed by L. monocytogenes . The results of Western blot analysis using anti-Lpd antibody against the cell lysate of HeLa cells either transformed with Lpd-expressing plasmid or transfected with 1 nM nonspecific Luc siRNA as a control with RAPH1 individual or mixed siRNAs for 3 days are shown. Tubulin was used as the control. The relative intensity of the band of each sample against HeLa cell lysate was measured using ImageJ. The number of plaques was significantly lower in HeLa cell knockdown of Lpd expression using a RAPH1 siRNA mixture and three of the individual siRNAs. Error bars indicate standard errors. Stars indicate statistically significant differences. *, P

    Journal: Infection and Immunity

    Article Title: Lamellipodin Is Important for Cell-to-Cell Spread and Actin-Based Motility in Listeria monocytogenes

    doi: 10.1128/IAI.00193-15

    Figure Lengend Snippet: Depletion of Lpd in HeLa cells using RAPH1 siRNA interference significantly reduced the number of plaques formed by L. monocytogenes . The results of Western blot analysis using anti-Lpd antibody against the cell lysate of HeLa cells either transformed with Lpd-expressing plasmid or transfected with 1 nM nonspecific Luc siRNA as a control with RAPH1 individual or mixed siRNAs for 3 days are shown. Tubulin was used as the control. The relative intensity of the band of each sample against HeLa cell lysate was measured using ImageJ. The number of plaques was significantly lower in HeLa cell knockdown of Lpd expression using a RAPH1 siRNA mixture and three of the individual siRNAs. Error bars indicate standard errors. Stars indicate statistically significant differences. *, P

    Article Snippet: Lpd RNA interference (RNAi) was performed using Interferin (Polyplus)-mediated delivery of Lpd-specific RAPH1 small interfering RNA (siRNA) (Thermo Scientific).

    Techniques: Western Blot, Transformation Assay, Expressing, Plasmid Preparation, Transfection