pard3b expression  (Roche)


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    Structured Review

    Roche pard3b expression
    Analysis of <t>PARD3B</t> single-nucleotide polymorphisms (SNPs). A , Haplotype and LD structure of the SNPs for the PARD3B region. SNPs outlined in blue were typed on Affymetrix 6.0 for European American samples and those highlighted with yellow were typed on Illummina300 in the GRIV and Amsterdam Cohort Study (ACS) European cohorts. Only HapMap SNPs are included here; underlying LD structure is from HapMap. SNPs with an asterisk were among the top ranking SNPs in this study. All haplotypes with a frequency > 1% in the discovery cohorts are shown. SNPs that rank in the top 10 of the AIDS 93 progression analysis track a single haplotype, hap 4 (tracking SNPs are highlighted in bold), that is itself significant at the genome-wide level. Alleles from the top hit in this study (rs11884476) are shown in green; alleles from the ranking SNP typed on both platforms (rs10185378) are shown in blue. The three other SNPs in this region that are typed in the European cohorts (yellow) do not track the significant haplotype. B , Distribution of rs10185378 genotypes in the combined GRIV and ACS cohorts. Genotypes and allele frequencies for in control subjects ( n = 1071) and case patients (rapid progressors; n = 231) CT ( light gray ), and TT ( black ) genotypes and T allele frequency ( dark gray ), where T is the minor allele with an overall frequency of .075, a frequency in controls of .078, and a frequency of .041 among rapid progressors.
    Pard3b Expression, supplied by Roche, used in various techniques. Bioz Stars score: 85/100, based on 348 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Genome-wide Association Study Implicates PARD3B-based AIDS Restriction"

    Article Title: Genome-wide Association Study Implicates PARD3B-based AIDS Restriction

    Journal: The Journal of Infectious Diseases

    doi: 10.1093/infdis/jir046

    Analysis of PARD3B single-nucleotide polymorphisms (SNPs). A , Haplotype and LD structure of the SNPs for the PARD3B region. SNPs outlined in blue were typed on Affymetrix 6.0 for European American samples and those highlighted with yellow were typed on Illummina300 in the GRIV and Amsterdam Cohort Study (ACS) European cohorts. Only HapMap SNPs are included here; underlying LD structure is from HapMap. SNPs with an asterisk were among the top ranking SNPs in this study. All haplotypes with a frequency > 1% in the discovery cohorts are shown. SNPs that rank in the top 10 of the AIDS 93 progression analysis track a single haplotype, hap 4 (tracking SNPs are highlighted in bold), that is itself significant at the genome-wide level. Alleles from the top hit in this study (rs11884476) are shown in green; alleles from the ranking SNP typed on both platforms (rs10185378) are shown in blue. The three other SNPs in this region that are typed in the European cohorts (yellow) do not track the significant haplotype. B , Distribution of rs10185378 genotypes in the combined GRIV and ACS cohorts. Genotypes and allele frequencies for in control subjects ( n = 1071) and case patients (rapid progressors; n = 231) CT ( light gray ), and TT ( black ) genotypes and T allele frequency ( dark gray ), where T is the minor allele with an overall frequency of .075, a frequency in controls of .078, and a frequency of .041 among rapid progressors.
    Figure Legend Snippet: Analysis of PARD3B single-nucleotide polymorphisms (SNPs). A , Haplotype and LD structure of the SNPs for the PARD3B region. SNPs outlined in blue were typed on Affymetrix 6.0 for European American samples and those highlighted with yellow were typed on Illummina300 in the GRIV and Amsterdam Cohort Study (ACS) European cohorts. Only HapMap SNPs are included here; underlying LD structure is from HapMap. SNPs with an asterisk were among the top ranking SNPs in this study. All haplotypes with a frequency > 1% in the discovery cohorts are shown. SNPs that rank in the top 10 of the AIDS 93 progression analysis track a single haplotype, hap 4 (tracking SNPs are highlighted in bold), that is itself significant at the genome-wide level. Alleles from the top hit in this study (rs11884476) are shown in green; alleles from the ranking SNP typed on both platforms (rs10185378) are shown in blue. The three other SNPs in this region that are typed in the European cohorts (yellow) do not track the significant haplotype. B , Distribution of rs10185378 genotypes in the combined GRIV and ACS cohorts. Genotypes and allele frequencies for in control subjects ( n = 1071) and case patients (rapid progressors; n = 231) CT ( light gray ), and TT ( black ) genotypes and T allele frequency ( dark gray ), where T is the minor allele with an overall frequency of .075, a frequency in controls of .078, and a frequency of .041 among rapid progressors.

    Techniques Used: Genome Wide

    A , Primer probe design for the expression of alternative splice forms. Introns are represented as thin blue lines, and exons are blue rectangles with the exon number designated in black. Probes are represented as red lines, and primers are blue with arrows. B , Expression of alternative PARD3B splice forms by rs10185378 genotype. The arithmetic means of PARD3B normalized transcript expression grouped by genotype (CC, n = 12; CT, n = 8; TT, n ). C , Relative difference between PARD3B expression of isoform A and isoforms B/C with 95% confidence intervals plotted by genotype ( P = .006, co-dominant model).
    Figure Legend Snippet: A , Primer probe design for the expression of alternative splice forms. Introns are represented as thin blue lines, and exons are blue rectangles with the exon number designated in black. Probes are represented as red lines, and primers are blue with arrows. B , Expression of alternative PARD3B splice forms by rs10185378 genotype. The arithmetic means of PARD3B normalized transcript expression grouped by genotype (CC, n = 12; CT, n = 8; TT, n ). C , Relative difference between PARD3B expression of isoform A and isoforms B/C with 95% confidence intervals plotted by genotype ( P = .006, co-dominant model).

    Techniques Used: Expressing

    2) Product Images from "Novel PEX11B Mutations Extend the Peroxisome Biogenesis Disorder 14B Phenotypic Spectrum and Underscore Congenital Cataract as an Early Feature"

    Article Title: Novel PEX11B Mutations Extend the Peroxisome Biogenesis Disorder 14B Phenotypic Spectrum and Underscore Congenital Cataract as an Early Feature

    Journal: Investigative ophthalmology & visual science

    doi: 10.1167/iovs.16-21026

    Abnormalities of the hands and feet of patients with PEX11B mutations. Patient I.1 ( A ) and patient I.2 ( B ) showing broad feet and hallux vulgus; hands of patient I.2 ( C ) showing abnormal metacarpal and phalangeal joints and proximal implanting of the thumb; hands of patient II.1 ( D ) showing abnormally short distal phalanges and proximal implanting of the thumb.
    Figure Legend Snippet: Abnormalities of the hands and feet of patients with PEX11B mutations. Patient I.1 ( A ) and patient I.2 ( B ) showing broad feet and hallux vulgus; hands of patient I.2 ( C ) showing abnormal metacarpal and phalangeal joints and proximal implanting of the thumb; hands of patient II.1 ( D ) showing abnormally short distal phalanges and proximal implanting of the thumb.

    Techniques Used:

    ( A ) Pedigree of Family I included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family I shows sequencing chromatogram of PEX11B c.235C > T p.(Arg79Ter) homozygous variant in I.1 and I.2 in comparison with control trace (arrow indicates altered nucleotide).
    Figure Legend Snippet: ( A ) Pedigree of Family I included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family I shows sequencing chromatogram of PEX11B c.235C > T p.(Arg79Ter) homozygous variant in I.1 and I.2 in comparison with control trace (arrow indicates altered nucleotide).

    Techniques Used: Sequencing, Variant Assay

    ( A ) Pedigree of Family II included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family II shows chromatogram of PEX11B c.136C > T p.(Arg46Ter) homozygous variant in II.1 that is heterozygous in his mother ( arrow indicates altered nucleotide).
    Figure Legend Snippet: ( A ) Pedigree of Family II included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family II shows chromatogram of PEX11B c.136C > T p.(Arg46Ter) homozygous variant in II.1 that is heterozygous in his mother ( arrow indicates altered nucleotide).

    Techniques Used: Variant Assay

    ( A ) Pedigree of Family III included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family III shows sequencing chromatogram indicating c.595C > T p.(Arg299Ter) heterozygous variant in III.1 and III.2 in comparison with normal control ( arrow indicates altered nucleotide). ( C ) ExomeDepth analysis indicating deletion of exons 1 to 3 of PEX11B according to WES read ratios in patient III.1.
    Figure Legend Snippet: ( A ) Pedigree of Family III included in this study. Arrows indicate proband. White square or circle = unaffected individual; black square or circle = affected individual; white circle with black segment = individual reported to have eye problems and short stature but not formal diagnosis; * = individual with eye abnormalities and/or short stature. ( B ) Family III shows sequencing chromatogram indicating c.595C > T p.(Arg299Ter) heterozygous variant in III.1 and III.2 in comparison with normal control ( arrow indicates altered nucleotide). ( C ) ExomeDepth analysis indicating deletion of exons 1 to 3 of PEX11B according to WES read ratios in patient III.1.

    Techniques Used: Sequencing, Variant Assay

    3) Product Images from "Accuracy, Precision, and Method Detection Limits of Quantitative PCR for Airborne Bacteria and Fungi ▿"

    Article Title: Accuracy, Precision, and Method Detection Limits of Quantitative PCR for Airborne Bacteria and Fungi ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.01240-10

    Instrument repeatability as a function of cell quantity COV ( n = 7). The qPCR MDLs are 5 cells for B. atrophaeus and 0.05 cells for A. fumigatus .
    Figure Legend Snippet: Instrument repeatability as a function of cell quantity COV ( n = 7). The qPCR MDLs are 5 cells for B. atrophaeus and 0.05 cells for A. fumigatus .

    Techniques Used: Real-time Polymerase Chain Reaction

    4) Product Images from "Imperatorin as a Promising Chemotherapeutic Agent against Human Larynx Cancer and Rhabdomyosarcoma Cells"

    Article Title: Imperatorin as a Promising Chemotherapeutic Agent against Human Larynx Cancer and Rhabdomyosarcoma Cells

    Journal: Molecules

    doi: 10.3390/molecules25092046

    p21, cyclin D1, and p53 expression on protein and mRNA level in human rhabdomyosarcoma and larynx cancer cell lines. Quantification of CCND1 ( a ) and CDKN1A ( c ) and TP53 ( e ) genes expression by means of qPCR in RK33 and TE671 cells exposed (24 h) to imperatorin (25–100 µM) compared with controls (* p
    Figure Legend Snippet: p21, cyclin D1, and p53 expression on protein and mRNA level in human rhabdomyosarcoma and larynx cancer cell lines. Quantification of CCND1 ( a ) and CDKN1A ( c ) and TP53 ( e ) genes expression by means of qPCR in RK33 and TE671 cells exposed (24 h) to imperatorin (25–100 µM) compared with controls (* p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    5) Product Images from "9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages"

    Article Title: 9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages

    Journal: Nutrients

    doi: 10.3390/nu8070435

    9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p
    Figure Legend Snippet: 9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    6) Product Images from "Dietary β-Carotene Rescues Vitamin A Deficiency and Inhibits Atherogenesis in Apolipoprotein E-Deficient Mice"

    Article Title: Dietary β-Carotene Rescues Vitamin A Deficiency and Inhibits Atherogenesis in Apolipoprotein E-Deficient Mice

    Journal: Nutrients

    doi: 10.3390/nu12061625

    Liver gene expression of CYP26A1 ( A ) CYP26B1 ( B ) and LDL R ( C ) in apoE −/− mice, fed with VAD diet, VA, BC or BC+VA. Liver mRNA levels of the indicated genes were detected by real-time PCR. GAPDH was used as a reference gene. Data are means ±SE, n = 5–8 in each group. Mean values (a,b) not sharing a common superscript were significantly different by one-way ANOVA and Tukey post-hoc test comparison ( p
    Figure Legend Snippet: Liver gene expression of CYP26A1 ( A ) CYP26B1 ( B ) and LDL R ( C ) in apoE −/− mice, fed with VAD diet, VA, BC or BC+VA. Liver mRNA levels of the indicated genes were detected by real-time PCR. GAPDH was used as a reference gene. Data are means ±SE, n = 5–8 in each group. Mean values (a,b) not sharing a common superscript were significantly different by one-way ANOVA and Tukey post-hoc test comparison ( p

    Techniques Used: Expressing, Mouse Assay, Real-time Polymerase Chain Reaction

    7) Product Images from "Thiamine deficiency activates hypoxia inducible factor-1α to facilitate pro-apoptotic responses in mouse primary astrocytes"

    Article Title: Thiamine deficiency activates hypoxia inducible factor-1α to facilitate pro-apoptotic responses in mouse primary astrocytes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0186707

    Effect of thiamine deficiency on expression of pro-apoptotic HIF-1α target genes. Primary astrocytes were treated with 10μM pyrithiamine up to 14d to induce thiamine deficiency compared to 3μM thiamine control (CTL). A) Representative Western blots are shown for expression of MCP1, BNIP3, Nix and Noxa in WCL. Actin was used as a loading control. B) Densitometry of mean protein expression +/- SD includes n = 3 independent replicates. C) Real time-PCR analysis of mRNA levels +/- SD of the HIF-1α target genes MCP1, BNIP3, Nix and Noxa. Data are normalized to Actin as a loading control and the control sample using the 2 -ΔΔCt method. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effect of thiamine deficiency on expression of pro-apoptotic HIF-1α target genes. Primary astrocytes were treated with 10μM pyrithiamine up to 14d to induce thiamine deficiency compared to 3μM thiamine control (CTL). A) Representative Western blots are shown for expression of MCP1, BNIP3, Nix and Noxa in WCL. Actin was used as a loading control. B) Densitometry of mean protein expression +/- SD includes n = 3 independent replicates. C) Real time-PCR analysis of mRNA levels +/- SD of the HIF-1α target genes MCP1, BNIP3, Nix and Noxa. Data are normalized to Actin as a loading control and the control sample using the 2 -ΔΔCt method. (★) Represents a statistically significant difference of p

    Techniques Used: Expressing, CTL Assay, Western Blot, Real-time Polymerase Chain Reaction

    Effects of thiamine repletion on the expression of HIF-1α regulated pro-apoptotic proteins. Primary astrocytes were treated with 10μM pyrithiamine treatment for 4d (PT). Subsequently, 3μM thiamine was repleted into the culturing media for up to 5d (5R). A) Representative Western blot of HIF-1α and the established target gene LDHA in WCL. Expression of the pro-apoptotic target genes MCP1, BNIP3, Nix and Noxa in WCL are also shown. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effects of thiamine repletion on the expression of HIF-1α regulated pro-apoptotic proteins. Primary astrocytes were treated with 10μM pyrithiamine treatment for 4d (PT). Subsequently, 3μM thiamine was repleted into the culturing media for up to 5d (5R). A) Representative Western blot of HIF-1α and the established target gene LDHA in WCL. Expression of the pro-apoptotic target genes MCP1, BNIP3, Nix and Noxa in WCL are also shown. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p

    Techniques Used: Expressing, Western Blot

    Schematic representation of the hypothesized role of HIF-1α in alcohol-induced neurological damage. The poor diet of chronic alcohol consumers and subsequent loss of intestinal thiamine transport contributes to TD in these patients. We have demonstrated that TD induces HIF-1α signaling and pro-apoptotic/inflammatory HIF-1α target genes such as MCP1, BNIP3, Nix and Noxa in astrocytes. Independent of TD, ethanol metab olism by CYP2E1 leads to an increase in oxygen consumption resulting in the development of a hypoxic microenvironment and an increase in ROS. In astrocytes, this may also lead to stabilization of HIF-1α and subsequent cellular death. Overall, this would suggest that apoptosis in either uncomplicated alcoholism or in conjunction with TD is mediated by a HIF-1α response to induce pro-apoptotic/inflammatory signaling, as observed in ischemic disease.
    Figure Legend Snippet: Schematic representation of the hypothesized role of HIF-1α in alcohol-induced neurological damage. The poor diet of chronic alcohol consumers and subsequent loss of intestinal thiamine transport contributes to TD in these patients. We have demonstrated that TD induces HIF-1α signaling and pro-apoptotic/inflammatory HIF-1α target genes such as MCP1, BNIP3, Nix and Noxa in astrocytes. Independent of TD, ethanol metab olism by CYP2E1 leads to an increase in oxygen consumption resulting in the development of a hypoxic microenvironment and an increase in ROS. In astrocytes, this may also lead to stabilization of HIF-1α and subsequent cellular death. Overall, this would suggest that apoptosis in either uncomplicated alcoholism or in conjunction with TD is mediated by a HIF-1α response to induce pro-apoptotic/inflammatory signaling, as observed in ischemic disease.

    Techniques Used:

    Effect of HIF-1α inhibition on expression of pro-apoptotic proteins. To achieve pharmacological inhibition of HIF-1α, 10μM YC1 was supplemented into PT containing media after a loading dose of 20μM for 24h. YC1 +/- pyrithiamine treatments lasted a total of 4d. A) WCL was assessed for expression of HIF-1α, LDHA, MCP1, BNIP3, Nix and Noxa. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effect of HIF-1α inhibition on expression of pro-apoptotic proteins. To achieve pharmacological inhibition of HIF-1α, 10μM YC1 was supplemented into PT containing media after a loading dose of 20μM for 24h. YC1 +/- pyrithiamine treatments lasted a total of 4d. A) WCL was assessed for expression of HIF-1α, LDHA, MCP1, BNIP3, Nix and Noxa. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p

    Techniques Used: Inhibition, Expressing

    8) Product Images from "9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages"

    Article Title: 9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages

    Journal: Nutrients

    doi: 10.3390/nu8070435

    9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p
    Figure Legend Snippet: 9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    9) Product Images from "Dietary β-Carotene Rescues Vitamin A Deficiency and Inhibits Atherogenesis in Apolipoprotein E-Deficient Mice"

    Article Title: Dietary β-Carotene Rescues Vitamin A Deficiency and Inhibits Atherogenesis in Apolipoprotein E-Deficient Mice

    Journal: Nutrients

    doi: 10.3390/nu12061625

    Liver gene expression of CYP26A1 ( A ) CYP26B1 ( B ) and LDL R ( C ) in apoE −/− mice, fed with VAD diet, VA, BC or BC+VA. Liver mRNA levels of the indicated genes were detected by real-time PCR. GAPDH was used as a reference gene. Data are means ±SE, n = 5–8 in each group. Mean values (a,b) not sharing a common superscript were significantly different by one-way ANOVA and Tukey post-hoc test comparison ( p
    Figure Legend Snippet: Liver gene expression of CYP26A1 ( A ) CYP26B1 ( B ) and LDL R ( C ) in apoE −/− mice, fed with VAD diet, VA, BC or BC+VA. Liver mRNA levels of the indicated genes were detected by real-time PCR. GAPDH was used as a reference gene. Data are means ±SE, n = 5–8 in each group. Mean values (a,b) not sharing a common superscript were significantly different by one-way ANOVA and Tukey post-hoc test comparison ( p

    Techniques Used: Expressing, Mouse Assay, Real-time Polymerase Chain Reaction

    10) Product Images from "The adaptive regulation of thiamine pyrophosphokinase-1 facilitates malignant growth during supplemental thiamine conditions"

    Article Title: The adaptive regulation of thiamine pyrophosphokinase-1 facilitates malignant growth during supplemental thiamine conditions

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26259

    Altered TPP homeostasis during hypoxic stress ( A ) HPLC analysis demonstrating ex vitro TPP production as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 5 independent experiments. ( B ) HPLC analysis demonstrating intracellular TPP levels as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 3 independent experiments. ( C , D ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells seeded at 25,000 cells/cm 2 and pretreated with 500 μM NaF, 100 μM MTX, 500 μM TRLX or 10 μM MitoQ for 12 h prior to hypoxic exposure for 24 h with sustained exposure to each compound including n = 5 independent experiments. ( E ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells exposed to 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 24 h including n = 3 independent experiments for 10 nM and n = 7 independent experiments for 3 μM. ( F ) Effect of thiamine dose on hypoxia-induced ROS levels demonstrated by hypoxic to normoxic fold change in MitoSOX median fluorescence intensity ± SD in wild type HCT 116 cultured in 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 48 h including n = 3 independent experiments. ( G ) Effect of thiamine dose on hypoxic tumor cell proliferation demonstrated by hypoxic to normoxic fold change in live cell count ± SD determined by trypan blue exclusion. Wild type HCT 116 cells were seeded at 500 cells/cm 2 were grown for 5 d in either 1% O 2 or normoxia including n = 5 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Altered TPP homeostasis during hypoxic stress ( A ) HPLC analysis demonstrating ex vitro TPP production as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 5 independent experiments. ( B ) HPLC analysis demonstrating intracellular TPP levels as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 3 independent experiments. ( C , D ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells seeded at 25,000 cells/cm 2 and pretreated with 500 μM NaF, 100 μM MTX, 500 μM TRLX or 10 μM MitoQ for 12 h prior to hypoxic exposure for 24 h with sustained exposure to each compound including n = 5 independent experiments. ( E ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells exposed to 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 24 h including n = 3 independent experiments for 10 nM and n = 7 independent experiments for 3 μM. ( F ) Effect of thiamine dose on hypoxia-induced ROS levels demonstrated by hypoxic to normoxic fold change in MitoSOX median fluorescence intensity ± SD in wild type HCT 116 cultured in 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 48 h including n = 3 independent experiments. ( G ) Effect of thiamine dose on hypoxic tumor cell proliferation demonstrated by hypoxic to normoxic fold change in live cell count ± SD determined by trypan blue exclusion. Wild type HCT 116 cells were seeded at 500 cells/cm 2 were grown for 5 d in either 1% O 2 or normoxia including n = 5 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: High Performance Liquid Chromatography, Cell Culture, Fluorescence, Cell Counting

    Attenuation of TPK1 expression using pharmacological inhibition of HIF-1α and reoxygenation ( A ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression under normoxic (N) and hypoxic conditions ± YC-1 in WCLs isolated from wild type HCT 116 cells seeded at 2500 cells/cm 2 and pre-treated with 5 μM YC-1 for 24 h prior to 48 h hypoxic exposure in the presence of 5 μM YC-1. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 in the presence or absence of YC-1 for wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 3 independent experiments. ( C ) Representative Western blots demonstrating HIF-1α and TPK1 in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated in 1% O 2 for 48 h with subsequent reoxygenation at 21% O 2 for 4 and 24 h. ( D ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 and subsequent reoxygenation in wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 4 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Attenuation of TPK1 expression using pharmacological inhibition of HIF-1α and reoxygenation ( A ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression under normoxic (N) and hypoxic conditions ± YC-1 in WCLs isolated from wild type HCT 116 cells seeded at 2500 cells/cm 2 and pre-treated with 5 μM YC-1 for 24 h prior to 48 h hypoxic exposure in the presence of 5 μM YC-1. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 in the presence or absence of YC-1 for wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 3 independent experiments. ( C ) Representative Western blots demonstrating HIF-1α and TPK1 in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated in 1% O 2 for 48 h with subsequent reoxygenation at 21% O 2 for 4 and 24 h. ( D ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 and subsequent reoxygenation in wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 4 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Expressing, Inhibition, Western Blot, Isolation

    Oxidative stress mediated regulation of TPK1 ( A ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from isogenic wild type and HIF-1α –/– HCT 116 cells. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 compared to wild type HCT 116 cells including n = 5 independent experiments. ( C ) Fold change in CM-H2DCFDA median fluorescence intensity ± SD demonstrating fold change in ROS levels between HIF-1α –/– relative to wild type HCT 116 cells including n = 4 independent experiments. ( D ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1 mM NAC or 100 μM ASC for 24 and 48 h relative to untreated HIF-1α –/– HCT 116 CTL (expression of TPK1 in wild type cells provided for comparison). ( E ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 cells treated with NAC and ASC compared to untreated HIF-1α –/– HCT 116 control including n = 4 independent experiments. ( F ) Representative Western blots demonstrating HIF-1α and TPK1 protein expression in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1% O 2 , 0.1 μM DOX, 10 μM CDDP, 5 μM AA or 10 μM TBHP for 24 h relative to normoxic control (N). ( G ) Densitometry analysis of the fold change in TPK1 expression ± SD for wild type HCT 116 cells treated with 1% O 2 , DOX, CDDP, AA or TBHP compared to untreated normoxic control (N) including n = 6 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Oxidative stress mediated regulation of TPK1 ( A ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from isogenic wild type and HIF-1α –/– HCT 116 cells. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 compared to wild type HCT 116 cells including n = 5 independent experiments. ( C ) Fold change in CM-H2DCFDA median fluorescence intensity ± SD demonstrating fold change in ROS levels between HIF-1α –/– relative to wild type HCT 116 cells including n = 4 independent experiments. ( D ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1 mM NAC or 100 μM ASC for 24 and 48 h relative to untreated HIF-1α –/– HCT 116 CTL (expression of TPK1 in wild type cells provided for comparison). ( E ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 cells treated with NAC and ASC compared to untreated HIF-1α –/– HCT 116 control including n = 4 independent experiments. ( F ) Representative Western blots demonstrating HIF-1α and TPK1 protein expression in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1% O 2 , 0.1 μM DOX, 10 μM CDDP, 5 μM AA or 10 μM TBHP for 24 h relative to normoxic control (N). ( G ) Densitometry analysis of the fold change in TPK1 expression ± SD for wild type HCT 116 cells treated with 1% O 2 , DOX, CDDP, AA or TBHP compared to untreated normoxic control (N) including n = 6 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Western Blot, Expressing, Isolation, Fluorescence, CTL Assay

    Effect of hypoxic stress and HIF-1α on TPK1 expression ( A ) Representative Western blots demonstrating TPK1 protein expression in WCLs isolated from seven tumor cell lines with tissue origins including breast (MCF7, MDA-MB-231), brain (LN-18, U-87 MG), and intestine (Caco-2, HCT 116, HuTu 80) following treatment with 1% O 2 for 24, 48, and 72 h relative to normoxic control (N). β-Actin expression serves as the loading control. ( B ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 150 μM DMOG or 1% O 2 for 24 h relative to normoxic control (N). ( C , D ) Densitometry analysis of the fold change in TPK1 expression ± standard deviation (SD) following DMOG and 1% O 2 treatment in wildtype and HIF-1α –/– HCT 116 cells compared to normoxic control (N) including n = 4 independent experiments for wild type and n = 3 independent experiments in HIF-1α –/– cells. ( E ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 2500 cells/cm 2 and transfected with 2.5 μg of HIF-1α CA plasmid DNA relative to vector control (VCTR) for 72 h. ( F , G ) Densitometry analysis of the fold change in TPK1 expression ± SD following HIF-1α CA overexpression in wildtype and HIF-1α –/– HCT 116 cells compared to vector control including n = 3 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Effect of hypoxic stress and HIF-1α on TPK1 expression ( A ) Representative Western blots demonstrating TPK1 protein expression in WCLs isolated from seven tumor cell lines with tissue origins including breast (MCF7, MDA-MB-231), brain (LN-18, U-87 MG), and intestine (Caco-2, HCT 116, HuTu 80) following treatment with 1% O 2 for 24, 48, and 72 h relative to normoxic control (N). β-Actin expression serves as the loading control. ( B ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 150 μM DMOG or 1% O 2 for 24 h relative to normoxic control (N). ( C , D ) Densitometry analysis of the fold change in TPK1 expression ± standard deviation (SD) following DMOG and 1% O 2 treatment in wildtype and HIF-1α –/– HCT 116 cells compared to normoxic control (N) including n = 4 independent experiments for wild type and n = 3 independent experiments in HIF-1α –/– cells. ( E ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 2500 cells/cm 2 and transfected with 2.5 μg of HIF-1α CA plasmid DNA relative to vector control (VCTR) for 72 h. ( F , G ) Densitometry analysis of the fold change in TPK1 expression ± SD following HIF-1α CA overexpression in wildtype and HIF-1α –/– HCT 116 cells compared to vector control including n = 3 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Expressing, Western Blot, Isolation, Multiple Displacement Amplification, Standard Deviation, Transfection, Plasmid Preparation, Over Expression

    11) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    12) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    13) Product Images from "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151"

    Article Title: Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022529

    Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).
    Figure Legend Snippet: Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).

    Techniques Used: Binding Assay

    Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.
    Figure Legend Snippet: Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.

    Techniques Used: Binding Assay, Sequencing

    Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).
    Figure Legend Snippet: Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).

    Techniques Used:

    14) Product Images from "9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages"

    Article Title: 9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages

    Journal: Nutrients

    doi: 10.3390/nu8070435

    9- cis -βc induced macrophage cytochrome P450 26B1 (CYP26B1) expression. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. The expression of CYP26B1 mRNA was measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. Different letters represent significant differences between treatments, p
    Figure Legend Snippet: 9- cis -βc induced macrophage cytochrome P450 26B1 (CYP26B1) expression. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. The expression of CYP26B1 mRNA was measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. Different letters represent significant differences between treatments, p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    15) Product Images from "Vitamin A-Deficient Diet Accelerated Atherogenesis in Apolipoprotein E−/− Mice and Dietary β-Carotene Prevents This Consequence"

    Article Title: Vitamin A-Deficient Diet Accelerated Atherogenesis in Apolipoprotein E−/− Mice and Dietary β-Carotene Prevents This Consequence

    Journal: BioMed Research International

    doi: 10.1155/2015/758723

    Liver gene expression in apoE −/− mice fed chow or vitamin A-deficient diet with or without β- carotene. Liver mRNA levels of the indicated genes were detected by real-time PCR. Gapdh was used as a reference gene. Gene expression was detected after 15 weeks of treatment. Cyp26a1 (a), Pparγ (b), Cyp7α (c), and Hmgr (d). Measured by real-time PCR and normalized to GAPDH. Values are means ± SE, n = 8. a, b, c Within each graph, means without a common letter differ, P
    Figure Legend Snippet: Liver gene expression in apoE −/− mice fed chow or vitamin A-deficient diet with or without β- carotene. Liver mRNA levels of the indicated genes were detected by real-time PCR. Gapdh was used as a reference gene. Gene expression was detected after 15 weeks of treatment. Cyp26a1 (a), Pparγ (b), Cyp7α (c), and Hmgr (d). Measured by real-time PCR and normalized to GAPDH. Values are means ± SE, n = 8. a, b, c Within each graph, means without a common letter differ, P

    Techniques Used: Expressing, Mouse Assay, Real-time Polymerase Chain Reaction

    16) Product Images from "Non-Circadian Expression Masking Clock-Driven Weak Transcription Rhythms in U2OS Cells"

    Article Title: Non-Circadian Expression Masking Clock-Driven Weak Transcription Rhythms in U2OS Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0102238

    Expression analysis of genes with CRBSs in their promoters. ( A ) UCSC browser views of BMAL1 (top), CLOCK (middle) and CRY1 (bottom) occupancy at the promoters of ATG3 , EIF5A2 , and SCN5A . Binding sites of the individual transcription regulators are indicated by colored bars. Black bars indicate common binding sites of the three regulators. ( B ) Temporal expression profiles (microarray analysis) of ATG3 , EIF5A2 , and SCN5A , which have strong CRBSs in their promoters. ( C, D ) Around the clock qRT-PCR analysis of preRNA ( C ) and mRNA ( D ) levels of ATG3 , EIF5A2 , and SCN5A . qRT-PCR analysis was carried out with intron- and exon-specific probes, respectively, of ATG3 , EIF5A2, and SCN5A using RNA of time courses A and B. Expression levels of HPRT1 were used for normalization.
    Figure Legend Snippet: Expression analysis of genes with CRBSs in their promoters. ( A ) UCSC browser views of BMAL1 (top), CLOCK (middle) and CRY1 (bottom) occupancy at the promoters of ATG3 , EIF5A2 , and SCN5A . Binding sites of the individual transcription regulators are indicated by colored bars. Black bars indicate common binding sites of the three regulators. ( B ) Temporal expression profiles (microarray analysis) of ATG3 , EIF5A2 , and SCN5A , which have strong CRBSs in their promoters. ( C, D ) Around the clock qRT-PCR analysis of preRNA ( C ) and mRNA ( D ) levels of ATG3 , EIF5A2 , and SCN5A . qRT-PCR analysis was carried out with intron- and exon-specific probes, respectively, of ATG3 , EIF5A2, and SCN5A using RNA of time courses A and B. Expression levels of HPRT1 were used for normalization.

    Techniques Used: Expressing, Binding Assay, Microarray, Quantitative RT-PCR

    17) Product Images from "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151"

    Article Title: Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022529

    Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).
    Figure Legend Snippet: Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).

    Techniques Used: Binding Assay

    Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.
    Figure Legend Snippet: Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.

    Techniques Used: Binding Assay, Sequencing

    Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).
    Figure Legend Snippet: Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).

    Techniques Used:

    18) Product Images from "ERK5 Activation Is Essential for Osteoclast Differentiation"

    Article Title: ERK5 Activation Is Essential for Osteoclast Differentiation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0125054

    The induction of c-Fos was blocked by inhibition of the ERK5 pathway. (A) 4B12 cells (2.5 × 10 4 ) were cultured with M-CSF (10 ng/ml) alone (M) or with M-CSF (10 ng/ml) and sRANKL (10 ng/ml) (MR). After the indicated times, c-Fos gene expression was measured by qRT-PCR. (B, C) 4B12 cells (2.5 × 10 4 ) were pretreated with or without BIX02189 or XMD8-92 for 6 hrs and then cultured in the presence of M-CSF (10 ng/ml) for 24 hrs. The expression of c-Fos was measured by qRT-PCR and Western blot analysis. Similar results were obtained in two independent experiments.
    Figure Legend Snippet: The induction of c-Fos was blocked by inhibition of the ERK5 pathway. (A) 4B12 cells (2.5 × 10 4 ) were cultured with M-CSF (10 ng/ml) alone (M) or with M-CSF (10 ng/ml) and sRANKL (10 ng/ml) (MR). After the indicated times, c-Fos gene expression was measured by qRT-PCR. (B, C) 4B12 cells (2.5 × 10 4 ) were pretreated with or without BIX02189 or XMD8-92 for 6 hrs and then cultured in the presence of M-CSF (10 ng/ml) for 24 hrs. The expression of c-Fos was measured by qRT-PCR and Western blot analysis. Similar results were obtained in two independent experiments.

    Techniques Used: Inhibition, Cell Culture, Expressing, Quantitative RT-PCR, Western Blot

    MEK5 siRNA inhibited the formation of TRAP (+) MNCs in 4B12 cells. (A) 4B12 cells were transfected with GFP siRNA or MEK5 siRNA. The 4B12 cells (2.5 × 10 4 ) were cultured in the presence of M-CSF (10 ng/ml) and sRANKL (20 ng/ml). After 3 days, MEK5 gene expression was measured by qRT-PCR. Similar results were obtained in two independent experiments. * P
    Figure Legend Snippet: MEK5 siRNA inhibited the formation of TRAP (+) MNCs in 4B12 cells. (A) 4B12 cells were transfected with GFP siRNA or MEK5 siRNA. The 4B12 cells (2.5 × 10 4 ) were cultured in the presence of M-CSF (10 ng/ml) and sRANKL (20 ng/ml). After 3 days, MEK5 gene expression was measured by qRT-PCR. Similar results were obtained in two independent experiments. * P

    Techniques Used: Transfection, Cell Culture, Expressing, Quantitative RT-PCR

    The induction of c-Fos in RAW264.7D clone cells was inhibited by BIX02189 or XMD8-92. (A) RAW264.7D clone cells (2.5 × 10 4 ) were cultured in the presence of sRANKL (50 ng/ml) with or without BIX02189 or XMD8-92. After 20 hrs, c-Fos gene expression was measured by qRT-PCR. Similar results were obtained in two independent experiments. * P
    Figure Legend Snippet: The induction of c-Fos in RAW264.7D clone cells was inhibited by BIX02189 or XMD8-92. (A) RAW264.7D clone cells (2.5 × 10 4 ) were cultured in the presence of sRANKL (50 ng/ml) with or without BIX02189 or XMD8-92. After 20 hrs, c-Fos gene expression was measured by qRT-PCR. Similar results were obtained in two independent experiments. * P

    Techniques Used: Cell Culture, Expressing, Quantitative RT-PCR

    19) Product Images from "Thiamine deficiency activates hypoxia inducible factor-1α to facilitate pro-apoptotic responses in mouse primary astrocytes"

    Article Title: Thiamine deficiency activates hypoxia inducible factor-1α to facilitate pro-apoptotic responses in mouse primary astrocytes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0186707

    Effect of thiamine deficiency on expression of pro-apoptotic HIF-1α target genes. Primary astrocytes were treated with 10μM pyrithiamine up to 14d to induce thiamine deficiency compared to 3μM thiamine control (CTL). A) Representative Western blots are shown for expression of MCP1, BNIP3, Nix and Noxa in WCL. Actin was used as a loading control. B) Densitometry of mean protein expression +/- SD includes n = 3 independent replicates. C) Real time-PCR analysis of mRNA levels +/- SD of the HIF-1α target genes MCP1, BNIP3, Nix and Noxa. Data are normalized to Actin as a loading control and the control sample using the 2 -ΔΔCt method. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effect of thiamine deficiency on expression of pro-apoptotic HIF-1α target genes. Primary astrocytes were treated with 10μM pyrithiamine up to 14d to induce thiamine deficiency compared to 3μM thiamine control (CTL). A) Representative Western blots are shown for expression of MCP1, BNIP3, Nix and Noxa in WCL. Actin was used as a loading control. B) Densitometry of mean protein expression +/- SD includes n = 3 independent replicates. C) Real time-PCR analysis of mRNA levels +/- SD of the HIF-1α target genes MCP1, BNIP3, Nix and Noxa. Data are normalized to Actin as a loading control and the control sample using the 2 -ΔΔCt method. (★) Represents a statistically significant difference of p

    Techniques Used: Expressing, CTL Assay, Western Blot, Real-time Polymerase Chain Reaction

    TD associated pro-apoptotic protein expression is reduced following inhibition of HIF-1α. Representative Western blots of cleaved Caspase-3 and cleaved Parp in WCL after A) treatment with 10μM pyrithiamine (PT) up to 14d, C) treatment with 10μM pyrithiamine for 4d with YC1 or E) treatment with 10μM pyrithiamine for 4d followed by 3μM thiamine repletion up to 5d (5R). Densitometry of mean protein expression +/- SD of each treatment set is shown with Actin as a loading control (B, D, F). (★) Represents a statistically significant difference of p
    Figure Legend Snippet: TD associated pro-apoptotic protein expression is reduced following inhibition of HIF-1α. Representative Western blots of cleaved Caspase-3 and cleaved Parp in WCL after A) treatment with 10μM pyrithiamine (PT) up to 14d, C) treatment with 10μM pyrithiamine for 4d with YC1 or E) treatment with 10μM pyrithiamine for 4d followed by 3μM thiamine repletion up to 5d (5R). Densitometry of mean protein expression +/- SD of each treatment set is shown with Actin as a loading control (B, D, F). (★) Represents a statistically significant difference of p

    Techniques Used: Expressing, Inhibition, Western Blot

    Effects of thiamine repletion on the expression of HIF-1α regulated pro-apoptotic proteins. Primary astrocytes were treated with 10μM pyrithiamine treatment for 4d (PT). Subsequently, 3μM thiamine was repleted into the culturing media for up to 5d (5R). A) Representative Western blot of HIF-1α and the established target gene LDHA in WCL. Expression of the pro-apoptotic target genes MCP1, BNIP3, Nix and Noxa in WCL are also shown. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effects of thiamine repletion on the expression of HIF-1α regulated pro-apoptotic proteins. Primary astrocytes were treated with 10μM pyrithiamine treatment for 4d (PT). Subsequently, 3μM thiamine was repleted into the culturing media for up to 5d (5R). A) Representative Western blot of HIF-1α and the established target gene LDHA in WCL. Expression of the pro-apoptotic target genes MCP1, BNIP3, Nix and Noxa in WCL are also shown. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p

    Techniques Used: Expressing, Western Blot

    Schematic representation of the hypothesized role of HIF-1α in alcohol-induced neurological damage. The poor diet of chronic alcohol consumers and subsequent loss of intestinal thiamine transport contributes to TD in these patients. We have demonstrated that TD induces HIF-1α signaling and pro-apoptotic/inflammatory HIF-1α target genes such as MCP1, BNIP3, Nix and Noxa in astrocytes. Independent of TD, ethanol metab olism by CYP2E1 leads to an increase in oxygen consumption resulting in the development of a hypoxic microenvironment and an increase in ROS. In astrocytes, this may also lead to stabilization of HIF-1α and subsequent cellular death. Overall, this would suggest that apoptosis in either uncomplicated alcoholism or in conjunction with TD is mediated by a HIF-1α response to induce pro-apoptotic/inflammatory signaling, as observed in ischemic disease.
    Figure Legend Snippet: Schematic representation of the hypothesized role of HIF-1α in alcohol-induced neurological damage. The poor diet of chronic alcohol consumers and subsequent loss of intestinal thiamine transport contributes to TD in these patients. We have demonstrated that TD induces HIF-1α signaling and pro-apoptotic/inflammatory HIF-1α target genes such as MCP1, BNIP3, Nix and Noxa in astrocytes. Independent of TD, ethanol metab olism by CYP2E1 leads to an increase in oxygen consumption resulting in the development of a hypoxic microenvironment and an increase in ROS. In astrocytes, this may also lead to stabilization of HIF-1α and subsequent cellular death. Overall, this would suggest that apoptosis in either uncomplicated alcoholism or in conjunction with TD is mediated by a HIF-1α response to induce pro-apoptotic/inflammatory signaling, as observed in ischemic disease.

    Techniques Used:

    Effect of HIF-1α inhibition on expression of pro-apoptotic proteins. To achieve pharmacological inhibition of HIF-1α, 10μM YC1 was supplemented into PT containing media after a loading dose of 20μM for 24h. YC1 +/- pyrithiamine treatments lasted a total of 4d. A) WCL was assessed for expression of HIF-1α, LDHA, MCP1, BNIP3, Nix and Noxa. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: Effect of HIF-1α inhibition on expression of pro-apoptotic proteins. To achieve pharmacological inhibition of HIF-1α, 10μM YC1 was supplemented into PT containing media after a loading dose of 20μM for 24h. YC1 +/- pyrithiamine treatments lasted a total of 4d. A) WCL was assessed for expression of HIF-1α, LDHA, MCP1, BNIP3, Nix and Noxa. B) Densitometry of mean protein expression +/- SD is included with Actin as a loading control. (★) Represents a statistically significant difference of p

    Techniques Used: Inhibition, Expressing

    HIF-1α activation in mouse primary astrocytes. Cells were treated with 10μM pyrithiamine (PT) up to 14d to induce thiamine deficiency relative to 3μM thiamine control (CTL). Representative Western blots are shown for expression of HIF-1α in WCL (A) and nuclear lysates (C). Actin was used as a loading control for WCL while p84 was used for nuclear samples. Densitometry of mean protein expression +/- SD includes n = 3 independent experiments for (B) WCL and (D) nuclear lysates. E) Real time-PCR analysis of mRNA expression +/- SD of the established HIF-1α target genes LDHA, GLUT1 and VEGF. Data are normalized to Actin as a loading control and the control sample using the 2- ΔΔCt method. (★) Represents a statistically significant difference of p
    Figure Legend Snippet: HIF-1α activation in mouse primary astrocytes. Cells were treated with 10μM pyrithiamine (PT) up to 14d to induce thiamine deficiency relative to 3μM thiamine control (CTL). Representative Western blots are shown for expression of HIF-1α in WCL (A) and nuclear lysates (C). Actin was used as a loading control for WCL while p84 was used for nuclear samples. Densitometry of mean protein expression +/- SD includes n = 3 independent experiments for (B) WCL and (D) nuclear lysates. E) Real time-PCR analysis of mRNA expression +/- SD of the established HIF-1α target genes LDHA, GLUT1 and VEGF. Data are normalized to Actin as a loading control and the control sample using the 2- ΔΔCt method. (★) Represents a statistically significant difference of p

    Techniques Used: Activation Assay, CTL Assay, Western Blot, Expressing, Real-time Polymerase Chain Reaction

    TD associated apoptosis is reduced following HIF-1α inhibition. Primary astrocytes were treated with 10μM pyrithiamine (10μM PT) for 4d, 10μM pyrithiamine for 4d with YC1 (10μM PT+YC1) or treatment with 10μM pyrithiamine for 4d followed by 3μM thiamine repletion for 2d (10μM PT+2R). Representative plots of TUNEL assay analyzed by flow cytometry (A) with a quantitative summary of n = 3 independent replicates +/- SD (B). C) Representative microscopy images of TUNEL assay performed on fixed cells are shown after treatment with PT for 4d, PT + YC1 for 4d or PT for 4d with 2d of repletion. D) N = 3 independent replicates of the Cell death ELISA +/- SD. E) Representative plots of PI/ Annexin V staining analyzed by flow cytometry with a summary of n = 3 independent replicates +/- SD (F). (★) Represents a statistically significant difference of p
    Figure Legend Snippet: TD associated apoptosis is reduced following HIF-1α inhibition. Primary astrocytes were treated with 10μM pyrithiamine (10μM PT) for 4d, 10μM pyrithiamine for 4d with YC1 (10μM PT+YC1) or treatment with 10μM pyrithiamine for 4d followed by 3μM thiamine repletion for 2d (10μM PT+2R). Representative plots of TUNEL assay analyzed by flow cytometry (A) with a quantitative summary of n = 3 independent replicates +/- SD (B). C) Representative microscopy images of TUNEL assay performed on fixed cells are shown after treatment with PT for 4d, PT + YC1 for 4d or PT for 4d with 2d of repletion. D) N = 3 independent replicates of the Cell death ELISA +/- SD. E) Representative plots of PI/ Annexin V staining analyzed by flow cytometry with a summary of n = 3 independent replicates +/- SD (F). (★) Represents a statistically significant difference of p

    Techniques Used: Inhibition, TUNEL Assay, Flow Cytometry, Cytometry, Microscopy, Enzyme-linked Immunosorbent Assay, Staining

    20) Product Images from "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151"

    Article Title: Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022529

    Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).
    Figure Legend Snippet: Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).

    Techniques Used: Binding Assay

    Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.
    Figure Legend Snippet: Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.

    Techniques Used: Binding Assay, Sequencing

    Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).
    Figure Legend Snippet: Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).

    Techniques Used:

    21) Product Images from "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151"

    Article Title: Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022529

    Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).
    Figure Legend Snippet: Characteristic features of the long control region (LCR) of HPV-150 and HPV-151, showing genomic locations of E2 binding sites (ACC-N 5-7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T).

    Techniques Used: Binding Assay

    Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.
    Figure Legend Snippet: Amino acid alignment of HPV-150 and HPV-151 E6 and E7 proteins with corresponding proteins of closely related genotypes from Betapapillomavirus species 2, 4 and 5. The locations of zinc-binding domains (CxxC(x) 29 CxxC) are indicated by black boxes, and the location of the pRb-binding core sequence (LxCxE) is indicated with a blue box.

    Techniques Used: Binding Assay, Sequencing

    Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).
    Figure Legend Snippet: Genomic organization of HPV-150 and HPV-151 showing genomic positions of viral genes E6, E7, E1, E2, L1, L2, and the non-coding regions located between L1 and E6 (LCR); and E2 and L2 (dotted line).

    Techniques Used:

    22) Product Images from "Exon-Skipping Strategy by Ratio Modulation between Cytoprotective versus Pro-Apoptotic Clusterin Forms Increased Sensitivity of LNCaP to Cell Death"

    Article Title: Exon-Skipping Strategy by Ratio Modulation between Cytoprotective versus Pro-Apoptotic Clusterin Forms Increased Sensitivity of LNCaP to Cell Death

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0054920

    U7-nCLU vector construct and CLU mRNA expression in LNCaP. (A) (Top) Antisens sequence position to induce exon 2 skipping. (Bottom) Structure of the pHIV-1-U7-nCLU. U7snRNA including antisens sequence is placed under the control of its own promoter and its regulating domains 3′. SmOPT: sequence indicates the Sm protein binding site. LTR : long terminal repeats. (B) U7 vector integration in transduced LNCaP cell genome. Curves represent qPCR amplification of U7-nCLU genomic DNA in different transduction conditions (middle curves). Human β-actin amplification corresponded to positive control (Top curves) and genomic DNA of non transduced cells was used as negative control. (C) (Top) mRNA from transduced LNCaP cells with U7-nCLU vector was analyzed by RT-PCR at 3 weeks posttransduction. The 344 bp and 218 bp bands correspond to sCLU and skipped form nCLU mRNA respectively without alteration of the sequence. Controls were from RNA of LNCaP alone or LNCaP transduced with U7-control. (Bottom) Relative mRNA expression levels determined by densitometry. βactin used to normalize changes in specific gene expressions. (D) DNA sequence of the 218 bp band showed skipping of exon 2.
    Figure Legend Snippet: U7-nCLU vector construct and CLU mRNA expression in LNCaP. (A) (Top) Antisens sequence position to induce exon 2 skipping. (Bottom) Structure of the pHIV-1-U7-nCLU. U7snRNA including antisens sequence is placed under the control of its own promoter and its regulating domains 3′. SmOPT: sequence indicates the Sm protein binding site. LTR : long terminal repeats. (B) U7 vector integration in transduced LNCaP cell genome. Curves represent qPCR amplification of U7-nCLU genomic DNA in different transduction conditions (middle curves). Human β-actin amplification corresponded to positive control (Top curves) and genomic DNA of non transduced cells was used as negative control. (C) (Top) mRNA from transduced LNCaP cells with U7-nCLU vector was analyzed by RT-PCR at 3 weeks posttransduction. The 344 bp and 218 bp bands correspond to sCLU and skipped form nCLU mRNA respectively without alteration of the sequence. Controls were from RNA of LNCaP alone or LNCaP transduced with U7-control. (Bottom) Relative mRNA expression levels determined by densitometry. βactin used to normalize changes in specific gene expressions. (D) DNA sequence of the 218 bp band showed skipping of exon 2.

    Techniques Used: Plasmid Preparation, Construct, Expressing, Sequencing, Protein Binding, Real-time Polymerase Chain Reaction, Amplification, Transduction, Positive Control, Negative Control, Reverse Transcription Polymerase Chain Reaction

    23) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    Prenatal stress enhances the expression of surface markers: CD40 and C1q and protein level of Iba1 in the hippocampus (A) and the frontal cortex (B) in adult rats . The mRNA expression is presented as the average fold ± SD, n = 6 in each group, * p
    Figure Legend Snippet: Prenatal stress enhances the expression of surface markers: CD40 and C1q and protein level of Iba1 in the hippocampus (A) and the frontal cortex (B) in adult rats . The mRNA expression is presented as the average fold ± SD, n = 6 in each group, * p

    Techniques Used: Expressing

    Prenatal stress enhances the expression of: CD40 and MHC II markers in microglial cell cultures . The expression of mRNA is presented as average fold ± SD from 3 independent experiments ( n = 6 in each group), * p
    Figure Legend Snippet: Prenatal stress enhances the expression of: CD40 and MHC II markers in microglial cell cultures . The expression of mRNA is presented as average fold ± SD from 3 independent experiments ( n = 6 in each group), * p

    Techniques Used: Expressing

    24) Product Images from "Long-Term Preservation of Cones and Improvement in Visual Function Following Gene Therapy in a Mouse Model of Leber Congenital Amaurosis Caused by Guanylate Cyclase-1 Deficiency"

    Article Title: Long-Term Preservation of Cones and Improvement in Visual Function Following Gene Therapy in a Mouse Model of Leber Congenital Amaurosis Caused by Guanylate Cyclase-1 Deficiency

    Journal: Human Gene Therapy

    doi: 10.1089/hum.2011.069

    Restoration of cone-mediated optomotor behavior in Gucy2e –/– treated eyes. Shown is the photopic visual acuity and contrast sensitivity measurements in two untreated Gucy2e –/– mice (animals 1 and 2), and six mice treated with high-titer vector (animals 3–8) 4 months post treatment. Results are presented for each animal and averaged per group in the right-hand graphs. (a) Robust improvement in visual acuity was consistently observed in treated eyes ( p
    Figure Legend Snippet: Restoration of cone-mediated optomotor behavior in Gucy2e –/– treated eyes. Shown is the photopic visual acuity and contrast sensitivity measurements in two untreated Gucy2e –/– mice (animals 1 and 2), and six mice treated with high-titer vector (animals 3–8) 4 months post treatment. Results are presented for each animal and averaged per group in the right-hand graphs. (a) Robust improvement in visual acuity was consistently observed in treated eyes ( p

    Techniques Used: Mouse Assay, Plasmid Preparation

    Comparison of photoreceptor function restoration after transfer of human GUCY2D and mouse Gucy2e transgenes. (a) Consistent rod ERG improvement was observed in eyes treated with both vectors (mean±SD). No statistically significant difference was observed between the efficacy of rescue using both vectors ( p =0.587, two-way ANOVA). (b) Cone-mediated ERG b-wave responses of Gucy2e –/– eyes treated with the mouse transcript did not differ from those treated with the human transcript ( p =0.9887, two-way ANOVA). Cone-mediated ERG responses achieved with the mouse transcript were approximately 62% of the response seen in C57BL/6J wild-type eyes, compared with 65% achieved with the human transgene.
    Figure Legend Snippet: Comparison of photoreceptor function restoration after transfer of human GUCY2D and mouse Gucy2e transgenes. (a) Consistent rod ERG improvement was observed in eyes treated with both vectors (mean±SD). No statistically significant difference was observed between the efficacy of rescue using both vectors ( p =0.587, two-way ANOVA). (b) Cone-mediated ERG b-wave responses of Gucy2e –/– eyes treated with the mouse transcript did not differ from those treated with the human transcript ( p =0.9887, two-way ANOVA). Cone-mediated ERG responses achieved with the mouse transcript were approximately 62% of the response seen in C57BL/6J wild-type eyes, compared with 65% achieved with the human transgene.

    Techniques Used:

    GUCY2D transcript levels in Gucy2e –/– eyes treated with high-titer vector. Real-time RT-PCR analyses comparing levels of GUCY2D transcript in high-titer vector-treated Gucy2e –/– eyes with endogenous Gucy2e transcript in C57BL/6J wild-type eyes and untreated Gucy2e –/– eyes. The levels of introduced GUCY2D transcript in treated eyes are 30-fold higher than those seen in C57BL/6J wild-type control eyes ( p
    Figure Legend Snippet: GUCY2D transcript levels in Gucy2e –/– eyes treated with high-titer vector. Real-time RT-PCR analyses comparing levels of GUCY2D transcript in high-titer vector-treated Gucy2e –/– eyes with endogenous Gucy2e transcript in C57BL/6J wild-type eyes and untreated Gucy2e –/– eyes. The levels of introduced GUCY2D transcript in treated eyes are 30-fold higher than those seen in C57BL/6J wild-type control eyes ( p

    Techniques Used: Plasmid Preparation, Quantitative RT-PCR

    Correct size and localization of guanylate cyclase-1 (GC1) protein in treated Gucy2e –/– eyes. GC1 immunofluorescence (green) was detected in the outer segments of photoreceptor cells in (a) wild-type eyes and (b) Gucy2e –/– eyes treated with low-titer (LT) vector. (c) No staining was observed in untreated Gucy2e –/– eyes. 4′,6-Diamidino-2-phenylindole (DAPI) nuclear counterstaining is shown in blue. (d) Western blot showing 120-kDa GC1 protein in Gucy2e –/– eyes treated with low-titer (LT) or high-titer (HT) vector and in C57BL/6J wild-type controls, but not in Gucy2e –/–
    Figure Legend Snippet: Correct size and localization of guanylate cyclase-1 (GC1) protein in treated Gucy2e –/– eyes. GC1 immunofluorescence (green) was detected in the outer segments of photoreceptor cells in (a) wild-type eyes and (b) Gucy2e –/– eyes treated with low-titer (LT) vector. (c) No staining was observed in untreated Gucy2e –/– eyes. 4′,6-Diamidino-2-phenylindole (DAPI) nuclear counterstaining is shown in blue. (d) Western blot showing 120-kDa GC1 protein in Gucy2e –/– eyes treated with low-titer (LT) or high-titer (HT) vector and in C57BL/6J wild-type controls, but not in Gucy2e –/–

    Techniques Used: Immunofluorescence, Plasmid Preparation, Staining, Western Blot

    Cone α-transducin levels and localization are restored in Gucy2e –/– treated eyes. C57BL/6J wild-type, Gucy2e –/– eyes treated with low-titer (LT) vector and untreated (UT) retinas were stained with antibodies against cone α-transducin ( a , red) and cone arrestin ( b , green). (a) Restored cone α-transducin localization to the outer segments of cones in the treated eyes, comparable to wild-type eyes. The images in the first three columns were taken using the same microscope settings, whereas the images in the last column, designated as Gucy2e –/– UT*, are identical to those in the Gucy2e –/– UT column except that they were taken with a long exposure and lighting levels were manipulated in Adobe Photoshop 7.0 Elements to reveal the signal in the red channel. The results indicate substantially reduced levels of cone α-transducin in untreated Gucy2e –/– eyes, and restored levels in treated eyes. (b) The two left-hand columns are images of retinal sections of eyes harvested and processed under normal light conditions and the right-hand columns are images of those harvested and processed in the dark. In the light, cone arrestin is localized in the cone outer segments and synaptic regions of wild-type as well as treated and untreated Gucy2e –/– eyes. In the dark, cone arrestin is localized throughout the cone cells in wild-type eyes, and in treated and untreated Gucy2e –/–
    Figure Legend Snippet: Cone α-transducin levels and localization are restored in Gucy2e –/– treated eyes. C57BL/6J wild-type, Gucy2e –/– eyes treated with low-titer (LT) vector and untreated (UT) retinas were stained with antibodies against cone α-transducin ( a , red) and cone arrestin ( b , green). (a) Restored cone α-transducin localization to the outer segments of cones in the treated eyes, comparable to wild-type eyes. The images in the first three columns were taken using the same microscope settings, whereas the images in the last column, designated as Gucy2e –/– UT*, are identical to those in the Gucy2e –/– UT column except that they were taken with a long exposure and lighting levels were manipulated in Adobe Photoshop 7.0 Elements to reveal the signal in the red channel. The results indicate substantially reduced levels of cone α-transducin in untreated Gucy2e –/– eyes, and restored levels in treated eyes. (b) The two left-hand columns are images of retinal sections of eyes harvested and processed under normal light conditions and the right-hand columns are images of those harvested and processed in the dark. In the light, cone arrestin is localized in the cone outer segments and synaptic regions of wild-type as well as treated and untreated Gucy2e –/– eyes. In the dark, cone arrestin is localized throughout the cone cells in wild-type eyes, and in treated and untreated Gucy2e –/–

    Techniques Used: Plasmid Preparation, Staining, Microscopy

    Improvement in cone and rod function in treated Gucy2e –/– eyes. (a) Representative electroretinographic (ERG) traces from C57BL/6J wild-type mice, Gucy2e –/– mice 6 months after treatment with high-titer (HT) or low-titer (LT) vector, and untreated Gucy2e –/– (UT) mice. Rod-mediated b-wave responses of Gucy2e –/– animals treated with low-titer vector were no different from those of untreated eyes, whereas responses of animals treated with high-titer vector were restored to an average of 65% of wild-type amplitudes. Cone-mediated ERG of Gucy2e –/– animals treated with low-titer vector improved on average to 20% of wild-type amplitudes, whereas the responses of animals treated with high-titer vector were restored to 65% compared with wild-type eyes. (b) Over time, scotopic b-wave amplitudes in Gucy2e –/– mice treated with high-titer vector were significantly higher than those in untreated mice ( p =0.0005, two-way ANOVA). (c) Data from animals treated with low-titer vector were significantly different from those of untreated and wild-type eyes at all time points examined ( p
    Figure Legend Snippet: Improvement in cone and rod function in treated Gucy2e –/– eyes. (a) Representative electroretinographic (ERG) traces from C57BL/6J wild-type mice, Gucy2e –/– mice 6 months after treatment with high-titer (HT) or low-titer (LT) vector, and untreated Gucy2e –/– (UT) mice. Rod-mediated b-wave responses of Gucy2e –/– animals treated with low-titer vector were no different from those of untreated eyes, whereas responses of animals treated with high-titer vector were restored to an average of 65% of wild-type amplitudes. Cone-mediated ERG of Gucy2e –/– animals treated with low-titer vector improved on average to 20% of wild-type amplitudes, whereas the responses of animals treated with high-titer vector were restored to 65% compared with wild-type eyes. (b) Over time, scotopic b-wave amplitudes in Gucy2e –/– mice treated with high-titer vector were significantly higher than those in untreated mice ( p =0.0005, two-way ANOVA). (c) Data from animals treated with low-titer vector were significantly different from those of untreated and wild-type eyes at all time points examined ( p

    Techniques Used: Mouse Assay, Plasmid Preparation

    Cone preservation in the transduced areas of Gucy2e –/– treated eyes. Shown are adjoining retinal sections of Gucy2e –/– eyes 6 months post treatment with low-titer vector (a and b) and untreated contralateral eyes (c and d) stained with antibodies against GC1 (a and c , green ) and cone α-transducin (b and d , yellow ) . (e – l) Insets are images of corresponding regions outlined in (a) and (b) . In the areas where GC1 staining is evident in the treated eyes (e and g) there is also expression of cone α-transducin (f and h) . In the untransduced areas, where there is no GC1 (i and k) , there is no cone α-transducin staining (j and l) . (m and n) Images of the superior retina, and (o and p) of the inferior retina of the untreated eye (c and d) . There is no GC1 staining in the untreated eye (c) . Weak cone α-transducin staining is evident in the superior untreated retina (n) with few cone cells present in the inferior part of the retina (p) . Scale bars: (a) 500 μm; (e) 100 μm. (r) Number of cone cells determined by cone α-transducin staining in Gucy2e –/– eyes treated with low-titer vector, compared with untreated Gucy2e –/– eyes and C57BL/6J wild-type controls. The cone number in treated eyes was 20% higher than in untreated eyes ( p
    Figure Legend Snippet: Cone preservation in the transduced areas of Gucy2e –/– treated eyes. Shown are adjoining retinal sections of Gucy2e –/– eyes 6 months post treatment with low-titer vector (a and b) and untreated contralateral eyes (c and d) stained with antibodies against GC1 (a and c , green ) and cone α-transducin (b and d , yellow ) . (e – l) Insets are images of corresponding regions outlined in (a) and (b) . In the areas where GC1 staining is evident in the treated eyes (e and g) there is also expression of cone α-transducin (f and h) . In the untransduced areas, where there is no GC1 (i and k) , there is no cone α-transducin staining (j and l) . (m and n) Images of the superior retina, and (o and p) of the inferior retina of the untreated eye (c and d) . There is no GC1 staining in the untreated eye (c) . Weak cone α-transducin staining is evident in the superior untreated retina (n) with few cone cells present in the inferior part of the retina (p) . Scale bars: (a) 500 μm; (e) 100 μm. (r) Number of cone cells determined by cone α-transducin staining in Gucy2e –/– eyes treated with low-titer vector, compared with untreated Gucy2e –/– eyes and C57BL/6J wild-type controls. The cone number in treated eyes was 20% higher than in untreated eyes ( p

    Techniques Used: Preserving, Plasmid Preparation, Staining, Expressing

    25) Product Images from "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151"

    Article Title: Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150 and HPV-151

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022529

    A consensus phylogenetic tree of 200 PV based on nucleotide sequences of the L1 gene. Numbers at nodes show maximum likelihood bootstrap support (%) above 50.  Betapapillomavirus  species numbers are indicated above the corresponding genotypes.
    Figure Legend Snippet: A consensus phylogenetic tree of 200 PV based on nucleotide sequences of the L1 gene. Numbers at nodes show maximum likelihood bootstrap support (%) above 50. Betapapillomavirus species numbers are indicated above the corresponding genotypes.

    Techniques Used:

    26) Product Images from "9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages"

    Article Title: 9-cis β-Carotene Increased Cholesterol Efflux to HDL in Macrophages

    Journal: Nutrients

    doi: 10.3390/nu8070435

    9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p
    Figure Legend Snippet: 9- cis -βc-induced mRNA and protein expression levels of genes involved in cholesterol efflux in macrophages. RAW264.7 macrophage cells were treated for 24 h with vehicle (TWEEN 40), 2 µM of 9- cis -βc or all- trans -βc. ( A ) The expression of ABCA1, ABCG1, ABCG4, and APOE mRNA were measured by quantitate real-time PCR assays (TaqMan) standardized against GAPDH mRNA levels. The results are expressed as mean ± SE. of six independent experiments. * p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    27) Product Images from "9-Cis-Retinoic acid reduces ischemic brain injury in rodents via bone morphogenetic protein"

    Article Title: 9-Cis-Retinoic acid reduces ischemic brain injury in rodents via bone morphogenetic protein

    Journal: Journal of neuroscience research

    doi: 10.1002/jnr.21865

    9cRA increases BMP7 mRNA expression at 24 hours after injection. Cerebral cortex was harvested at 8 to 24 hours after i.c.v. of 9cRA or vehicle. Vehicle did not alter the expression of any BMP genes, measured by qRT-PCR. 9cRA-mediated changes in BMP mRNA
    Figure Legend Snippet: 9cRA increases BMP7 mRNA expression at 24 hours after injection. Cerebral cortex was harvested at 8 to 24 hours after i.c.v. of 9cRA or vehicle. Vehicle did not alter the expression of any BMP genes, measured by qRT-PCR. 9cRA-mediated changes in BMP mRNA

    Techniques Used: Expressing, Injection, Quantitative RT-PCR

    28) Product Images from "Identification of Cell Type-Specific Differences in Erythropoietin Receptor Signaling in Primary Erythroid and Lung Cancer Cells"

    Article Title: Identification of Cell Type-Specific Differences in Erythropoietin Receptor Signaling in Primary Erythroid and Lung Cancer Cells

    Journal: PLoS Computational Biology

    doi: 10.1371/journal.pcbi.1005049

    Experimental validation of the cell type-specific CISH and SOCS3 mRNA parameters. The parsimonious model was employed to predict the dynamics of CISH mRNA and SOCS3 mRNA upon treatment with a transcriptional inhibitor. The mRNA dynamics in CFU-E stimulated with 5 U/ml EPO alfa alone (black) or with transcriptional inhibition after 60 min (blue) was predicted. Additionally, the mRNA dynamics in H838-HA-hEPOR stimulated with 10 U/ml EPO beta alone (black) or with transcriptional inhibition after 30 min (blue) was predicted. Shadings surrounded by dotted lines depict uncertainty of the prediction. CFU-E cells were stimulated with 5 U/ml EPO alfa and either additionally treated with 1 μg/ml actinomycin D, to inhibit transcription, at 60 min (blue arrows) or left untreated. The H838-HA-hEPOR cells were either stimulated with 10 U/ml EPO beta alone (black) or additionally with 1 μg/ml actinomycin D at 30 min (blue arrows). The mRNA was extracted at the indicated time and the SOCS3 and CISH mRNA levels were measured with qRT-PCR. Experimental data are depicted as closed circles. The experiment was performed in triplicates and one representative example is shown.
    Figure Legend Snippet: Experimental validation of the cell type-specific CISH and SOCS3 mRNA parameters. The parsimonious model was employed to predict the dynamics of CISH mRNA and SOCS3 mRNA upon treatment with a transcriptional inhibitor. The mRNA dynamics in CFU-E stimulated with 5 U/ml EPO alfa alone (black) or with transcriptional inhibition after 60 min (blue) was predicted. Additionally, the mRNA dynamics in H838-HA-hEPOR stimulated with 10 U/ml EPO beta alone (black) or with transcriptional inhibition after 30 min (blue) was predicted. Shadings surrounded by dotted lines depict uncertainty of the prediction. CFU-E cells were stimulated with 5 U/ml EPO alfa and either additionally treated with 1 μg/ml actinomycin D, to inhibit transcription, at 60 min (blue arrows) or left untreated. The H838-HA-hEPOR cells were either stimulated with 10 U/ml EPO beta alone (black) or additionally with 1 μg/ml actinomycin D at 30 min (blue arrows). The mRNA was extracted at the indicated time and the SOCS3 and CISH mRNA levels were measured with qRT-PCR. Experimental data are depicted as closed circles. The experiment was performed in triplicates and one representative example is shown.

    Techniques Used: Chromogenic In Situ Hybridization, Inhibition, Quantitative RT-PCR

    Model selection. The model trajectories for a selection of key pathway components are shown for CFU-E, H838 and H838-HA-hEPOR cells. This includes expression of the EPOR targets CISH mRNA and SOCS3 mRNA measured by qRT-PCR as well as pEPOR, pJAK2 and cytoplasmic STAT5 data measured by quantitative immunoblotting. The amount of pSTAT5 was determined by either mass spectrometry or quantitative immunoblotting. The closed circles represent experimentally measured data in H838 and H838-HA-hEPOR cells. CFU-E data previously published [ 19 ] are shown as circles. The lines depict the three applied model strategies: dashed green (only cell type-specific parameters), dashed blue (no cell type-specific parameters) and solid red (parsimonious model, only relevant cell type-specific parameters). The parsimonious model describes the data similarly to the model with only cell type-specific parameters, whereas the trajectories of the model without cell type-specific parameters are not in line with the experimental data, e.g. for SOCS3 mRNA in CFU-E and for pSTAT5 in H838. All data sets, replicates and trajectories of the parsimonious model are shown in S8 and S9 Figs.
    Figure Legend Snippet: Model selection. The model trajectories for a selection of key pathway components are shown for CFU-E, H838 and H838-HA-hEPOR cells. This includes expression of the EPOR targets CISH mRNA and SOCS3 mRNA measured by qRT-PCR as well as pEPOR, pJAK2 and cytoplasmic STAT5 data measured by quantitative immunoblotting. The amount of pSTAT5 was determined by either mass spectrometry or quantitative immunoblotting. The closed circles represent experimentally measured data in H838 and H838-HA-hEPOR cells. CFU-E data previously published [ 19 ] are shown as circles. The lines depict the three applied model strategies: dashed green (only cell type-specific parameters), dashed blue (no cell type-specific parameters) and solid red (parsimonious model, only relevant cell type-specific parameters). The parsimonious model describes the data similarly to the model with only cell type-specific parameters, whereas the trajectories of the model without cell type-specific parameters are not in line with the experimental data, e.g. for SOCS3 mRNA in CFU-E and for pSTAT5 in H838. All data sets, replicates and trajectories of the parsimonious model are shown in S8 and S9 Figs.

    Techniques Used: Selection, Expressing, Chromogenic In Situ Hybridization, Quantitative RT-PCR, Mass Spectrometry

    29) Product Images from "Statins impair glucose uptake in human cells"

    Article Title: Statins impair glucose uptake in human cells

    Journal: BMJ Open Diabetes Research & Care

    doi: 10.1136/bmjdrc-2014-000017

    Human embryonic kidney (HEK293T) cells expressing mutated glucose transporter 1-flag gene (MUT-GLUT1-flag) uptake less glucose than their WT-GLUT1-flag counterparts. (A) Evaluation of GLUT1 and GLUT1-flag protein expression in total cellular lysates of two independent sets of parental (non-transduced) HEK293T cells, cells transduced with empty vector, WT-GLUT1-flag and MUT-GLUT1-flag with Western blotting. β-actin levels served as loading control. (B) Absolute quantification of GLUT1-flag and β-2-microglobulin (B2M) transcripts in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (C) Relative quantification of GLUT1-flag transcript in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (D) [1,2- 3 H]-deoxy-D-glucose (2-DOG) uptake in two independent sets of HEK293T cells transduced with empty vector, WT-GLUT-flag, or MUT-GLUT1-flag. The figure presents mean counts per minute (cpm) value±SD; *p
    Figure Legend Snippet: Human embryonic kidney (HEK293T) cells expressing mutated glucose transporter 1-flag gene (MUT-GLUT1-flag) uptake less glucose than their WT-GLUT1-flag counterparts. (A) Evaluation of GLUT1 and GLUT1-flag protein expression in total cellular lysates of two independent sets of parental (non-transduced) HEK293T cells, cells transduced with empty vector, WT-GLUT1-flag and MUT-GLUT1-flag with Western blotting. β-actin levels served as loading control. (B) Absolute quantification of GLUT1-flag and β-2-microglobulin (B2M) transcripts in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (C) Relative quantification of GLUT1-flag transcript in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (D) [1,2- 3 H]-deoxy-D-glucose (2-DOG) uptake in two independent sets of HEK293T cells transduced with empty vector, WT-GLUT-flag, or MUT-GLUT1-flag. The figure presents mean counts per minute (cpm) value±SD; *p

    Techniques Used: Expressing, Transduction, Plasmid Preparation, Western Blot

    Localization of putative cholesterol-binding motifs in the homology model of human glucose transporter 1 (GLUT1) protein. (A) A homology model of human GLUT1 protein: N-termini and C-termini are indicated and the placement within the plasma membrane is only schematic. (B). Putative cholesterol recognition/interaction amino acid consensus (CRAC)-like motifs in GLUT1: aa 83–89 (VGLFVNR, left) and aa 322–330 (VVSLFVVER, right).
    Figure Legend Snippet: Localization of putative cholesterol-binding motifs in the homology model of human glucose transporter 1 (GLUT1) protein. (A) A homology model of human GLUT1 protein: N-termini and C-termini are indicated and the placement within the plasma membrane is only schematic. (B). Putative cholesterol recognition/interaction amino acid consensus (CRAC)-like motifs in GLUT1: aa 83–89 (VGLFVNR, left) and aa 322–330 (VVSLFVVER, right).

    Techniques Used: Binding Assay

    30) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    31) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    32) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    33) Product Images from "Characterization of a Novel Cutaneous Human Papillomavirus Genotype HPV-125"

    Article Title: Characterization of a Novel Cutaneous Human Papillomavirus Genotype HPV-125

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0022414

    Amino acid alignment of HPV-125 E6 and E7 proteins with corresponding proteins of closely related genotypes from Alphapapillomavirus species 2 and genotypes HPV-16, HPV-18, HPV-6 and HPV-11. Black boxes indicate the location of zinc-binding domains (CxxC(x) 29 CxxC) in both E6 and E7 amino acid alignments. The purple box indicates the location of the pRb-binding core sequence (LxCxE), absent in several Alphapapillomavirus species 2 genotypes [30] , including HPV-125.
    Figure Legend Snippet: Amino acid alignment of HPV-125 E6 and E7 proteins with corresponding proteins of closely related genotypes from Alphapapillomavirus species 2 and genotypes HPV-16, HPV-18, HPV-6 and HPV-11. Black boxes indicate the location of zinc-binding domains (CxxC(x) 29 CxxC) in both E6 and E7 amino acid alignments. The purple box indicates the location of the pRb-binding core sequence (LxCxE), absent in several Alphapapillomavirus species 2 genotypes [30] , including HPV-125.

    Techniques Used: Binding Assay, Sequencing

    Genomic organisation of HPV-125. Genomic positions of viral genes E6, E7, E1, E2, E4 (E1∧E4), L1 and L2 are indicated next to the respective gene. The non-coding regions located between L1 and E6 (LCR); and E2 and L2 are indicated with a dotted line.
    Figure Legend Snippet: Genomic organisation of HPV-125. Genomic positions of viral genes E6, E7, E1, E2, E4 (E1∧E4), L1 and L2 are indicated next to the respective gene. The non-coding regions located between L1 and E6 (LCR); and E2 and L2 are indicated with a dotted line.

    Techniques Used:

    Characteristic features of the long control region (LCR) of HPV-125. The genomic locations of E2 binding sites (ACC-N 5–7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T)) are indicated on the coding strand.
    Figure Legend Snippet: Characteristic features of the long control region (LCR) of HPV-125. The genomic locations of E2 binding sites (ACC-N 5–7 -GGT), polyadenilation sites (AATAAA), and TATA signals (TATAAA or TATA(A/T)A(A/T)) are indicated on the coding strand.

    Techniques Used: Binding Assay

    34) Product Images from "Accuracy, Precision, and Method Detection Limits of Quantitative PCR for Airborne Bacteria and Fungi ▿"

    Article Title: Accuracy, Precision, and Method Detection Limits of Quantitative PCR for Airborne Bacteria and Fungi ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.01240-10

    Instrument repeatability as a function of cell quantity COV ( n = 7). The qPCR MDLs are 5 cells for B. atrophaeus and 0.05 cells for A. fumigatus .
    Figure Legend Snippet: Instrument repeatability as a function of cell quantity COV ( n = 7). The qPCR MDLs are 5 cells for B. atrophaeus and 0.05 cells for A. fumigatus .

    Techniques Used: Real-time Polymerase Chain Reaction

    35) Product Images from "Dehydroepiandrosterone Induces Human CYP2B6 through the Constitutive Androstane Receptor"

    Article Title: Dehydroepiandrosterone Induces Human CYP2B6 through the Constitutive Androstane Receptor

    Journal: Drug metabolism and disposition: the biological fate of chemicals

    doi: 10.1124/dmd.107.016303

    Induction of CYP3A4 activities (a) and mRNA levels (b) in primary human hepatocytes. Human liver cells were treated for 48 h with dexamethasone (DXM, 1 and 10 μ M), DHEA (50 μ M), and its metabolites: 7 α -hydroxy-DHEA (OH-DHEA, 50 μ M) and 7-oxo-DHEA (oxo-DHEA, 50 μ M). CYP3A4 activities were determined in microsomes prepared from hepatocytes isolated from five donors. Levels of CYP3A4 mRNA in human hepatocytes ( n = 5 donors) were quantified and normalized to GAPDH as described under Materials and Methods . Statistical analysis of the results obtained in untreated and treated cells indicated significant increase in both the activities and mRNA levels of CYP3A4 as a consequence of various treatments. Controls for each independent experiment were assigned values of 1 and results of treatments are expressed relative to the controls. Error bars represent standard deviations from the mean of five donors.
    Figure Legend Snippet: Induction of CYP3A4 activities (a) and mRNA levels (b) in primary human hepatocytes. Human liver cells were treated for 48 h with dexamethasone (DXM, 1 and 10 μ M), DHEA (50 μ M), and its metabolites: 7 α -hydroxy-DHEA (OH-DHEA, 50 μ M) and 7-oxo-DHEA (oxo-DHEA, 50 μ M). CYP3A4 activities were determined in microsomes prepared from hepatocytes isolated from five donors. Levels of CYP3A4 mRNA in human hepatocytes ( n = 5 donors) were quantified and normalized to GAPDH as described under Materials and Methods . Statistical analysis of the results obtained in untreated and treated cells indicated significant increase in both the activities and mRNA levels of CYP3A4 as a consequence of various treatments. Controls for each independent experiment were assigned values of 1 and results of treatments are expressed relative to the controls. Error bars represent standard deviations from the mean of five donors.

    Techniques Used: Isolation

    36) Product Images from "Statins impair glucose uptake in human cells"

    Article Title: Statins impair glucose uptake in human cells

    Journal: BMJ Open Diabetes Research & Care

    doi: 10.1136/bmjdrc-2014-000017

    Human embryonic kidney (HEK293T) cells expressing mutated glucose transporter 1-flag gene (MUT-GLUT1-flag) uptake less glucose than their WT-GLUT1-flag counterparts. (A) Evaluation of GLUT1 and GLUT1-flag protein expression in total cellular lysates of two independent sets of parental (non-transduced) HEK293T cells, cells transduced with empty vector, WT-GLUT1-flag and MUT-GLUT1-flag with Western blotting. β-actin levels served as loading control. (B) Absolute quantification of GLUT1-flag and β-2-microglobulin (B2M) transcripts in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (C) Relative quantification of GLUT1-flag transcript in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (D) [1,2- 3 H]-deoxy-D-glucose (2-DOG) uptake in two independent sets of HEK293T cells transduced with empty vector, WT-GLUT-flag, or MUT-GLUT1-flag. The figure presents mean counts per minute (cpm) value±SD; *p
    Figure Legend Snippet: Human embryonic kidney (HEK293T) cells expressing mutated glucose transporter 1-flag gene (MUT-GLUT1-flag) uptake less glucose than their WT-GLUT1-flag counterparts. (A) Evaluation of GLUT1 and GLUT1-flag protein expression in total cellular lysates of two independent sets of parental (non-transduced) HEK293T cells, cells transduced with empty vector, WT-GLUT1-flag and MUT-GLUT1-flag with Western blotting. β-actin levels served as loading control. (B) Absolute quantification of GLUT1-flag and β-2-microglobulin (B2M) transcripts in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (C) Relative quantification of GLUT1-flag transcript in HEK-WT-GLUT1-flag and HEK-MUT-GLUT1-flag cells. (D) [1,2- 3 H]-deoxy-D-glucose (2-DOG) uptake in two independent sets of HEK293T cells transduced with empty vector, WT-GLUT-flag, or MUT-GLUT1-flag. The figure presents mean counts per minute (cpm) value±SD; *p

    Techniques Used: Expressing, Transduction, Plasmid Preparation, Western Blot

    Localization of putative cholesterol-binding motifs in the homology model of human glucose transporter 1 (GLUT1) protein. (A) A homology model of human GLUT1 protein: N-termini and C-termini are indicated and the placement within the plasma membrane is only schematic. (B). Putative cholesterol recognition/interaction amino acid consensus (CRAC)-like motifs in GLUT1: aa 83–89 (VGLFVNR, left) and aa 322–330 (VVSLFVVER, right).
    Figure Legend Snippet: Localization of putative cholesterol-binding motifs in the homology model of human glucose transporter 1 (GLUT1) protein. (A) A homology model of human GLUT1 protein: N-termini and C-termini are indicated and the placement within the plasma membrane is only schematic. (B). Putative cholesterol recognition/interaction amino acid consensus (CRAC)-like motifs in GLUT1: aa 83–89 (VGLFVNR, left) and aa 322–330 (VVSLFVVER, right).

    Techniques Used: Binding Assay

    37) Product Images from "ERK Crosstalks with 4EBP1 to Activate Cyclin D1 Translation during Quinol-Thioether-Induced Tuberous Sclerosis Renal Cell Carcinoma"

    Article Title: ERK Crosstalks with 4EBP1 to Activate Cyclin D1 Translation during Quinol-Thioether-Induced Tuberous Sclerosis Renal Cell Carcinoma

    Journal: Toxicological Sciences

    doi: 10.1093/toxsci/kfr203

    B-Raf, Raf-1, and p-ERK1/2 protein levels are elevated in TGHQ-induced renal tumors from Tsc-2 EK/+ rats. Whole tissue lysates from the OSOM or from renal tumors of 4-, 6-, or 8-month vehicle- or TGHQ-treated Tsc-2 +/+ and Tsc-2 EK/+ rats were immunoblotted for (A) B-Raf in 4- or 6-month tissues, (B) B-Raf (top panel) and Raf-1 (middle panel) in 8-month tissues, and (C) p-ERK1/2 (T202/Y204) (top panel) and ERK1/2 (middle panel) in 8-month tissues. GAPDH (A–C, bottom panels) was used as a loading control. n = 3 rat kidneys per group, representative OSOM or renal tumor sample displayed. The films for the 8-month blots were exposed for 1 s due to the extremely high levels of B-Raf in the tumors. In contrast, the 4- and 6-month films were overexposed for longer than 20 min before developing.
    Figure Legend Snippet: B-Raf, Raf-1, and p-ERK1/2 protein levels are elevated in TGHQ-induced renal tumors from Tsc-2 EK/+ rats. Whole tissue lysates from the OSOM or from renal tumors of 4-, 6-, or 8-month vehicle- or TGHQ-treated Tsc-2 +/+ and Tsc-2 EK/+ rats were immunoblotted for (A) B-Raf in 4- or 6-month tissues, (B) B-Raf (top panel) and Raf-1 (middle panel) in 8-month tissues, and (C) p-ERK1/2 (T202/Y204) (top panel) and ERK1/2 (middle panel) in 8-month tissues. GAPDH (A–C, bottom panels) was used as a loading control. n = 3 rat kidneys per group, representative OSOM or renal tumor sample displayed. The films for the 8-month blots were exposed for 1 s due to the extremely high levels of B-Raf in the tumors. In contrast, the 4- and 6-month films were overexposed for longer than 20 min before developing.

    Techniques Used:

    Raf-1 is the dominant regulator of p-4EBP1 protein levels in QTRRE cells. QTRRE cells were transfected with either (A) Raf-1 (100nM) or (B) B-Raf (100nM) ON_TARGETplus SMARTpool siRNA or siCONTROL Non-Targeting siRNA #5 (Dharmacon RNA Technologies, NY). The siRNA-DharmaFECT complex solution was incubated with cells for 72 or 96 h. 4EBP1 and p-4EBP1-Ser65, -Thr70, and -Thr37/46 were visualized by Western blot analysis. GAPDH was used as a loading control. Values are means ± SD ( n = 3). A significant difference was seen between control siRNA and Raf-1 or B-Raf siRNA-treated cells at * p
    Figure Legend Snippet: Raf-1 is the dominant regulator of p-4EBP1 protein levels in QTRRE cells. QTRRE cells were transfected with either (A) Raf-1 (100nM) or (B) B-Raf (100nM) ON_TARGETplus SMARTpool siRNA or siCONTROL Non-Targeting siRNA #5 (Dharmacon RNA Technologies, NY). The siRNA-DharmaFECT complex solution was incubated with cells for 72 or 96 h. 4EBP1 and p-4EBP1-Ser65, -Thr70, and -Thr37/46 were visualized by Western blot analysis. GAPDH was used as a loading control. Values are means ± SD ( n = 3). A significant difference was seen between control siRNA and Raf-1 or B-Raf siRNA-treated cells at * p

    Techniques Used: Transfection, Incubation, Western Blot

    Raf-1 is the dominant regulator of cyclin D1 protein levels in QTRRE cells. QTRRE cells were transfected with 100nM (A) B-Raf or (B) Raf-1 ON_TARGETplus SMARTpool siRNA or siCONTROL Non-Targeting siRNA #5 (Dharmacon RNA Technologies, NY). The siRNA-DharmaFECT complex solution was incubated with cells for 72 or 96 h. Whole cell lysates were subjected to Western blotting with antibodies specific to B-Raf, Raf-1, cyclin D1, and GAPDH. Values represent the mean ± SD ( n = 3). A significant difference was seen between control siRNA and Raf-1 or B-Raf siRNA-treated cells at * p
    Figure Legend Snippet: Raf-1 is the dominant regulator of cyclin D1 protein levels in QTRRE cells. QTRRE cells were transfected with 100nM (A) B-Raf or (B) Raf-1 ON_TARGETplus SMARTpool siRNA or siCONTROL Non-Targeting siRNA #5 (Dharmacon RNA Technologies, NY). The siRNA-DharmaFECT complex solution was incubated with cells for 72 or 96 h. Whole cell lysates were subjected to Western blotting with antibodies specific to B-Raf, Raf-1, cyclin D1, and GAPDH. Values represent the mean ± SD ( n = 3). A significant difference was seen between control siRNA and Raf-1 or B-Raf siRNA-treated cells at * p

    Techniques Used: Transfection, Incubation, Western Blot

    38) Product Images from "The adaptive regulation of thiamine pyrophosphokinase-1 facilitates malignant growth during supplemental thiamine conditions"

    Article Title: The adaptive regulation of thiamine pyrophosphokinase-1 facilitates malignant growth during supplemental thiamine conditions

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26259

    Altered TPP homeostasis during hypoxic stress ( A ) HPLC analysis demonstrating ex vitro TPP production as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 5 independent experiments. ( B ) HPLC analysis demonstrating intracellular TPP levels as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 3 independent experiments. ( C , D ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells seeded at 25,000 cells/cm 2 and pretreated with 500 μM NaF, 100 μM MTX, 500 μM TRLX or 10 μM MitoQ for 12 h prior to hypoxic exposure for 24 h with sustained exposure to each compound including n = 5 independent experiments. ( E ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells exposed to 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 24 h including n = 3 independent experiments for 10 nM and n = 7 independent experiments for 3 μM. ( F ) Effect of thiamine dose on hypoxia-induced ROS levels demonstrated by hypoxic to normoxic fold change in MitoSOX median fluorescence intensity ± SD in wild type HCT 116 cultured in 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 48 h including n = 3 independent experiments. ( G ) Effect of thiamine dose on hypoxic tumor cell proliferation demonstrated by hypoxic to normoxic fold change in live cell count ± SD determined by trypan blue exclusion. Wild type HCT 116 cells were seeded at 500 cells/cm 2 were grown for 5 d in either 1% O 2 or normoxia including n = 5 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Altered TPP homeostasis during hypoxic stress ( A ) HPLC analysis demonstrating ex vitro TPP production as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 5 independent experiments. ( B ) HPLC analysis demonstrating intracellular TPP levels as fold change in TPP ± SD comparing wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and cultured for 96 h or wild type cells seeded at 1250 cells/cm 2 and treated with 1% O 2 for 24 h relative to normoxic control (N) including n = 3 independent experiments. ( C , D ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells seeded at 25,000 cells/cm 2 and pretreated with 500 μM NaF, 100 μM MTX, 500 μM TRLX or 10 μM MitoQ for 12 h prior to hypoxic exposure for 24 h with sustained exposure to each compound including n = 5 independent experiments. ( E ) HPLC analysis demonstrating mean intracellular TPP levels ± SD established in wild type HCT 116 cells exposed to 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 24 h including n = 3 independent experiments for 10 nM and n = 7 independent experiments for 3 μM. ( F ) Effect of thiamine dose on hypoxia-induced ROS levels demonstrated by hypoxic to normoxic fold change in MitoSOX median fluorescence intensity ± SD in wild type HCT 116 cultured in 10 nM or 3 μM thiamine for 5 d prior to seeding at 50,000 cells/cm 2 and exposure to 1% O 2 for 48 h including n = 3 independent experiments. ( G ) Effect of thiamine dose on hypoxic tumor cell proliferation demonstrated by hypoxic to normoxic fold change in live cell count ± SD determined by trypan blue exclusion. Wild type HCT 116 cells were seeded at 500 cells/cm 2 were grown for 5 d in either 1% O 2 or normoxia including n = 5 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: High Performance Liquid Chromatography, Cell Culture, Fluorescence, Cell Counting

    Attenuation of TPK1 expression using pharmacological inhibition of HIF-1α and reoxygenation ( A ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression under normoxic (N) and hypoxic conditions ± YC-1 in WCLs isolated from wild type HCT 116 cells seeded at 2500 cells/cm 2 and pre-treated with 5 μM YC-1 for 24 h prior to 48 h hypoxic exposure in the presence of 5 μM YC-1. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 in the presence or absence of YC-1 for wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 3 independent experiments. ( C ) Representative Western blots demonstrating HIF-1α and TPK1 in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated in 1% O 2 for 48 h with subsequent reoxygenation at 21% O 2 for 4 and 24 h. ( D ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 and subsequent reoxygenation in wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 4 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Attenuation of TPK1 expression using pharmacological inhibition of HIF-1α and reoxygenation ( A ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression under normoxic (N) and hypoxic conditions ± YC-1 in WCLs isolated from wild type HCT 116 cells seeded at 2500 cells/cm 2 and pre-treated with 5 μM YC-1 for 24 h prior to 48 h hypoxic exposure in the presence of 5 μM YC-1. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 in the presence or absence of YC-1 for wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 3 independent experiments. ( C ) Representative Western blots demonstrating HIF-1α and TPK1 in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated in 1% O 2 for 48 h with subsequent reoxygenation at 21% O 2 for 4 and 24 h. ( D ) Densitometry analysis of the fold change in TPK1 expression ± SD following exposure to 1% O 2 and subsequent reoxygenation in wildtype HCT 116 cells compared to untreated normoxic control (N) including n = 4 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Expressing, Inhibition, Western Blot, Isolation

    Oxidative stress mediated regulation of TPK1 ( A ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from isogenic wild type and HIF-1α –/– HCT 116 cells. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 compared to wild type HCT 116 cells including n = 5 independent experiments. ( C ) Fold change in CM-H2DCFDA median fluorescence intensity ± SD demonstrating fold change in ROS levels between HIF-1α –/– relative to wild type HCT 116 cells including n = 4 independent experiments. ( D ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1 mM NAC or 100 μM ASC for 24 and 48 h relative to untreated HIF-1α –/– HCT 116 CTL (expression of TPK1 in wild type cells provided for comparison). ( E ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 cells treated with NAC and ASC compared to untreated HIF-1α –/– HCT 116 control including n = 4 independent experiments. ( F ) Representative Western blots demonstrating HIF-1α and TPK1 protein expression in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1% O 2 , 0.1 μM DOX, 10 μM CDDP, 5 μM AA or 10 μM TBHP for 24 h relative to normoxic control (N). ( G ) Densitometry analysis of the fold change in TPK1 expression ± SD for wild type HCT 116 cells treated with 1% O 2 , DOX, CDDP, AA or TBHP compared to untreated normoxic control (N) including n = 6 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Oxidative stress mediated regulation of TPK1 ( A ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from isogenic wild type and HIF-1α –/– HCT 116 cells. β-Actin expression serves as the loading control. ( B ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 compared to wild type HCT 116 cells including n = 5 independent experiments. ( C ) Fold change in CM-H2DCFDA median fluorescence intensity ± SD demonstrating fold change in ROS levels between HIF-1α –/– relative to wild type HCT 116 cells including n = 4 independent experiments. ( D ) Representative Western blot demonstrating TPK1 expression in WCLs isolated from HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1 mM NAC or 100 μM ASC for 24 and 48 h relative to untreated HIF-1α –/– HCT 116 CTL (expression of TPK1 in wild type cells provided for comparison). ( E ) Densitometry analysis of the fold change in TPK1 expression ± SD for HIF-1α –/– HCT 116 cells treated with NAC and ASC compared to untreated HIF-1α –/– HCT 116 control including n = 4 independent experiments. ( F ) Representative Western blots demonstrating HIF-1α and TPK1 protein expression in WCLs isolated from wild type HCT 116 cells seeded at 1250 cells/cm 2 and treated with 1% O 2 , 0.1 μM DOX, 10 μM CDDP, 5 μM AA or 10 μM TBHP for 24 h relative to normoxic control (N). ( G ) Densitometry analysis of the fold change in TPK1 expression ± SD for wild type HCT 116 cells treated with 1% O 2 , DOX, CDDP, AA or TBHP compared to untreated normoxic control (N) including n = 6 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Western Blot, Expressing, Isolation, Fluorescence, CTL Assay

    Effect of hypoxic stress and HIF-1α on TPK1 expression ( A ) Representative Western blots demonstrating TPK1 protein expression in WCLs isolated from seven tumor cell lines with tissue origins including breast (MCF7, MDA-MB-231), brain (LN-18, U-87 MG), and intestine (Caco-2, HCT 116, HuTu 80) following treatment with 1% O 2 for 24, 48, and 72 h relative to normoxic control (N). β-Actin expression serves as the loading control. ( B ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 150 μM DMOG or 1% O 2 for 24 h relative to normoxic control (N). ( C , D ) Densitometry analysis of the fold change in TPK1 expression ± standard deviation (SD) following DMOG and 1% O 2 treatment in wildtype and HIF-1α –/– HCT 116 cells compared to normoxic control (N) including n = 4 independent experiments for wild type and n = 3 independent experiments in HIF-1α –/– cells. ( E ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 2500 cells/cm 2 and transfected with 2.5 μg of HIF-1α CA plasmid DNA relative to vector control (VCTR) for 72 h. ( F , G ) Densitometry analysis of the fold change in TPK1 expression ± SD following HIF-1α CA overexpression in wildtype and HIF-1α –/– HCT 116 cells compared to vector control including n = 3 independent experiments. (*) Represents statistically significant difference ( p
    Figure Legend Snippet: Effect of hypoxic stress and HIF-1α on TPK1 expression ( A ) Representative Western blots demonstrating TPK1 protein expression in WCLs isolated from seven tumor cell lines with tissue origins including breast (MCF7, MDA-MB-231), brain (LN-18, U-87 MG), and intestine (Caco-2, HCT 116, HuTu 80) following treatment with 1% O 2 for 24, 48, and 72 h relative to normoxic control (N). β-Actin expression serves as the loading control. ( B ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 1250 cells/cm 2 and treated with 150 μM DMOG or 1% O 2 for 24 h relative to normoxic control (N). ( C , D ) Densitometry analysis of the fold change in TPK1 expression ± standard deviation (SD) following DMOG and 1% O 2 treatment in wildtype and HIF-1α –/– HCT 116 cells compared to normoxic control (N) including n = 4 independent experiments for wild type and n = 3 independent experiments in HIF-1α –/– cells. ( E ) Representative Western blots demonstrating HIF-1α, LDHA, and TPK1 protein expression in WCLs isolated from wild type and HIF-1α –/– HCT 116 cells seeded at 2500 cells/cm 2 and transfected with 2.5 μg of HIF-1α CA plasmid DNA relative to vector control (VCTR) for 72 h. ( F , G ) Densitometry analysis of the fold change in TPK1 expression ± SD following HIF-1α CA overexpression in wildtype and HIF-1α –/– HCT 116 cells compared to vector control including n = 3 independent experiments. (*) Represents statistically significant difference ( p

    Techniques Used: Expressing, Western Blot, Isolation, Multiple Displacement Amplification, Standard Deviation, Transfection, Plasmid Preparation, Over Expression

    39) Product Images from "Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells"

    Article Title: Prenatal stress is a vulnerability factor for altered morphology and biological activity of microglia cells

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2015.00082

    The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p
    Figure Legend Snippet: The impact of prenatal stress on protein levels of cytokines: IL-1β, IL-18, TNF-α and IL-6 (left panel) and chemokines: CCL2, CXCL12 and their receptors: CCR2, CXCR4 (right panel) in microglial cells . Protein levels obtained from ELISA are shown as pg/ml or ng/ml ± SD from 3 independent experiments ( n = 8 in each group); The results from western blot analyses are normalized with β-actin and presented as % of control ± SD from 3 independent experiments ( n = 6 in each group); * p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    40) Product Images from "BONE MORPHOGENETIC PROTEIN-7 REDUCES TOXICITY INDUCED BY HIGH DOSES OF METHAMPHETAMINE IN RODENTS"

    Article Title: BONE MORPHOGENETIC PROTEIN-7 REDUCES TOXICITY INDUCED BY HIGH DOSES OF METHAMPHETAMINE IN RODENTS

    Journal: Neuroscience

    doi: 10.1016/j.neuroscience.2007.10.044

    BMP7 heterozygous knockout mice exhibit decreased striatal TH-immunoreactivity following MA exposure. (A) MA administration suppressed THir in +/+ (1 vs. 2) and +/− mice (3 vs. 4). Scale bar=2 mm. (B) THir fiber density analysis indicated that MA suppressed THir in +/+ and +/− mice. There is a marginal difference in striatal THir ( P =0.086) between +/+ and +/− mice after MA injection.
    Figure Legend Snippet: BMP7 heterozygous knockout mice exhibit decreased striatal TH-immunoreactivity following MA exposure. (A) MA administration suppressed THir in +/+ (1 vs. 2) and +/− mice (3 vs. 4). Scale bar=2 mm. (B) THir fiber density analysis indicated that MA suppressed THir in +/+ and +/− mice. There is a marginal difference in striatal THir ( P =0.086) between +/+ and +/− mice after MA injection.

    Techniques Used: Knock-Out, Mouse Assay, Injection

    Exogenous BMP7 restores THir in striatum after MA administration in CD1 mice. Animals received 4×10 mg/kg doses of MA. Four days after MA exposure, animals were killed and brains analyzed for TH immunoreactivity (A) TH immunostaining indicates that MA administration suppressed striatal THir (1 vs. 2). I.c.v. administration of BMP7 restored THir (2 vs. 4). Scale bar=2 mm. (B) MA significantly reduced striatal THir fiber density in mice pretreated with i.c.v. vehicle. Administration of BMP7 antagonized the loss of TH fiber density in striatum in MA-treated mice (* P
    Figure Legend Snippet: Exogenous BMP7 restores THir in striatum after MA administration in CD1 mice. Animals received 4×10 mg/kg doses of MA. Four days after MA exposure, animals were killed and brains analyzed for TH immunoreactivity (A) TH immunostaining indicates that MA administration suppressed striatal THir (1 vs. 2). I.c.v. administration of BMP7 restored THir (2 vs. 4). Scale bar=2 mm. (B) MA significantly reduced striatal THir fiber density in mice pretreated with i.c.v. vehicle. Administration of BMP7 antagonized the loss of TH fiber density in striatum in MA-treated mice (* P

    Techniques Used: Mouse Assay, Immunostaining

    BMP7 mRNA levels are decreased in the brains of BMP7 heterozygous mice. Brain mRNA levels for BMP7, PGK1 and HPRT1 were measured in adult BMP7 +/+ ( n =5) and +/− mice ( n =5) by qRT-PCR. For each sample, mRNA levels for genes of interest were normalized to the housekeeping gene HPRT1 mRNA level. Another housekeeping gene PGK1 mRNA level did not differ between +/+ and +/− mice. BMP7 mRNA level is significantly decreased (50%) in +/− mice compared with the level in +/+ mice (* P
    Figure Legend Snippet: BMP7 mRNA levels are decreased in the brains of BMP7 heterozygous mice. Brain mRNA levels for BMP7, PGK1 and HPRT1 were measured in adult BMP7 +/+ ( n =5) and +/− mice ( n =5) by qRT-PCR. For each sample, mRNA levels for genes of interest were normalized to the housekeeping gene HPRT1 mRNA level. Another housekeeping gene PGK1 mRNA level did not differ between +/+ and +/− mice. BMP7 mRNA level is significantly decreased (50%) in +/− mice compared with the level in +/+ mice (* P

    Techniques Used: Mouse Assay, Quantitative RT-PCR

    MA suppresses BMP7 mRNA levels in mouse SN. The effect of MA on BMP-7 gene regulation was directly measured by quantitative RT-PCR. mRNA levels for BMP7, PGK1 and HPRT were measured by qRT-PCR 1 day after injection of either MA or saline in CD1 mice. For each sample, mRNA levels for the specific gene were normalized to the housekeeping gene HPRT mRNA level. The housekeeping gene PGK1 mRNA level did not differ between saline and MA groups (A). Nigral BMP7 mRNA levels were significantly decreased in MA injected mice ( n =9) compared with the levels in the saline injected group ( n =9) (B, C; * P
    Figure Legend Snippet: MA suppresses BMP7 mRNA levels in mouse SN. The effect of MA on BMP-7 gene regulation was directly measured by quantitative RT-PCR. mRNA levels for BMP7, PGK1 and HPRT were measured by qRT-PCR 1 day after injection of either MA or saline in CD1 mice. For each sample, mRNA levels for the specific gene were normalized to the housekeeping gene HPRT mRNA level. The housekeeping gene PGK1 mRNA level did not differ between saline and MA groups (A). Nigral BMP7 mRNA levels were significantly decreased in MA injected mice ( n =9) compared with the levels in the saline injected group ( n =9) (B, C; * P

    Techniques Used: Quantitative RT-PCR, Injection, Mouse Assay

    BMP7 reduces MA-induced toxicity in ventral mesencephalic cultures. (A) Primary cultures prepared from rat VM (E14) were treated with 1.5 nM BMP7 for 20 min then exposed to 1 mM MA for 72 h. Cells were fixed and assayed using TH immunostaining (red) and TUNEL (green). MA increased TUNEL and decreased TH cell numbers and fiber density. (B1) BMP7 alone did not alter the THir fiber density; however, BMP7 antagonized the MA-mediated decrease in THir. (B2) BMP7 also antagonized the MA-induced decrease in number of TH positive neurons in culture. (B3) Pretreatment with BMP7 reduced the MA-mediated increase in TUNEL (* P
    Figure Legend Snippet: BMP7 reduces MA-induced toxicity in ventral mesencephalic cultures. (A) Primary cultures prepared from rat VM (E14) were treated with 1.5 nM BMP7 for 20 min then exposed to 1 mM MA for 72 h. Cells were fixed and assayed using TH immunostaining (red) and TUNEL (green). MA increased TUNEL and decreased TH cell numbers and fiber density. (B1) BMP7 alone did not alter the THir fiber density; however, BMP7 antagonized the MA-mediated decrease in THir. (B2) BMP7 also antagonized the MA-induced decrease in number of TH positive neurons in culture. (B3) Pretreatment with BMP7 reduced the MA-mediated increase in TUNEL (* P

    Techniques Used: Immunostaining, TUNEL Assay

    Basal locomotor activity of CD1 and BMP7 transgenic mice. (A) In CD1 mice, BMP7 (1 μ g/ μ l×5 μl , i.c.v., –∇–) did not alter (A1) total distance traveled, (A2) movement time, and (A3) horizontal activity, compared with animals receiving i.c.v. vehicle (—■—). (B) BMP7 +/− mice (—▲—) had a significant increase in all basal locomotor activities compared with the +/+ mice (—●—).
    Figure Legend Snippet: Basal locomotor activity of CD1 and BMP7 transgenic mice. (A) In CD1 mice, BMP7 (1 μ g/ μ l×5 μl , i.c.v., –∇–) did not alter (A1) total distance traveled, (A2) movement time, and (A3) horizontal activity, compared with animals receiving i.c.v. vehicle (—■—). (B) BMP7 +/− mice (—▲—) had a significant increase in all basal locomotor activities compared with the +/+ mice (—●—).

    Techniques Used: Activity Assay, Transgenic Assay, Mouse Assay

    Behavioral interactions of BMP7 and MA in CD1 and BMP7 transgenic mice. Daily locomotor activity after MA injection was normalized by comparison to the average activity on day 1 from the control mice. (A) In CD1 mice, MA alone (—■—) reduced locomotor activity. Administration of BMP7 (—∇—) significantly antagonized the MA-mediated decrease in (A1) total distance traveled, (A2) movement time, and (A3) horizontal activity ( P
    Figure Legend Snippet: Behavioral interactions of BMP7 and MA in CD1 and BMP7 transgenic mice. Daily locomotor activity after MA injection was normalized by comparison to the average activity on day 1 from the control mice. (A) In CD1 mice, MA alone (—■—) reduced locomotor activity. Administration of BMP7 (—∇—) significantly antagonized the MA-mediated decrease in (A1) total distance traveled, (A2) movement time, and (A3) horizontal activity ( P

    Techniques Used: Transgenic Assay, Mouse Assay, Activity Assay, Injection

    BMP7 heterozygous knockout mice exhibit decreased TH-immunoreactivity in SNpr following MA exposure. (A) TH immunostaining indicates that MA administration increases the reduction of THir in the SNpr of BMP7 +/−, compared with +/+, mice (2 vs. 4). Scale bar=500 μ m. (B) THir fiber density analysis indicated MA reduced THir fiber density in SNpr in +/+ and +/− mice. A greater reduction in TH immunoreactivity was found in the BMP7 +/− mice.
    Figure Legend Snippet: BMP7 heterozygous knockout mice exhibit decreased TH-immunoreactivity in SNpr following MA exposure. (A) TH immunostaining indicates that MA administration increases the reduction of THir in the SNpr of BMP7 +/−, compared with +/+, mice (2 vs. 4). Scale bar=500 μ m. (B) THir fiber density analysis indicated MA reduced THir fiber density in SNpr in +/+ and +/− mice. A greater reduction in TH immunoreactivity was found in the BMP7 +/− mice.

    Techniques Used: Knock-Out, Mouse Assay, Immunostaining

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