gapdh glyceraldehyde-3-phosphate dehydrogenase gene Search Results


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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    Everolimus (EV) inhibits cancer cell growth in vitro and in vivo. a The murine melanoma cell line B16-F10 and the human breast cancer cell lines MCF-7 and MDA-MB-231 were treated with EV in a dose-dependent (0, 1, 10, and 100 nM) and time-dependent (0, 24, 48, and 72 h) manner. Cell viability was assessed with the CellTiter-Blue® assay. b Western blots used to assess the ability of EV concentrations to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) protein and p70 S6 kinase after 24 h of treatment in the cell lines investigated. Glyceraldehyde 3-phosphate dehydrogenase ( <t>GAPDH</t> ) is shown as the housekeeping control. c Female immunocompetent (C57BL/6) and immunocompromised (NMRI nude) mice were inoculated subcutaneously with B16-F10 and MDA-MB-231 cells, respectively. Tumor growth was assessed after daily treatment with 1 mg/kg of EV for 2 and 4 weeks in each respective model. In vitro and in vivo data are shown as mean ± SD of at least three independent experiments or ten mice per group, respectively. Cell viability assays were analyzed for each time point using two-way analysis of variance and in vivo data by Student’s t test. Significance between EV treatments and the control condition was apparent only at 72 h and is indicated by asterisks on the graphs. In the B16-F10 graph, EV treatment was significant at inhibiting viability only at 72 h at concentrations of 10 and 100 nM. In the MDA-MB-231 and MCF-7 graphs, all concentrations of EV were significant to the same degree. ** p
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    Everolimus (EV) inhibits cancer cell growth in vitro and in vivo. a The murine melanoma cell line B16-F10 and the human breast cancer cell lines MCF-7 and MDA-MB-231 were treated with EV in a dose-dependent (0, 1, 10, and 100 nM) and time-dependent (0, 24, 48, and 72 h) manner. Cell viability was assessed with the CellTiter-Blue® assay. b Western blots used to assess the ability of EV concentrations to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) protein and p70 S6 kinase after 24 h of treatment in the cell lines investigated. Glyceraldehyde 3-phosphate dehydrogenase ( <t>GAPDH</t> ) is shown as the housekeeping control. c Female immunocompetent (C57BL/6) and immunocompromised (NMRI nude) mice were inoculated subcutaneously with B16-F10 and MDA-MB-231 cells, respectively. Tumor growth was assessed after daily treatment with 1 mg/kg of EV for 2 and 4 weeks in each respective model. In vitro and in vivo data are shown as mean ± SD of at least three independent experiments or ten mice per group, respectively. Cell viability assays were analyzed for each time point using two-way analysis of variance and in vivo data by Student’s t test. Significance between EV treatments and the control condition was apparent only at 72 h and is indicated by asterisks on the graphs. In the B16-F10 graph, EV treatment was significant at inhibiting viability only at 72 h at concentrations of 10 and 100 nM. In the MDA-MB-231 and MCF-7 graphs, all concentrations of EV were significant to the same degree. ** p
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    Thermo Fisher enzyme glyceraldehyde 3 phosphate dehydrogenase gapdh human housekeeping gene
    Everolimus (EV) inhibits cancer cell growth in vitro and in vivo. a The murine melanoma cell line B16-F10 and the human breast cancer cell lines MCF-7 and MDA-MB-231 were treated with EV in a dose-dependent (0, 1, 10, and 100 nM) and time-dependent (0, 24, 48, and 72 h) manner. Cell viability was assessed with the CellTiter-Blue® assay. b Western blots used to assess the ability of EV concentrations to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) protein and p70 S6 kinase after 24 h of treatment in the cell lines investigated. Glyceraldehyde 3-phosphate dehydrogenase ( <t>GAPDH</t> ) is shown as the housekeeping control. c Female immunocompetent (C57BL/6) and immunocompromised (NMRI nude) mice were inoculated subcutaneously with B16-F10 and MDA-MB-231 cells, respectively. Tumor growth was assessed after daily treatment with 1 mg/kg of EV for 2 and 4 weeks in each respective model. In vitro and in vivo data are shown as mean ± SD of at least three independent experiments or ten mice per group, respectively. Cell viability assays were analyzed for each time point using two-way analysis of variance and in vivo data by Student’s t test. Significance between EV treatments and the control condition was apparent only at 72 h and is indicated by asterisks on the graphs. In the B16-F10 graph, EV treatment was significant at inhibiting viability only at 72 h at concentrations of 10 and 100 nM. In the MDA-MB-231 and MCF-7 graphs, all concentrations of EV were significant to the same degree. ** p
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    Image Search Results


    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.

    Journal: Breast Cancer Research : BCR

    Article Title: Large isoform of MRJ (DNAJB6) reduces malignant activity of breast cancer

    doi: 10.1186/bcr1874

    Figure Lengend Snippet: Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.

    Article Snippet: The PCR primers and probes for KiSS1, nucleophosmin (NPM1), osteonectin (SPARC), osteopontin (SPP1), zinc binding α2 -glycoprotein 1 (AZGP1) and VGF nerve growth factor inducible (VGF), and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were purchased from Applied Biosystems Inc. Quantative RT-PCR was performed on an ABI 7500 HT instrument (Applied Biosystems, Foster City, CA, USA).

    Techniques: Mass Spectrometry, Western Blot, Multiple Displacement Amplification, Plasmid Preparation, Binding Assay, Expressing, Quantitative RT-PCR, Polymerase Chain Reaction

    Expression of MRJ in breast cancer cell lines and tissues. (a) Expression of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) is significantly lower in various breast cancer cell lines as compared with that observed in RNA from normal breast. Real-time quantitative RT-PCR was used to assess expression of MRJ(L) relative to endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The data are represented as fold change in the abundance of the MRJ(L) transcripts using commercially available normal breast RNA as a calibrator. Each reaction was carried out in triplicate, and the experiment was repeated once with RNA from the same cell lines at a different passage. The error bars represent the standard error. (b) Expression of MRJ isoforms in various breast cancer cell lines. An equal amount of protein lysate (20 μg) was resolved on SDS-PAGE and immunoblotted for levels of MRJ isoforms. Equal loading was confirmed by comparable β-actin signal. (c) Tissue microarray staining for MRJ. A breast carcinoma progression array (CC08-00-001; developed by Cybrdi Inc.) was stained by 1:100 dilution (10 μg/ml) of DNAJB6 monoclonal antibody. Mouse IgG 1 was used for the isotype background control. Photomicrographs were taken in the area of most intense and diffuse staining for MRJ. The photomicrographs are representative images showing staining patterns of MRJ. Panel 1 corresponds to cystic hyperplasia, and panel 2 corresponds to infiltrating ductal carcinoma grade III.

    Journal: Breast Cancer Research : BCR

    Article Title: Large isoform of MRJ (DNAJB6) reduces malignant activity of breast cancer

    doi: 10.1186/bcr1874

    Figure Lengend Snippet: Expression of MRJ in breast cancer cell lines and tissues. (a) Expression of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) is significantly lower in various breast cancer cell lines as compared with that observed in RNA from normal breast. Real-time quantitative RT-PCR was used to assess expression of MRJ(L) relative to endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The data are represented as fold change in the abundance of the MRJ(L) transcripts using commercially available normal breast RNA as a calibrator. Each reaction was carried out in triplicate, and the experiment was repeated once with RNA from the same cell lines at a different passage. The error bars represent the standard error. (b) Expression of MRJ isoforms in various breast cancer cell lines. An equal amount of protein lysate (20 μg) was resolved on SDS-PAGE and immunoblotted for levels of MRJ isoforms. Equal loading was confirmed by comparable β-actin signal. (c) Tissue microarray staining for MRJ. A breast carcinoma progression array (CC08-00-001; developed by Cybrdi Inc.) was stained by 1:100 dilution (10 μg/ml) of DNAJB6 monoclonal antibody. Mouse IgG 1 was used for the isotype background control. Photomicrographs were taken in the area of most intense and diffuse staining for MRJ. The photomicrographs are representative images showing staining patterns of MRJ. Panel 1 corresponds to cystic hyperplasia, and panel 2 corresponds to infiltrating ductal carcinoma grade III.

    Article Snippet: The PCR primers and probes for KiSS1, nucleophosmin (NPM1), osteonectin (SPARC), osteopontin (SPP1), zinc binding α2 -glycoprotein 1 (AZGP1) and VGF nerve growth factor inducible (VGF), and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were purchased from Applied Biosystems Inc. Quantative RT-PCR was performed on an ABI 7500 HT instrument (Applied Biosystems, Foster City, CA, USA).

    Techniques: Expressing, Quantitative RT-PCR, SDS Page, Microarray, Staining

    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.

    Journal: Infectious Diseases

    Article Title: Retinoid Expression in Onchocercal Skin Disease: Pilot Study

    doi: 10.1177/1178633617731741

    Figure Lengend Snippet: Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.

    Article Snippet: Quantitative polymerase chain reaction and data analysis A target-specific TaqMan assay for O volvulus genomic sequence, for RAR-α transcripts, and for the genomic sequence of human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene, was obtained from Applied Biosystems Inc. (ABI).

    Techniques: Expressing

    Fold expression of RAR-α relative to control sample (normalized with expression levels of GAPDH). GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Uncolored bars indicate that no average Ct was obtained for the retinoic acid receptor (RAR) and/or GAPDH assay for that sample. Retinoic acid receptor expression levels for the control sample have been adjusted to 1 and are highlighted in green.

    Journal: Infectious Diseases

    Article Title: Retinoid Expression in Onchocercal Skin Disease: Pilot Study

    doi: 10.1177/1178633617731741

    Figure Lengend Snippet: Fold expression of RAR-α relative to control sample (normalized with expression levels of GAPDH). GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Uncolored bars indicate that no average Ct was obtained for the retinoic acid receptor (RAR) and/or GAPDH assay for that sample. Retinoic acid receptor expression levels for the control sample have been adjusted to 1 and are highlighted in green.

    Article Snippet: Quantitative polymerase chain reaction and data analysis A target-specific TaqMan assay for O volvulus genomic sequence, for RAR-α transcripts, and for the genomic sequence of human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene, was obtained from Applied Biosystems Inc. (ABI).

    Techniques: Expressing

    Everolimus (EV) inhibits cancer cell growth in vitro and in vivo. a The murine melanoma cell line B16-F10 and the human breast cancer cell lines MCF-7 and MDA-MB-231 were treated with EV in a dose-dependent (0, 1, 10, and 100 nM) and time-dependent (0, 24, 48, and 72 h) manner. Cell viability was assessed with the CellTiter-Blue® assay. b Western blots used to assess the ability of EV concentrations to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) protein and p70 S6 kinase after 24 h of treatment in the cell lines investigated. Glyceraldehyde 3-phosphate dehydrogenase ( GAPDH ) is shown as the housekeeping control. c Female immunocompetent (C57BL/6) and immunocompromised (NMRI nude) mice were inoculated subcutaneously with B16-F10 and MDA-MB-231 cells, respectively. Tumor growth was assessed after daily treatment with 1 mg/kg of EV for 2 and 4 weeks in each respective model. In vitro and in vivo data are shown as mean ± SD of at least three independent experiments or ten mice per group, respectively. Cell viability assays were analyzed for each time point using two-way analysis of variance and in vivo data by Student’s t test. Significance between EV treatments and the control condition was apparent only at 72 h and is indicated by asterisks on the graphs. In the B16-F10 graph, EV treatment was significant at inhibiting viability only at 72 h at concentrations of 10 and 100 nM. In the MDA-MB-231 and MCF-7 graphs, all concentrations of EV were significant to the same degree. ** p

    Journal: Breast Cancer Research : BCR

    Article Title: Concurrent antitumor and bone-protective effects of everolimus in osteotropic breast cancer

    doi: 10.1186/s13058-017-0885-7

    Figure Lengend Snippet: Everolimus (EV) inhibits cancer cell growth in vitro and in vivo. a The murine melanoma cell line B16-F10 and the human breast cancer cell lines MCF-7 and MDA-MB-231 were treated with EV in a dose-dependent (0, 1, 10, and 100 nM) and time-dependent (0, 24, 48, and 72 h) manner. Cell viability was assessed with the CellTiter-Blue® assay. b Western blots used to assess the ability of EV concentrations to inhibit the phosphorylation of the mammalian target of rapamycin (mTOR) protein and p70 S6 kinase after 24 h of treatment in the cell lines investigated. Glyceraldehyde 3-phosphate dehydrogenase ( GAPDH ) is shown as the housekeeping control. c Female immunocompetent (C57BL/6) and immunocompromised (NMRI nude) mice were inoculated subcutaneously with B16-F10 and MDA-MB-231 cells, respectively. Tumor growth was assessed after daily treatment with 1 mg/kg of EV for 2 and 4 weeks in each respective model. In vitro and in vivo data are shown as mean ± SD of at least three independent experiments or ten mice per group, respectively. Cell viability assays were analyzed for each time point using two-way analysis of variance and in vivo data by Student’s t test. Significance between EV treatments and the control condition was apparent only at 72 h and is indicated by asterisks on the graphs. In the B16-F10 graph, EV treatment was significant at inhibiting viability only at 72 h at concentrations of 10 and 100 nM. In the MDA-MB-231 and MCF-7 graphs, all concentrations of EV were significant to the same degree. ** p

    Article Snippet: An antibody for the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (5G4) was purchased from HyTest Oy (Turku, Finland).

    Techniques: In Vitro, In Vivo, Multiple Displacement Amplification, CtB Assay, Western Blot, Mouse Assay