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  • 90
    Thermo Fisher dmso anhydrous
    Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with <t>Graspin</t> (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or <t>DMSO</t> as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P
    Dmso Anhydrous, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dmso  (3M Co)
    90
    3M Co dmso
    Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with <t>Graspin</t> (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or <t>DMSO</t> as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P
    Dmso, supplied by 3M Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    AAT Bioquest dmso
    Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with <t>Graspin</t> (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or <t>DMSO</t> as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P
    Dmso, supplied by AAT Bioquest, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Amresco dmso
    Protocol flowchart. The bilateral common carotid arteries were colligated for 10 min to establish forebrain ischemia followed by <t>reperfusion.</t> SA: salvinorin A; <t>DMSO:</t> dimethyl sulfoxide; nor-BIN: norbinaltorphimine; BCCAO: bilateral common carotid artery occlusion; CSF: cerebrospinal fluid.
    Dmso, supplied by Amresco, used in various techniques. Bioz Stars score: 98/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Applichem dmso
    Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control <t>IgG/DMSO</t> without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).
    Dmso, supplied by Applichem, used in various techniques. Bioz Stars score: 98/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    PanReac AppliChem dmso
    Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control <t>IgG/DMSO</t> without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).
    Dmso, supplied by PanReac AppliChem, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Avantor dmso
    Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% <t>DMSO)</t> showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor <t>SU5402</t> showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.
    Dmso, supplied by Avantor, used in various techniques. Bioz Stars score: 98/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Beyotime dmso
    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL <t>IFN-γ</t> for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or <t>DMSO</t> for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P
    Dmso, supplied by Beyotime, used in various techniques. Bioz Stars score: 98/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Burdick & Jackson dmso
    Effects of the antioxidant <t>DMSO</t> and neutrophil depletion on upregulation of <t>P-selectin</t> in IgG immune complex-induced lung injury ( A ) and in CVF-induced lung injury ( B ). For each column, n ≥ 4.
    Dmso, supplied by Burdick & Jackson, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Carl Roth GmbH dmso
    Immunofluorescence staining with phalloidin of U2OS cells treated with <t>cytochalasans.</t> ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM <t>DMSO</t> (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.
    Dmso, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 98/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Duchefa dmso
    Recruitment of HDAC2 and PAX5 to the promoters of target genes. (A) Flag-tagged PAX5 was overexpressed in HEK293T cells. Extracts were immunoprecipitated with anti-Flag antibodies. Associated proteins were eluted, resolved by SDS-PAGE, and immunoblotted with anti-Flag and anti-HDAC2 antibodies. (B) Differential changes in interaction between HDAC2 and PAX5 48 hrs after treatment with 32 nM <t>TPA</t> were determined by IP. Extracts from TPA- or <t>DMSO-treated</t> HL-60 cells were immunoprecipitated with anti-PAX5 antibodies. HDAC2 that interacted with PAX5 in HL-60 cells was eluted and immunoblotted with a HDAC2 antibody. (C) The mRNA levels of atypically active genes in PAX5 -depleted HL-60 cells were determined by qPCR. PAX5 protein level was detected by western blotting. These data were normalized by GAPDH. (D) HEK293T cells were co-transfected with pCMV-Flag-PAX5 and pGL3.0- IL10RA or pGL3.0- RGCC promoters. Luciferase activities were measured 48 hrs after transfection, and normalized to that of β-galactosidase. (C–D) All results represent at least three independent experiments (± SEMs). * P
    Dmso, supplied by Duchefa, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Enzo Biochem dmso
    ROCK localization to medioapical foci requires the actin cytoskeleton and Dia ( A ) Apical views of ventral furrow cells in embryos expressing ubi-GFP::ROCK, Gap43::mCherry (Membrane) or GFP::ROCK, Utr::mCherry (F-actin) and injected with <t>DMSO</t> after 0 sec time point. ( B ) Same as (A) but with <t>Latrunculin</t> B injection. Disrupted ROCK polarity (white outline and arrow). ( C ) Apical ROCK in wild-type and maternal dia 5 .
    Dmso, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 98/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Euromedex dmso
    Knockdown of Bfl-1 by shRNA sensitizes HTLV-1-infected C91PL T-cells to <t>ABT-737-</t> or etoposide-induced apoptosis. A , effect of ABT-737 on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle <t>(DMSO)</t> or ABT-737. After 2 days, percentages of cell death (PI + ) were measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. B , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later exposed to different concentrations of DMSO or ABT-737 for 2 additional days. Cell death was assessed by PI staining and measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. C , effect of etoposide on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle (DMSO) or etoposide. After 2 days, the percentages of cell death were measured as in A . Results are expressed as mean ± S.D. of three independent experiments. D , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later were exposed to different concentrations of etoposide for 2 additional days. Apoptosis was assessed by anti-active caspase-3 Ab staining and measured by flow cytometry. Results are from one representative experiment of two.
    Dmso, supplied by Euromedex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Fisher Scientific dmso
    Time to complete transmigration. (A) Transmigration time (through endothelium on 5 kPa gel) for all neutrophils, from when the first protrusion is seen under the endothelium, to complete transmigration (except tails for the cases of blebbistain and ML-7), for all treatments. Bars represent mean ± SEM of pooled data from 3 independent experiments (N = 61, 103, 75, 182, 32 for <t>DMSO,</t> <t>blebbistatin,</t> ML-7, nocodazole, and taxol, respectively). ** indicates P
    Dmso, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 98/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    FUJIFILM dmso
    Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater <t>(ASW),</t> 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% <t>DMSO</t> (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.
    Dmso, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 98/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    HiMedia Laboratories dmso
    Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater <t>(ASW),</t> 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% <t>DMSO</t> (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.
    Dmso, supplied by HiMedia Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    IDT Biologika dmso
    Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater <t>(ASW),</t> 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% <t>DMSO</t> (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.
    Dmso, supplied by IDT Biologika, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    LC Laboratories dmso
    Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater <t>(ASW),</t> 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% <t>DMSO</t> (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.
    Dmso, supplied by LC Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Mediatech dmso
    UVB-activated caspase-9 is inhibited by <t>CoQ10.</t> A–F , Immunocytochemistry of cleaved caspase-9. Number of caspase-9 positive cells increased after UVB irradiation with or without 0.1% <t>DMSO</t> ( B,C ) compared to control ( A ). Pretreatment with CoQ10 at 0.01, 0.1, or 1 M significantly reduced the number of caspase-9 positive cells ( D–F ). Green color represents cleaved caspase-9 staining and blue color denotes DAPI stained nuclei. Insert in Figure 3C shows cytosolic localization of cleaved caspase-9. G , western blotting showing full length (49 KD) and cleaved (39 KD) caspase-9 in control, UVB, and CoQ10 treated cells. Total and cleaved caspase-9 increased after UVB and CoQ10 pretreatment reduced both total and cleaved caspase-9 in the cytosolic fraction. H , Number of cleaved caspase-9 positive cells per high magnification field counted from 3 independent immunocytochemistry experiments, each performed in triplicate. # p
    Dmso, supplied by Mediatech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Merck & Co dmso
    Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% <t>DMSO</t> (vehicle), 0.25 µM <t>calyculin</t> (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P
    Dmso, supplied by Merck & Co, used in various techniques. Bioz Stars score: 98/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA dmso
    Effects of the specific BMP inhibitor <t>K02288</t> on bone mineralization. Alizarine red staining of 5 dpf larvae previously treated at 2 ( B , D ) or 3 dpf ( F ) during 24 h with K02288 10 (B) and 20 µM (D,F). Control embryos ( A , C , E ) were treated with <t>DMSO.</t> c: cleithrum; en: entopterygoid; o: operculum; p: parasphenoid. Scale bar: 200 µM.
    Dmso, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 98/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore dmso
    Inhibition of DOX or <t>RES</t> on proliferation of MCF-7/DOX (DOX-resistant cell line) and MCF-7/sensitive (s) cells. MCF-7/DOX and MCF-7/s cells were exposed to serial dilutions of (A) DOX or (B) RES for 48 h and cell inhibition rate was determined via an MTT assay for MCF-7/s (circle) and MCF-7/DOX (square) cells. DOX, doxorubicin; IR, inhibition ratio; <t>DMSO,</t> dimethylsulfoxide; RES, resveratrol.
    Dmso, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1873 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Nacalai dmso
    Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or <t>DMSO</t> (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of <t>proteasome</t> activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).
    Dmso, supplied by Nacalai, used in various techniques. Bioz Stars score: 98/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega dmso
    Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or <t>DMSO</t> (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of <t>proteasome</t> activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).
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    Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or <t>DMSO</t> (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of <t>proteasome</t> activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).
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    Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or <t>DMSO</t> (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of <t>proteasome</t> activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).
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    Click-iT Plus EdU proliferation assay. Plot depicts percent of A549 cell nuclei positive for EdU on day 4 in monoculture and the A549/CCL-210 co-cultures, separated by gel and media type. The nondegradable gels contained a peptide crosslinker insensitive to <t>MMP</t> cleavage. GM6001 was added at 10 μM, and the <t>DMSO</t> control media contained 0.05% DMSO. The degradable bars refer to the original experiment in MMP-degradable gels with regular growth media. Results are presented as means ± SEM of three biological replicates of each condition. *p
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    Click-iT Plus EdU proliferation assay. Plot depicts percent of A549 cell nuclei positive for EdU on day 4 in monoculture and the A549/CCL-210 co-cultures, separated by gel and media type. The nondegradable gels contained a peptide crosslinker insensitive to <t>MMP</t> cleavage. GM6001 was added at 10 μM, and the <t>DMSO</t> control media contained 0.05% DMSO. The degradable bars refer to the original experiment in MMP-degradable gels with regular growth media. Results are presented as means ± SEM of three biological replicates of each condition. *p
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    Movement angle is the angle between expected sheet direction ( i . e . wound closing or 0°) and PIV determined velocity vectors. Color bar indicates fraction of all PIV vectors with a particular orientation. Reference condition is <t>DMSO</t> treated and dysregulated condition is <t>ICG-001</t> treated. CCM stands for control conditioned media; WCM stands for Wnt3a conditioned media.
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    <t>AHR</t> prevents IL-1R1 hi ILC3s from acquiring the capacity for IFN-γ production in vitro ( A-D ) IL-1R1 hi ILC3s were FACS-sorted from SLT and cultured in conditions shown. After 14 d, an equal number of cells from each condition were stimulated for 12 h with IL-12, IL-15, and IL-18 then assessed for ( A-C ) intracellular (n = 3) or ( D ) secreted (n = 4) IFN-γ production. ( A ) Represents an individual donor (CH-223191, ; <t>DMSO,</t> ; FICZ, dashed line), while ( B-D ) depicts the average result from multiple donors, presented as mean ± SEM, * for P
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    Image Search Results


    Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with Graspin (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or DMSO as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P

    Journal: PLoS Genetics

    Article Title: Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

    doi: 10.1371/journal.pgen.1006803

    Figure Lengend Snippet: Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with Graspin (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or DMSO as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P

    Article Snippet: Graspin stock solution was dissolved at 10mM concentration in anhydrous DMSO (Cat# D12345, Life Technology).

    Techniques: Fluorescence, Incubation

    Protocol flowchart. The bilateral common carotid arteries were colligated for 10 min to establish forebrain ischemia followed by reperfusion. SA: salvinorin A; DMSO: dimethyl sulfoxide; nor-BIN: norbinaltorphimine; BCCAO: bilateral common carotid artery occlusion; CSF: cerebrospinal fluid.

    Journal: Brazilian Journal of Medical and Biological Research

    Article Title: Salvinorin A preserves cerebral pial artery autoregulation after forebrain ischemia via the PI3K/AKT/cGMP pathway

    doi: 10.1590/1414-431X20176714

    Figure Lengend Snippet: Protocol flowchart. The bilateral common carotid arteries were colligated for 10 min to establish forebrain ischemia followed by reperfusion. SA: salvinorin A; DMSO: dimethyl sulfoxide; nor-BIN: norbinaltorphimine; BCCAO: bilateral common carotid artery occlusion; CSF: cerebrospinal fluid.

    Article Snippet: The ischemia reperfusion (IR) control group received DMSO (Amresco, USA, 1 µL/kg, iv ) administration immediately after ischemia (n=6).

    Techniques:

    Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Blocking Assay, Modification, Western Blot, Irradiation, Immunofluorescence

    Combined β1 integrin/JNK targeting blocks GBM cell invasion ( A ) Work flow of 3D invasion assays. ( B ) Representative images of indicated GBM cells invading into 3D type I collagen 72 h after treatment with AIIB2/SP600125 (EC50) or control IgG/DMSO. Scale bar, 50 μm. ( C ) Invasion distance of indicated treated GBM cell populations. Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Combined β1 integrin/JNK targeting blocks GBM cell invasion ( A ) Work flow of 3D invasion assays. ( B ) Representative images of indicated GBM cells invading into 3D type I collagen 72 h after treatment with AIIB2/SP600125 (EC50) or control IgG/DMSO. Scale bar, 50 μm. ( C ) Invasion distance of indicated treated GBM cell populations. Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Flow Cytometry

    Dual inhibition of β1 integrin and JNK delays tumor growth and prolongs survival in combination with radiochemotherapy ( A ) Treatment scheme of mice bearing tumors of GS-8_GFP/fLuc stem-like cells. ( B ) Left panel shows representative image of a mouse brain with GS-8_GFP/fLuc tumor. Scale bar, 2 mm. Region 1 and 2 corresponding to middle and right panel magnifications show invading tumor cells (IC) and blood vessel (BV) of GS-8_GFP/fLuc tumors, respectively. Scale bar, 100 μm. ( C ) Representative images from GS-8_GFP/fLuc tumors showing β1 integrin (green), phospho-JNK (T183/Y185) (red) or merge with nuclei (DAPI, blue). Scale bar, 100 μm. ( D ) Gadolinium-enhanced (Gd) T1-weighted magnetic resonance images (MRI) from mice bearing GS-8_GFP/fLuc tumors 24 days after transplantation and β1 integrin/JNK inhibition without or in combination with radiochemotherapy (RCT). Dashed lines delineate tumors. Lower images show luminescence analyses of representative GS-8_GFP/fLuc tumors 24 days after transplantation and indicated treatment. ( E ) GS-8_GFP/fLuc tumor growth time to 100 fold radiance after indicated treatment. Data are mean +/− SEM (6 - 8 mice per group, one-way ANOVA). ( F ) Survival of GS-8_GFP/fLuc mice treated as indicated. Kaplan Meier analysis includes 6 mice IgG/DMSO, 8 mice AIIB2/SP600125, 6 mice IgG/DMSO+RCT, 6 mice AIIB2/SP600125+RCT (two-sided log rank test, p

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Dual inhibition of β1 integrin and JNK delays tumor growth and prolongs survival in combination with radiochemotherapy ( A ) Treatment scheme of mice bearing tumors of GS-8_GFP/fLuc stem-like cells. ( B ) Left panel shows representative image of a mouse brain with GS-8_GFP/fLuc tumor. Scale bar, 2 mm. Region 1 and 2 corresponding to middle and right panel magnifications show invading tumor cells (IC) and blood vessel (BV) of GS-8_GFP/fLuc tumors, respectively. Scale bar, 100 μm. ( C ) Representative images from GS-8_GFP/fLuc tumors showing β1 integrin (green), phospho-JNK (T183/Y185) (red) or merge with nuclei (DAPI, blue). Scale bar, 100 μm. ( D ) Gadolinium-enhanced (Gd) T1-weighted magnetic resonance images (MRI) from mice bearing GS-8_GFP/fLuc tumors 24 days after transplantation and β1 integrin/JNK inhibition without or in combination with radiochemotherapy (RCT). Dashed lines delineate tumors. Lower images show luminescence analyses of representative GS-8_GFP/fLuc tumors 24 days after transplantation and indicated treatment. ( E ) GS-8_GFP/fLuc tumor growth time to 100 fold radiance after indicated treatment. Data are mean +/− SEM (6 - 8 mice per group, one-way ANOVA). ( F ) Survival of GS-8_GFP/fLuc mice treated as indicated. Kaplan Meier analysis includes 6 mice IgG/DMSO, 8 mice AIIB2/SP600125, 6 mice IgG/DMSO+RCT, 6 mice AIIB2/SP600125+RCT (two-sided log rank test, p

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Inhibition, Mouse Assay, Magnetic Resonance Imaging, Transplantation Assay

    β1 integrin/JNK co-targeting interferes with cell cycle regulatory networks ( A ) Hierarchical clustering of altered phosphorylation sites (30% decrease, 50% increase, fold change) from phosphoproteome analysis of U343MG cells 1 h after indicated treatment with AIIB2, JNKi or AIIB2/JNKi (EC10) normalized to controls (percentage of phosphorylation site changes is shown on the right). ( B ) Percentage of phospho-sites showing 30% decreased and 50% increased phosphorylation upon indicated treatment among the 606 phosphorylations sited investigated in the phosphoproteome analysis. ( C ) Venn diagram analysis of altered phosphosites from (A). ( D ) Functional classification of altered proteins after treatment with AIIB2/SP600125 (EC10) in comparison to the IgG/DMSO controls. Enrichment of genes in signaling pathway: # p

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: β1 integrin/JNK co-targeting interferes with cell cycle regulatory networks ( A ) Hierarchical clustering of altered phosphorylation sites (30% decrease, 50% increase, fold change) from phosphoproteome analysis of U343MG cells 1 h after indicated treatment with AIIB2, JNKi or AIIB2/JNKi (EC10) normalized to controls (percentage of phosphorylation site changes is shown on the right). ( B ) Percentage of phospho-sites showing 30% decreased and 50% increased phosphorylation upon indicated treatment among the 606 phosphorylations sited investigated in the phosphoproteome analysis. ( C ) Venn diagram analysis of altered phosphosites from (A). ( D ) Functional classification of altered proteins after treatment with AIIB2/SP600125 (EC10) in comparison to the IgG/DMSO controls. Enrichment of genes in signaling pathway: # p

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Functional Assay

    Inhibition of β1 integrin and JNK enhances G2/M cell cycle arrest ( A ) Western blot analysis of indicated proteins and phosphorylation sites from whole cell lysates of U343MG cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative blots are shown. ( B ) Quantification of ATM (S1981) and Cdc25A (S216) phosphorylation and p53 expression shown in (A). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls. Results are mean +/− SEM ( n = 3, t -test). ( C ) Flow cytometric cell cycle analysis (BrdU, propidium iodide) of U343MG cells 24 h after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative dot blots are shown. ( D ) Quantification of flow cytometric analysis from (C) showing distribution of treated GBM cells into G1/G0, S and G2/M phase of the cell cycle. Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Inhibition of β1 integrin and JNK enhances G2/M cell cycle arrest ( A ) Western blot analysis of indicated proteins and phosphorylation sites from whole cell lysates of U343MG cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative blots are shown. ( B ) Quantification of ATM (S1981) and Cdc25A (S216) phosphorylation and p53 expression shown in (A). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls. Results are mean +/− SEM ( n = 3, t -test). ( C ) Flow cytometric cell cycle analysis (BrdU, propidium iodide) of U343MG cells 24 h after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative dot blots are shown. ( D ) Quantification of flow cytometric analysis from (C) showing distribution of treated GBM cells into G1/G0, S and G2/M phase of the cell cycle. Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Inhibition, Western Blot, Irradiation, Expressing, Flow Cytometry, Cell Cycle Assay

    Co-targeting of β1 integrin and JNK sensitizes GBM cells to radiotherapy ( A ) Workflow of GBM sphere formation and clonogenic survival assay. ( B ) Relative sphere formation and basal surviving fraction of GBM stem-like cells (GS-8), patient-derived GBM cultures (DK32, DK41) and GBM cell lines (U343MG, DD-T4) upon treatment with AIIB2/SP600125 (EC10, EC50) or controls (IgG, DMSO). ( C ) Relative sphere formation and clonogenic survival upon treatment with AIIB2/SP600125 (EC10, EC50) and X-ray irradiation (2, 4, 6 Gy) (controls are IgG and DMSO). (B, C) Results are mean +/− SEM ( n = 3–4, t -test). ( D ) Western blot analysis of β1 integrin, phospho-cJun (S63), cJun and β-actin of whole cell lysates from indicated GBM cells treated as indicated with AIIB2 (10 μg/ml), SP600125 (EC10), IgG control (10 μg/ml) and DMSO. Fold change is calculated by normalization to β-actin and IgG/DMSO controls according to representative blots.

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Co-targeting of β1 integrin and JNK sensitizes GBM cells to radiotherapy ( A ) Workflow of GBM sphere formation and clonogenic survival assay. ( B ) Relative sphere formation and basal surviving fraction of GBM stem-like cells (GS-8), patient-derived GBM cultures (DK32, DK41) and GBM cell lines (U343MG, DD-T4) upon treatment with AIIB2/SP600125 (EC10, EC50) or controls (IgG, DMSO). ( C ) Relative sphere formation and clonogenic survival upon treatment with AIIB2/SP600125 (EC10, EC50) and X-ray irradiation (2, 4, 6 Gy) (controls are IgG and DMSO). (B, C) Results are mean +/− SEM ( n = 3–4, t -test). ( D ) Western blot analysis of β1 integrin, phospho-cJun (S63), cJun and β-actin of whole cell lysates from indicated GBM cells treated as indicated with AIIB2 (10 μg/ml), SP600125 (EC10), IgG control (10 μg/ml) and DMSO. Fold change is calculated by normalization to β-actin and IgG/DMSO controls according to representative blots.

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Clonogenic Cell Survival Assay, Derivative Assay, Irradiation, Western Blot

    Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% DMSO) showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor SU5402 showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.

    Journal: Frontiers in Neuroanatomy

    Article Title: Origin and Migration of Olfactory Cajal-Retzius Cells

    doi: 10.3389/fnana.2017.00097

    Figure Lengend Snippet: Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% DMSO) showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor SU5402 showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.

    Article Snippet: Serum was replaced every 12 h. For FGF inhibition experiments, serum was supplemented with 10 μM of SU5402 (572630, Calbiochem, Billerica, MA, USA) dissolved in DMSO (9224–01 J.T.Baker Center Valley, PA, USA) with an equivalent volume of DMSO used in control cultures.

    Techniques: Derivative Assay, In Situ Hybridization, Labeling, Expressing, Migration, Cell Culture, Knock-Out

    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or DMSO for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P

    Journal: World Journal of Gastroenterology

    Article Title: Sodium chloride exacerbates dextran sulfate sodium-induced colitis by tuning proinflammatory and antiinflammatory lamina propria mononuclear cells through p38/MAPK pathway in mice

    doi: 10.3748/wjg.v24.i16.1779

    Figure Lengend Snippet: NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or DMSO for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P

    Article Snippet: Isolated LPMCs were cultured at a concentration of 5 × 106 cells/mL for 24 h, after which the culture supernatants were collected and cytokine levels were analyzed by enzyme-linked immunosorbent assay (ELISA) or were stimulated using different NaCl concentrations (5, 10, 20, 40, 60 or 80 mmol/L) in the presence of 100 ng/mL LPS (Sigma, United States) and 20 ng/mL IFN-γ (Sigma) with SB20358 (p38 inhibitor) or DMSO (ST038; Beyotime) for 24 h. The cells were detected by western blot (WB) or real time-PCR (RT-PCR).

    Techniques: Western Blot, Expressing, Reverse Transcription Polymerase Chain Reaction

    Effects of the antioxidant DMSO and neutrophil depletion on upregulation of P-selectin in IgG immune complex-induced lung injury ( A ) and in CVF-induced lung injury ( B ). For each column, n ≥ 4.

    Journal: The American Journal of Pathology

    Article Title: Differing Patterns of P-Selectin Expression in Lung Injury

    doi:

    Figure Lengend Snippet: Effects of the antioxidant DMSO and neutrophil depletion on upregulation of P-selectin in IgG immune complex-induced lung injury ( A ) and in CVF-induced lung injury ( B ). For each column, n ≥ 4.

    Article Snippet: To assess the extent to which upregulation of lung vascular P-selectin may be related to requirement for oxidants, 1.0 ml of DMSO (Burdick & Jackson Laboratories, Inc., Muskegon, MI) was injected intraperitoneally 10 minutes before initiation of lung inflammatory reactions.

    Techniques:

    Immunofluorescence staining with phalloidin of U2OS cells treated with cytochalasans. ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM DMSO (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.

    Journal: Biomolecules

    Article Title: The Effect of Cytochalasans on the Actin Cytoskeleton of Eukaryotic Cells and Preliminary Structure–Activity Relationships

    doi: 10.3390/biom9020073

    Figure Lengend Snippet: Immunofluorescence staining with phalloidin of U2OS cells treated with cytochalasans. ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM DMSO (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.

    Article Snippet: For treatment of the cells, the cytochalasans were dissolved in DMSO (Carl Roth GmbH, Karlsruhe, Germany).

    Techniques: Immunofluorescence, Staining, Negative Control

    Recruitment of HDAC2 and PAX5 to the promoters of target genes. (A) Flag-tagged PAX5 was overexpressed in HEK293T cells. Extracts were immunoprecipitated with anti-Flag antibodies. Associated proteins were eluted, resolved by SDS-PAGE, and immunoblotted with anti-Flag and anti-HDAC2 antibodies. (B) Differential changes in interaction between HDAC2 and PAX5 48 hrs after treatment with 32 nM TPA were determined by IP. Extracts from TPA- or DMSO-treated HL-60 cells were immunoprecipitated with anti-PAX5 antibodies. HDAC2 that interacted with PAX5 in HL-60 cells was eluted and immunoblotted with a HDAC2 antibody. (C) The mRNA levels of atypically active genes in PAX5 -depleted HL-60 cells were determined by qPCR. PAX5 protein level was detected by western blotting. These data were normalized by GAPDH. (D) HEK293T cells were co-transfected with pCMV-Flag-PAX5 and pGL3.0- IL10RA or pGL3.0- RGCC promoters. Luciferase activities were measured 48 hrs after transfection, and normalized to that of β-galactosidase. (C–D) All results represent at least three independent experiments (± SEMs). * P

    Journal: PLoS ONE

    Article Title: Deacetylase activity-independent transcriptional activation by HDAC2 during TPA-induced HL-60 cell differentiation

    doi: 10.1371/journal.pone.0202935

    Figure Lengend Snippet: Recruitment of HDAC2 and PAX5 to the promoters of target genes. (A) Flag-tagged PAX5 was overexpressed in HEK293T cells. Extracts were immunoprecipitated with anti-Flag antibodies. Associated proteins were eluted, resolved by SDS-PAGE, and immunoblotted with anti-Flag and anti-HDAC2 antibodies. (B) Differential changes in interaction between HDAC2 and PAX5 48 hrs after treatment with 32 nM TPA were determined by IP. Extracts from TPA- or DMSO-treated HL-60 cells were immunoprecipitated with anti-PAX5 antibodies. HDAC2 that interacted with PAX5 in HL-60 cells was eluted and immunoblotted with a HDAC2 antibody. (C) The mRNA levels of atypically active genes in PAX5 -depleted HL-60 cells were determined by qPCR. PAX5 protein level was detected by western blotting. These data were normalized by GAPDH. (D) HEK293T cells were co-transfected with pCMV-Flag-PAX5 and pGL3.0- IL10RA or pGL3.0- RGCC promoters. Luciferase activities were measured 48 hrs after transfection, and normalized to that of β-galactosidase. (C–D) All results represent at least three independent experiments (± SEMs). * P

    Article Snippet: For differentiation, HL-60 cells were seeded in a 100-mm plate at a concentration of 1 × 106 per mL and treated with 32 nM TPA (Sigma Aldrich) or DMSO (Duchefa).

    Techniques: Immunoprecipitation, SDS Page, Real-time Polymerase Chain Reaction, Western Blot, Transfection, Luciferase

    HDAC2 was recruited to the promoters of atypically active genes and induced transcription during HL-60 cell differentiation. (A–B) HL-60 cells were treated with TPA (32 nM) or DMSO for 48 hrs. (A) The occupancies of AcH3, H3K27me3, HDAC2, and RNA Pol II at the promoters of atypically active genes, typically active and repressive genes during HL-60 cell differentiation were analyzed. The data were normalized by input. These results are shown as means ± SDs (n = 3). (B) The differential changes in expression of the genes in TPA-treated HL-60 cells were confirmed by qPCR. (C) The mRNA levels of atypically active genes in HDAC2 -depleted HL-60 cells were analyzed using qPCR. Knockdown of HDAC2 was confirmed by western blotting. (B–C) These data were normalized by GAPDH. All results represent at least three independent experiments (± SEMs). * P

    Journal: PLoS ONE

    Article Title: Deacetylase activity-independent transcriptional activation by HDAC2 during TPA-induced HL-60 cell differentiation

    doi: 10.1371/journal.pone.0202935

    Figure Lengend Snippet: HDAC2 was recruited to the promoters of atypically active genes and induced transcription during HL-60 cell differentiation. (A–B) HL-60 cells were treated with TPA (32 nM) or DMSO for 48 hrs. (A) The occupancies of AcH3, H3K27me3, HDAC2, and RNA Pol II at the promoters of atypically active genes, typically active and repressive genes during HL-60 cell differentiation were analyzed. The data were normalized by input. These results are shown as means ± SDs (n = 3). (B) The differential changes in expression of the genes in TPA-treated HL-60 cells were confirmed by qPCR. (C) The mRNA levels of atypically active genes in HDAC2 -depleted HL-60 cells were analyzed using qPCR. Knockdown of HDAC2 was confirmed by western blotting. (B–C) These data were normalized by GAPDH. All results represent at least three independent experiments (± SEMs). * P

    Article Snippet: For differentiation, HL-60 cells were seeded in a 100-mm plate at a concentration of 1 × 106 per mL and treated with 32 nM TPA (Sigma Aldrich) or DMSO (Duchefa).

    Techniques: Cell Differentiation, Expressing, Real-time Polymerase Chain Reaction, Western Blot

    Genome-wide distribution profiles of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells. (A) Heat map analysis showing AcH3, RNA Pol II, HDAC2, and H3K27me3 occupancies covering ± 3 kb region centered over each peak in DMSO- or TPA-treated HL-60 cells. The same color scales (white, no enrichment; red, high enrichment) were used for all data sets (upper panel). Merged profiles show each ChIP-seq signal around the TSS in DMSO- or TPA-treated HL-60 cells (lower panel) (B) Pie charts illustrate the genomic locations of AcH3, RNA Pol II, HDAC2, and H3K27me3 binding sites in TPA-treated HL-60 cells. (C) An area-proportional Venn diagram shows the overlap between AcH3, RNA Pol II, HDAC2, and H3K27me3 enrichment in TPA-treated HL-60 cells based on ChIP-seq data. (D) A heat map represents the binding profiles of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells at the indicated target genes (± 3 kb around the TSSs). The same color scales (white, no enrichment; red, high enrichment) were used for all data sets. (E) ChIP-seq tracks of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells along the AHNAK , USP13 , and SLC2A3 loci.

    Journal: PLoS ONE

    Article Title: Deacetylase activity-independent transcriptional activation by HDAC2 during TPA-induced HL-60 cell differentiation

    doi: 10.1371/journal.pone.0202935

    Figure Lengend Snippet: Genome-wide distribution profiles of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells. (A) Heat map analysis showing AcH3, RNA Pol II, HDAC2, and H3K27me3 occupancies covering ± 3 kb region centered over each peak in DMSO- or TPA-treated HL-60 cells. The same color scales (white, no enrichment; red, high enrichment) were used for all data sets (upper panel). Merged profiles show each ChIP-seq signal around the TSS in DMSO- or TPA-treated HL-60 cells (lower panel) (B) Pie charts illustrate the genomic locations of AcH3, RNA Pol II, HDAC2, and H3K27me3 binding sites in TPA-treated HL-60 cells. (C) An area-proportional Venn diagram shows the overlap between AcH3, RNA Pol II, HDAC2, and H3K27me3 enrichment in TPA-treated HL-60 cells based on ChIP-seq data. (D) A heat map represents the binding profiles of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells at the indicated target genes (± 3 kb around the TSSs). The same color scales (white, no enrichment; red, high enrichment) were used for all data sets. (E) ChIP-seq tracks of AcH3, RNA Pol II, HDAC2, and H3K27me3 in TPA-treated HL-60 cells along the AHNAK , USP13 , and SLC2A3 loci.

    Article Snippet: For differentiation, HL-60 cells were seeded in a 100-mm plate at a concentration of 1 × 106 per mL and treated with 32 nM TPA (Sigma Aldrich) or DMSO (Duchefa).

    Techniques: Genome Wide, Chromatin Immunoprecipitation, Binding Assay

    ROCK localization to medioapical foci requires the actin cytoskeleton and Dia ( A ) Apical views of ventral furrow cells in embryos expressing ubi-GFP::ROCK, Gap43::mCherry (Membrane) or GFP::ROCK, Utr::mCherry (F-actin) and injected with DMSO after 0 sec time point. ( B ) Same as (A) but with Latrunculin B injection. Disrupted ROCK polarity (white outline and arrow). ( C ) Apical ROCK in wild-type and maternal dia 5 .

    Journal: Developmental cell

    Article Title: Apical sarcomere-like actomyosin contracts nonmuscle Drosophila epithelial cells

    doi: 10.1016/j.devcel.2016.09.023

    Figure Lengend Snippet: ROCK localization to medioapical foci requires the actin cytoskeleton and Dia ( A ) Apical views of ventral furrow cells in embryos expressing ubi-GFP::ROCK, Gap43::mCherry (Membrane) or GFP::ROCK, Utr::mCherry (F-actin) and injected with DMSO after 0 sec time point. ( B ) Same as (A) but with Latrunculin B injection. Disrupted ROCK polarity (white outline and arrow). ( C ) Apical ROCK in wild-type and maternal dia 5 .

    Article Snippet: Embryos were injected with dsRNA in water, or profilin:actin-488 (10 μM each) in G-Buffer (2mM Tris pH 8, 0.2 mM ATP, 0.5 mM DTT, 0.1 mM CaCl2 , 1 mM NaN3) , or Y-27632 (50 mM) in water, Latrunculin B (5 mg/mL) in DMSO, or Cytochalasin D (0.25 mg/mL) in DMSO (Enzo Life Sciences, Farmingdale, NY).

    Techniques: Expressing, Injection, Size-exclusion Chromatography

    Knockdown of Bfl-1 by shRNA sensitizes HTLV-1-infected C91PL T-cells to ABT-737- or etoposide-induced apoptosis. A , effect of ABT-737 on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle (DMSO) or ABT-737. After 2 days, percentages of cell death (PI + ) were measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. B , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later exposed to different concentrations of DMSO or ABT-737 for 2 additional days. Cell death was assessed by PI staining and measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. C , effect of etoposide on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle (DMSO) or etoposide. After 2 days, the percentages of cell death were measured as in A . Results are expressed as mean ± S.D. of three independent experiments. D , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later were exposed to different concentrations of etoposide for 2 additional days. Apoptosis was assessed by anti-active caspase-3 Ab staining and measured by flow cytometry. Results are from one representative experiment of two.

    Journal: The Journal of Biological Chemistry

    Article Title: Tax Protein-induced Expression of Antiapoptotic Bfl-1 Protein Contributes to Survival of Human T-cell Leukemia Virus Type 1 (HTLV-1)-infected T-cells *

    doi: 10.1074/jbc.M112.340992

    Figure Lengend Snippet: Knockdown of Bfl-1 by shRNA sensitizes HTLV-1-infected C91PL T-cells to ABT-737- or etoposide-induced apoptosis. A , effect of ABT-737 on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle (DMSO) or ABT-737. After 2 days, percentages of cell death (PI + ) were measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. B , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later exposed to different concentrations of DMSO or ABT-737 for 2 additional days. Cell death was assessed by PI staining and measured by flow cytometry. Results are expressed as means ± S.D. of three independent experiments. C , effect of etoposide on HTLV-1-infected C91PL T-cell death. Cells were treated with different concentrations of vehicle (DMSO) or etoposide. After 2 days, the percentages of cell death were measured as in A . Results are expressed as mean ± S.D. of three independent experiments. D , C91PL cells were transduced with Bfl-1 or scramble Bfl-1 Ctl shRNA and 5 days later were exposed to different concentrations of etoposide for 2 additional days. Apoptosis was assessed by anti-active caspase-3 Ab staining and measured by flow cytometry. Results are from one representative experiment of two.

    Article Snippet: T-cell lines (4 × 105 /ml) were cultured in the absence or presence of various concentrations of DMSO, ABT-737 (Euromedex, Selleck Chem) ( ) or etoposide (Sigma).

    Techniques: shRNA, Infection, Flow Cytometry, Cytometry, Transduction, CTL Assay, Staining

    Time to complete transmigration. (A) Transmigration time (through endothelium on 5 kPa gel) for all neutrophils, from when the first protrusion is seen under the endothelium, to complete transmigration (except tails for the cases of blebbistain and ML-7), for all treatments. Bars represent mean ± SEM of pooled data from 3 independent experiments (N = 61, 103, 75, 182, 32 for DMSO, blebbistatin, ML-7, nocodazole, and taxol, respectively). ** indicates P

    Journal: PLoS ONE

    Article Title: Human Neutrophil Cytoskeletal Dynamics and Contractility Actively Contribute to Trans-Endothelial Migration

    doi: 10.1371/journal.pone.0061377

    Figure Lengend Snippet: Time to complete transmigration. (A) Transmigration time (through endothelium on 5 kPa gel) for all neutrophils, from when the first protrusion is seen under the endothelium, to complete transmigration (except tails for the cases of blebbistain and ML-7), for all treatments. Bars represent mean ± SEM of pooled data from 3 independent experiments (N = 61, 103, 75, 182, 32 for DMSO, blebbistatin, ML-7, nocodazole, and taxol, respectively). ** indicates P

    Article Snippet: Drugs included DMSO (Fisher Scientific) as the vehicle control, blebbistatin (15 µM, 5 minutes; Sigma Aldrich) to inhibit myosin II, ML-7 (15 µM, 8 minutes; Sigma Aldrich) to inhibit MLCK, nocodazole (5 µM, 5 minutes; Sigma Aldrich) to inhibit microtubule polymerization, taxol (1 µM, 30 minutes; Sigma Aldrich) to stabilize microtubules, jasplakinolide (1 µM, 5 minutes; Calbiochem) to stabilize and polymerize actin, and latrunculin-A (1 µM, 30 minutes; Sigma Aldrich) to disrupt actin.

    Techniques: Transmigration Assay

    Incomplete transmigration upon inhibition of contractility. (A) A representative phase contrast sequence of a DMSO-treated neutrophil transmigrating through the endothelium on a 5 kPa gel. The neutrophil on top of the endothelium appears bright white in phase contrast microscopy, while the portion that has already transmigrated through the endothelium appears dark (white arrow). (B) A representative phase contrast sequence of blebbistatin-treated neutrophils transmigrating through the endothelium. Black arrowhead points to the first cell of interest. White arrows point to the darkened portion of the neutrophil under the endothelium. White arrowheads point to the portion of the tail that remains above the endothelium for several minutes after the rest of the neutrophil has transmigrated. Gray arrowheads point to another neutrophil that attempts to transmigrate, but does not ever fully succeed. For panels A and B, time = 0:00 (in minutes∶seconds format) in the upper right corner of the first image in each sequence indicates the time of the frame just before transmigration begins. (C) An example of an ML-7-treated neutrophil (indicated by black arrowhead) that makes two attempts at transmigration. A protrusion is sent beneath the endothelium (designated by white arrow at 0:30), but the neutrophil does not transmigrate on this attempt. Later, at time = 2:50 the neutrophil begins to transmigrate again (designated by white arrows in images 2:50–3:10). Similar to blebbistatin, a tail is left behind (white arrowhead at 3:10), but full transmigration, including the tail, occurs by time = 4:30. Scale bar for the first image in each sequence is 20 µm. (D) A time sequence is shown for a blebbistatin-treated neutrophil that transmigrates, leaves a tail behind, and later detaches from the tail. Time after plating neutrophils is shown in the upper right corner of each image in minutes∶seconds fomat. Scale bar in panel D is 20 µm and applies to all images in panel D.

    Journal: PLoS ONE

    Article Title: Human Neutrophil Cytoskeletal Dynamics and Contractility Actively Contribute to Trans-Endothelial Migration

    doi: 10.1371/journal.pone.0061377

    Figure Lengend Snippet: Incomplete transmigration upon inhibition of contractility. (A) A representative phase contrast sequence of a DMSO-treated neutrophil transmigrating through the endothelium on a 5 kPa gel. The neutrophil on top of the endothelium appears bright white in phase contrast microscopy, while the portion that has already transmigrated through the endothelium appears dark (white arrow). (B) A representative phase contrast sequence of blebbistatin-treated neutrophils transmigrating through the endothelium. Black arrowhead points to the first cell of interest. White arrows point to the darkened portion of the neutrophil under the endothelium. White arrowheads point to the portion of the tail that remains above the endothelium for several minutes after the rest of the neutrophil has transmigrated. Gray arrowheads point to another neutrophil that attempts to transmigrate, but does not ever fully succeed. For panels A and B, time = 0:00 (in minutes∶seconds format) in the upper right corner of the first image in each sequence indicates the time of the frame just before transmigration begins. (C) An example of an ML-7-treated neutrophil (indicated by black arrowhead) that makes two attempts at transmigration. A protrusion is sent beneath the endothelium (designated by white arrow at 0:30), but the neutrophil does not transmigrate on this attempt. Later, at time = 2:50 the neutrophil begins to transmigrate again (designated by white arrows in images 2:50–3:10). Similar to blebbistatin, a tail is left behind (white arrowhead at 3:10), but full transmigration, including the tail, occurs by time = 4:30. Scale bar for the first image in each sequence is 20 µm. (D) A time sequence is shown for a blebbistatin-treated neutrophil that transmigrates, leaves a tail behind, and later detaches from the tail. Time after plating neutrophils is shown in the upper right corner of each image in minutes∶seconds fomat. Scale bar in panel D is 20 µm and applies to all images in panel D.

    Article Snippet: Drugs included DMSO (Fisher Scientific) as the vehicle control, blebbistatin (15 µM, 5 minutes; Sigma Aldrich) to inhibit myosin II, ML-7 (15 µM, 8 minutes; Sigma Aldrich) to inhibit MLCK, nocodazole (5 µM, 5 minutes; Sigma Aldrich) to inhibit microtubule polymerization, taxol (1 µM, 30 minutes; Sigma Aldrich) to stabilize microtubules, jasplakinolide (1 µM, 5 minutes; Calbiochem) to stabilize and polymerize actin, and latrunculin-A (1 µM, 30 minutes; Sigma Aldrich) to disrupt actin.

    Techniques: Transmigration Assay, Inhibition, Sequencing, Microscopy

    Fraction of neutrophils that transmigrate. Neutrophils were pretreated with DMSO (vehicle control), blebbistatin (“Bleb”; to inhibit myosin II), ML-7 (to inhibit myosin light chain kinase), nocodazole (“Noc”; to inhibit microtubule polymerization), taxol (“Tax”; to stabilize microtubules), latrunculin-A (“Lat-A”; to inhibit actin polymerization) or jasplakinolide (“Jasp”; to inhibit actin depolymerization) and plated onto a TNF-α-activated HUVEC monolayer on a 5 kPa polyacrylamide gel. Bars represent mean ± SEM of 3–4 independent experiments. * indicates P

    Journal: PLoS ONE

    Article Title: Human Neutrophil Cytoskeletal Dynamics and Contractility Actively Contribute to Trans-Endothelial Migration

    doi: 10.1371/journal.pone.0061377

    Figure Lengend Snippet: Fraction of neutrophils that transmigrate. Neutrophils were pretreated with DMSO (vehicle control), blebbistatin (“Bleb”; to inhibit myosin II), ML-7 (to inhibit myosin light chain kinase), nocodazole (“Noc”; to inhibit microtubule polymerization), taxol (“Tax”; to stabilize microtubules), latrunculin-A (“Lat-A”; to inhibit actin polymerization) or jasplakinolide (“Jasp”; to inhibit actin depolymerization) and plated onto a TNF-α-activated HUVEC monolayer on a 5 kPa polyacrylamide gel. Bars represent mean ± SEM of 3–4 independent experiments. * indicates P

    Article Snippet: Drugs included DMSO (Fisher Scientific) as the vehicle control, blebbistatin (15 µM, 5 minutes; Sigma Aldrich) to inhibit myosin II, ML-7 (15 µM, 8 minutes; Sigma Aldrich) to inhibit MLCK, nocodazole (5 µM, 5 minutes; Sigma Aldrich) to inhibit microtubule polymerization, taxol (1 µM, 30 minutes; Sigma Aldrich) to stabilize microtubules, jasplakinolide (1 µM, 5 minutes; Calbiochem) to stabilize and polymerize actin, and latrunculin-A (1 µM, 30 minutes; Sigma Aldrich) to disrupt actin.

    Techniques:

    Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater (ASW), 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% DMSO (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Distinct Roles of Soluble and Transmembrane Adenylyl Cyclases in the Regulation of Flagellar Motility in Ciona Sperm

    doi: 10.3390/ijms150813192

    Figure Lengend Snippet: Effects of AC inhibitors on SAAF-, valinomycin (Val)- or theophylline (Theo)-induced protein phosphorylation by protein kinase (PKA). CBB-stained pattern and corresponding western blot with anti-PKA-substrate antibody were shown for sperm treated by artificial seawater (ASW), 100 nM SAAF, 10 nM valinomycin or 1 mM theophylline with 0.5% DMSO (control), 100 μM MDL12330A or 10 μM KH-7. Data obtained in ASW ( top ) and in CaFSW ( bottom ) are shown. The percentage of polyacrylamide in the separating gel is 10%. Proteins with significant increase in phosphorylation by SAAF-activation are indicated by asterisks in the lane of sperm sample activated by SAAF in ASW. Those showing decreased phospholylation by KH-7 in ASW are marked in green and others are in red. Data show a typical result from three independent experiments.

    Article Snippet: Semen was suspended in 2000 volumes of ASW containing DMSO (WAKO, Osaka, Japan) or inhibitors and incubated for 3 min, and SAAF (final concentration 100 nM) was added to the suspension.

    Techniques: Staining, Western Blot, Activation Assay

    UVB-activated caspase-9 is inhibited by CoQ10. A–F , Immunocytochemistry of cleaved caspase-9. Number of caspase-9 positive cells increased after UVB irradiation with or without 0.1% DMSO ( B,C ) compared to control ( A ). Pretreatment with CoQ10 at 0.01, 0.1, or 1 M significantly reduced the number of caspase-9 positive cells ( D–F ). Green color represents cleaved caspase-9 staining and blue color denotes DAPI stained nuclei. Insert in Figure 3C shows cytosolic localization of cleaved caspase-9. G , western blotting showing full length (49 KD) and cleaved (39 KD) caspase-9 in control, UVB, and CoQ10 treated cells. Total and cleaved caspase-9 increased after UVB and CoQ10 pretreatment reduced both total and cleaved caspase-9 in the cytosolic fraction. H , Number of cleaved caspase-9 positive cells per high magnification field counted from 3 independent immunocytochemistry experiments, each performed in triplicate. # p

    Journal: International Journal of Molecular Sciences

    Article Title: Coenzyme Q10 Ameliorates Ultraviolet B Irradiation Induced Cell Death Through Inhibition of Mitochondrial Intrinsic Cell Death Pathway

    doi: 10.3390/ijms12118302

    Figure Lengend Snippet: UVB-activated caspase-9 is inhibited by CoQ10. A–F , Immunocytochemistry of cleaved caspase-9. Number of caspase-9 positive cells increased after UVB irradiation with or without 0.1% DMSO ( B,C ) compared to control ( A ). Pretreatment with CoQ10 at 0.01, 0.1, or 1 M significantly reduced the number of caspase-9 positive cells ( D–F ). Green color represents cleaved caspase-9 staining and blue color denotes DAPI stained nuclei. Insert in Figure 3C shows cytosolic localization of cleaved caspase-9. G , western blotting showing full length (49 KD) and cleaved (39 KD) caspase-9 in control, UVB, and CoQ10 treated cells. Total and cleaved caspase-9 increased after UVB and CoQ10 pretreatment reduced both total and cleaved caspase-9 in the cytosolic fraction. H , Number of cleaved caspase-9 positive cells per high magnification field counted from 3 independent immunocytochemistry experiments, each performed in triplicate. # p

    Article Snippet: CoQ10, was purchased from Sigma-Aldrich (USA), dissolved in DMSO (Mediatech, USA) and diluted in culture medium.

    Techniques: Immunocytochemistry, Irradiation, Staining, Western Blot

    Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% DMSO (vehicle), 0.25 µM calyculin (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P

    Journal: PLoS ONE

    Article Title: Phosphorylation and Transport in the Na-K-2Cl Cotransporters, NKCC1 and NKCC2A, Compared in HEK-293 Cells

    doi: 10.1371/journal.pone.0017992

    Figure Lengend Snippet: Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% DMSO (vehicle), 0.25 µM calyculin (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P

    Article Snippet: 4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP1, Enzo Life Sciences, Farmingdale, NY), genistein (Sigma-Aldrich), calyculin A (Enzo Life Sciences) were dissolved in DMSO (Merck) whereas ouabain (Sigma-Aldrich) and bumetanide (Leo Laboratories, Ballerup, Denmark) were dissolved in water.

    Techniques: Incubation

    Effects of the specific BMP inhibitor K02288 on bone mineralization. Alizarine red staining of 5 dpf larvae previously treated at 2 ( B , D ) or 3 dpf ( F ) during 24 h with K02288 10 (B) and 20 µM (D,F). Control embryos ( A , C , E ) were treated with DMSO. c: cleithrum; en: entopterygoid; o: operculum; p: parasphenoid. Scale bar: 200 µM.

    Journal: Molecules

    Article Title: BMP Signaling Regulates Bone Morphogenesis in Zebrafish through Promoting Osteoblast Function as Assessed by Their Nitric Oxide Production

    doi: 10.3390/molecules20057586

    Figure Lengend Snippet: Effects of the specific BMP inhibitor K02288 on bone mineralization. Alizarine red staining of 5 dpf larvae previously treated at 2 ( B , D ) or 3 dpf ( F ) during 24 h with K02288 10 (B) and 20 µM (D,F). Control embryos ( A , C , E ) were treated with DMSO. c: cleithrum; en: entopterygoid; o: operculum; p: parasphenoid. Scale bar: 200 µM.

    Article Snippet: Inhibition of Bmp signaling 10 mM stock solution of dorsomorphin (CAS No: 1219168-18-9) (Sigma-Aldrich), K02288 (CAS No: 1431985-92-0) (Tocris Bioscience® , Lille, France) was diluted in DMSO (Merck Chemicals, Overijse, Belgium).

    Techniques: Staining

    Effects of dorsomorphin ( A – F ) and K02288 ( G – L ) on NO production and osterix expression. (A,B,G,H) Nitric oxide labelling by DAF-FM DA of 5 dpf Tg (osx:mcherry) larvae previously treated during 24 h with 100 µM dorsomorphin (B) or 20 µM K02288 (H) at 2 dpf. (C,D,I,J) mCherry red fluorescence of 5 dpf Tg (osx:mcherry) larvae previously treated during 24 h with 100 µM dorsomorphin (D) or 20 µM K02288 (H) at 2 dpf. Control embryos (A,C,G,I) were treated with DMSO. c: cleithrum; en: entopterygoid; o: operculum; p: parasphenoid. Scale bar: 200 µM. (E,F,K,L) Statistical analysis of replicate experiments investigating the effect of dorsomorphin (E, F) or K02288 (K,L) on nitric oxide (E,K) or mCherry (F, L) detection. *** indicates p -value

    Journal: Molecules

    Article Title: BMP Signaling Regulates Bone Morphogenesis in Zebrafish through Promoting Osteoblast Function as Assessed by Their Nitric Oxide Production

    doi: 10.3390/molecules20057586

    Figure Lengend Snippet: Effects of dorsomorphin ( A – F ) and K02288 ( G – L ) on NO production and osterix expression. (A,B,G,H) Nitric oxide labelling by DAF-FM DA of 5 dpf Tg (osx:mcherry) larvae previously treated during 24 h with 100 µM dorsomorphin (B) or 20 µM K02288 (H) at 2 dpf. (C,D,I,J) mCherry red fluorescence of 5 dpf Tg (osx:mcherry) larvae previously treated during 24 h with 100 µM dorsomorphin (D) or 20 µM K02288 (H) at 2 dpf. Control embryos (A,C,G,I) were treated with DMSO. c: cleithrum; en: entopterygoid; o: operculum; p: parasphenoid. Scale bar: 200 µM. (E,F,K,L) Statistical analysis of replicate experiments investigating the effect of dorsomorphin (E, F) or K02288 (K,L) on nitric oxide (E,K) or mCherry (F, L) detection. *** indicates p -value

    Article Snippet: Inhibition of Bmp signaling 10 mM stock solution of dorsomorphin (CAS No: 1219168-18-9) (Sigma-Aldrich), K02288 (CAS No: 1431985-92-0) (Tocris Bioscience® , Lille, France) was diluted in DMSO (Merck Chemicals, Overijse, Belgium).

    Techniques: Expressing, Fluorescence

    ( A – D ) Effects of BMP inhibitor treatment at 2–3 dpf on cartilage formation. Alcian blue staining of 5 dpf larvae previously treated at 2 dpf during 24 h with 100 µM dorsomorphin (B) or 20 µM K02288 (D). Control embryos (A,C) were treated with DMSO; ( E – H ) In situ hybridization using the sox9a probe. No difference in cartilage formation was observed between control (E,G) and treated (F,H). cb 1–4: ceratobranchial ray 1 to 4; ch: ceratohyal; mk: Meckel’s cartilage. Scale bar: 200 µM.

    Journal: Molecules

    Article Title: BMP Signaling Regulates Bone Morphogenesis in Zebrafish through Promoting Osteoblast Function as Assessed by Their Nitric Oxide Production

    doi: 10.3390/molecules20057586

    Figure Lengend Snippet: ( A – D ) Effects of BMP inhibitor treatment at 2–3 dpf on cartilage formation. Alcian blue staining of 5 dpf larvae previously treated at 2 dpf during 24 h with 100 µM dorsomorphin (B) or 20 µM K02288 (D). Control embryos (A,C) were treated with DMSO; ( E – H ) In situ hybridization using the sox9a probe. No difference in cartilage formation was observed between control (E,G) and treated (F,H). cb 1–4: ceratobranchial ray 1 to 4; ch: ceratohyal; mk: Meckel’s cartilage. Scale bar: 200 µM.

    Article Snippet: Inhibition of Bmp signaling 10 mM stock solution of dorsomorphin (CAS No: 1219168-18-9) (Sigma-Aldrich), K02288 (CAS No: 1431985-92-0) (Tocris Bioscience® , Lille, France) was diluted in DMSO (Merck Chemicals, Overijse, Belgium).

    Techniques: Staining, In Situ Hybridization

    Inhibition of DOX or RES on proliferation of MCF-7/DOX (DOX-resistant cell line) and MCF-7/sensitive (s) cells. MCF-7/DOX and MCF-7/s cells were exposed to serial dilutions of (A) DOX or (B) RES for 48 h and cell inhibition rate was determined via an MTT assay for MCF-7/s (circle) and MCF-7/DOX (square) cells. DOX, doxorubicin; IR, inhibition ratio; DMSO, dimethylsulfoxide; RES, resveratrol.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Resveratrol reverses multidrug resistance in human breast cancer doxorubicin-resistant cells

    doi: 10.3892/etm.2014.1662

    Figure Lengend Snippet: Inhibition of DOX or RES on proliferation of MCF-7/DOX (DOX-resistant cell line) and MCF-7/sensitive (s) cells. MCF-7/DOX and MCF-7/s cells were exposed to serial dilutions of (A) DOX or (B) RES for 48 h and cell inhibition rate was determined via an MTT assay for MCF-7/s (circle) and MCF-7/DOX (square) cells. DOX, doxorubicin; IR, inhibition ratio; DMSO, dimethylsulfoxide; RES, resveratrol.

    Article Snippet: Following 24 h, the culture medium was refreshed with RPMI-1640 that was supplemented with various concentrations of RES (4, 8, 12 or 16 μM) dissolved in DMSO with a final concentration of 0.1% (Sigma-Aldrich, St. Louis, MO, USA).

    Techniques: Inhibition, MTT Assay

    Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or DMSO (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of proteasome activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).

    Journal: Genes to cells : devoted to molecular & cellular mechanisms

    Article Title: Dysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1

    doi: 10.1111/gtc.12125

    Figure Lengend Snippet: Disaggregation of mutant SOD1 from inclusions to the cytosol. (A) HeLa cell lines stably expressing SOD1-WT-YFP or SOD1-G85R-YFP were treated with MG-132 or DMSO (used as a negative control). The white arrow indicates a perinuclear inclusion. (B) Numbers of cells containing SOD1-YFP inclusions during 16-h treatment with MG-132 (mean ± SD, n > 600). (C) Disappearance of inclusions during recovery of proteasome activity. After 16-h treatment with MG-132, cells were transferred to a recovery culture without MG-132 and incubated for the indicated periods. Time-lapse images were taken using a confocal microscope. White arrows indicate inclusions. (D) Numbers of cells containing inclusions during the recovery culture (mean ± S.D., n > 600).

    Article Snippet: As a negative control for proteasome inhibition, 0.02% DMSO (Nacalai Tesque) was added instead of MG-132.

    Techniques: Mutagenesis, Stable Transfection, Expressing, Negative Control, Activity Assay, Incubation, Microscopy

    Click-iT Plus EdU proliferation assay. Plot depicts percent of A549 cell nuclei positive for EdU on day 4 in monoculture and the A549/CCL-210 co-cultures, separated by gel and media type. The nondegradable gels contained a peptide crosslinker insensitive to MMP cleavage. GM6001 was added at 10 μM, and the DMSO control media contained 0.05% DMSO. The degradable bars refer to the original experiment in MMP-degradable gels with regular growth media. Results are presented as means ± SEM of three biological replicates of each condition. *p

    Journal: Biomaterials

    Article Title: Epithelial-mesenchymal crosstalk influences cellular behavior in a 3D alveolus-fibroblast model system

    doi: 10.1016/j.biomaterials.2017.11.008

    Figure Lengend Snippet: Click-iT Plus EdU proliferation assay. Plot depicts percent of A549 cell nuclei positive for EdU on day 4 in monoculture and the A549/CCL-210 co-cultures, separated by gel and media type. The nondegradable gels contained a peptide crosslinker insensitive to MMP cleavage. GM6001 was added at 10 μM, and the DMSO control media contained 0.05% DMSO. The degradable bars refer to the original experiment in MMP-degradable gels with regular growth media. Results are presented as means ± SEM of three biological replicates of each condition. *p

    Article Snippet: For MMP inhibition studies, 10 μM GM6001 in DMSO (Santa Cruz Biotechnology) or 0.05% DMSO was added to the media.

    Techniques: Proliferation Assay

    Movement angle is the angle between expected sheet direction ( i . e . wound closing or 0°) and PIV determined velocity vectors. Color bar indicates fraction of all PIV vectors with a particular orientation. Reference condition is DMSO treated and dysregulated condition is ICG-001 treated. CCM stands for control conditioned media; WCM stands for Wnt3a conditioned media.

    Journal: PLoS Computational Biology

    Article Title: The Integrated Role of Wnt/β-Catenin, N-Glycosylation, and E-Cadherin-Mediated Adhesion in Network Dynamics

    doi: 10.1371/journal.pcbi.1005007

    Figure Lengend Snippet: Movement angle is the angle between expected sheet direction ( i . e . wound closing or 0°) and PIV determined velocity vectors. Color bar indicates fraction of all PIV vectors with a particular orientation. Reference condition is DMSO treated and dysregulated condition is ICG-001 treated. CCM stands for control conditioned media; WCM stands for Wnt3a conditioned media.

    Article Snippet: To determine the effect of a perturbation in the RCN, cells were either treated with 25 μM ICG-001 in 0.05% DMSO (Selleck Chemicals, Houston, TX) or only DMSO as a control.

    Techniques:

    E-cadherin mobility shift from treatment of total cell lysates with glycosidases: Endoglycosidase H (EndoH) or Peptide-N-Glycosidase F (PNGaseF). a) Immunoblots of E-cadherin from cells grown without exogenous Wnt3a (CCM). b) Immunoblots for lysate from cells grown in exogenous Wnt3a (WCM). Cells were grown in the presence of either no inhibitor (DMSO) or ICG-001.

    Journal: PLoS Computational Biology

    Article Title: The Integrated Role of Wnt/β-Catenin, N-Glycosylation, and E-Cadherin-Mediated Adhesion in Network Dynamics

    doi: 10.1371/journal.pcbi.1005007

    Figure Lengend Snippet: E-cadherin mobility shift from treatment of total cell lysates with glycosidases: Endoglycosidase H (EndoH) or Peptide-N-Glycosidase F (PNGaseF). a) Immunoblots of E-cadherin from cells grown without exogenous Wnt3a (CCM). b) Immunoblots for lysate from cells grown in exogenous Wnt3a (WCM). Cells were grown in the presence of either no inhibitor (DMSO) or ICG-001.

    Article Snippet: To determine the effect of a perturbation in the RCN, cells were either treated with 25 μM ICG-001 in 0.05% DMSO (Selleck Chemicals, Houston, TX) or only DMSO as a control.

    Techniques: Mobility Shift, Western Blot

    MDCK cells were treated with either conditioned media with (WCM) or without (CCM) Wnt3a, and either no inhibitor (DMSO) or ICG-001. a) Representative immunoblots (IBs) of ABC in total cell lysates (TCL). Images were taken from a single membrane. Quantified intensity values are averages; errors bars represent standard error of the mean (SEM) (N = 4). Full IB with duplicates can be found in S3 Fig (supplemental). b) IBs for α-catenin and E-cadherin in E-cadherin immunoprecipitates (IP). CCM TLC and WCM TLC represent input, with isotype controls (IP IgG) included. Blots were quantified and normalized to the ICG-001 condition in each activation state. * represents statistically significant difference, p

    Journal: PLoS Computational Biology

    Article Title: The Integrated Role of Wnt/β-Catenin, N-Glycosylation, and E-Cadherin-Mediated Adhesion in Network Dynamics

    doi: 10.1371/journal.pcbi.1005007

    Figure Lengend Snippet: MDCK cells were treated with either conditioned media with (WCM) or without (CCM) Wnt3a, and either no inhibitor (DMSO) or ICG-001. a) Representative immunoblots (IBs) of ABC in total cell lysates (TCL). Images were taken from a single membrane. Quantified intensity values are averages; errors bars represent standard error of the mean (SEM) (N = 4). Full IB with duplicates can be found in S3 Fig (supplemental). b) IBs for α-catenin and E-cadherin in E-cadherin immunoprecipitates (IP). CCM TLC and WCM TLC represent input, with isotype controls (IP IgG) included. Blots were quantified and normalized to the ICG-001 condition in each activation state. * represents statistically significant difference, p

    Article Snippet: To determine the effect of a perturbation in the RCN, cells were either treated with 25 μM ICG-001 in 0.05% DMSO (Selleck Chemicals, Houston, TX) or only DMSO as a control.

    Techniques: Western Blot, Thin Layer Chromatography, Activation Assay

    a) Average magnitude of velocity field from PIV analysis in MDCK cell sheets and b) lateral correlation length at migrating wound edge. The four conditions correspond to treatment with: Either conditioned media with (WCM) or without (CCM) Wnt3a, and either no inhibitor (DMSO) or ICG-001. Values are the average (errors bars represent SEM) of three independent experiments for 27 time points in each (N = 81). ** and * represent statistically significant difference, p

    Journal: PLoS Computational Biology

    Article Title: The Integrated Role of Wnt/β-Catenin, N-Glycosylation, and E-Cadherin-Mediated Adhesion in Network Dynamics

    doi: 10.1371/journal.pcbi.1005007

    Figure Lengend Snippet: a) Average magnitude of velocity field from PIV analysis in MDCK cell sheets and b) lateral correlation length at migrating wound edge. The four conditions correspond to treatment with: Either conditioned media with (WCM) or without (CCM) Wnt3a, and either no inhibitor (DMSO) or ICG-001. Values are the average (errors bars represent SEM) of three independent experiments for 27 time points in each (N = 81). ** and * represent statistically significant difference, p

    Article Snippet: To determine the effect of a perturbation in the RCN, cells were either treated with 25 μM ICG-001 in 0.05% DMSO (Selleck Chemicals, Houston, TX) or only DMSO as a control.

    Techniques:

    AHR prevents IL-1R1 hi ILC3s from acquiring the capacity for IFN-γ production in vitro ( A-D ) IL-1R1 hi ILC3s were FACS-sorted from SLT and cultured in conditions shown. After 14 d, an equal number of cells from each condition were stimulated for 12 h with IL-12, IL-15, and IL-18 then assessed for ( A-C ) intracellular (n = 3) or ( D ) secreted (n = 4) IFN-γ production. ( A ) Represents an individual donor (CH-223191, ; DMSO, ; FICZ, dashed line), while ( B-D ) depicts the average result from multiple donors, presented as mean ± SEM, * for P

    Journal: Cell reports

    Article Title: AHR prevents human IL-1R1hi ILC3 differentiation to natural killer cells

    doi: 10.1016/j.celrep.2014.05.042

    Figure Lengend Snippet: AHR prevents IL-1R1 hi ILC3s from acquiring the capacity for IFN-γ production in vitro ( A-D ) IL-1R1 hi ILC3s were FACS-sorted from SLT and cultured in conditions shown. After 14 d, an equal number of cells from each condition were stimulated for 12 h with IL-12, IL-15, and IL-18 then assessed for ( A-C ) intracellular (n = 3) or ( D ) secreted (n = 4) IFN-γ production. ( A ) Represents an individual donor (CH-223191, ; DMSO, ; FICZ, dashed line), while ( B-D ) depicts the average result from multiple donors, presented as mean ± SEM, * for P

    Article Snippet: FACS-purified IL-1R1hi ILC3s were cultured in a round-bottom 96-well plate (Costar) at a starting density of 25,000 cells/ml in α-MEM medium containing 10% FBS, penicillin G (100 μg/ml), and streptomycin (100 μg/ml) (Invitrogen), supplemented with recombinant human IL-15 (1 nM; Amgen) with or without IL-1β (10 ng/ml; Peprotech), and either carrier alone (DMSO, 1 μl/ml; Invitrogen) or carrier containing AHR agonist (FICZ, 300 nM; Enzo Life Sciences) or AHR antagonist (CH-223191, 3 μM; Calbiochem) at concentrations previously reported to modulate TH 17 differentiation ( ).

    Techniques: In Vitro, FACS, Cell Culture

    AHR prevents differentiation of human IL-1R1 hi ILC3s to NK cells in vitro ( A-E ) IL-1R1 hi ILC3s were FACS-purified from SLT, cultured for 14 d under indicated conditions, then assessed for expression of CD56, CD94, and CD117. Data in ( A, D ) depict staining in a representative donor (CH-223191, ; DMSO, ; FICZ, dashed line; n ≥ 8). Data in ( B, C, E ) depict average: ( B ) mean fluorescence intensity (MFI) of CD56 surface expression (n = 12), ( C ) percentage of cells that acquired CD94 surface expression (n = 8), and ( E ) percentage of cells that lost CD117 and acquired CD94 (n = 4). Data presented as mean ± SEM; * for P

    Journal: Cell reports

    Article Title: AHR prevents human IL-1R1hi ILC3 differentiation to natural killer cells

    doi: 10.1016/j.celrep.2014.05.042

    Figure Lengend Snippet: AHR prevents differentiation of human IL-1R1 hi ILC3s to NK cells in vitro ( A-E ) IL-1R1 hi ILC3s were FACS-purified from SLT, cultured for 14 d under indicated conditions, then assessed for expression of CD56, CD94, and CD117. Data in ( A, D ) depict staining in a representative donor (CH-223191, ; DMSO, ; FICZ, dashed line; n ≥ 8). Data in ( B, C, E ) depict average: ( B ) mean fluorescence intensity (MFI) of CD56 surface expression (n = 12), ( C ) percentage of cells that acquired CD94 surface expression (n = 8), and ( E ) percentage of cells that lost CD117 and acquired CD94 (n = 4). Data presented as mean ± SEM; * for P

    Article Snippet: FACS-purified IL-1R1hi ILC3s were cultured in a round-bottom 96-well plate (Costar) at a starting density of 25,000 cells/ml in α-MEM medium containing 10% FBS, penicillin G (100 μg/ml), and streptomycin (100 μg/ml) (Invitrogen), supplemented with recombinant human IL-15 (1 nM; Amgen) with or without IL-1β (10 ng/ml; Peprotech), and either carrier alone (DMSO, 1 μl/ml; Invitrogen) or carrier containing AHR agonist (FICZ, 300 nM; Enzo Life Sciences) or AHR antagonist (CH-223191, 3 μM; Calbiochem) at concentrations previously reported to modulate TH 17 differentiation ( ).

    Techniques: In Vitro, FACS, Purification, Cell Culture, Expressing, Staining, Fluorescence

    Human IL-1R1 hi ILC3s express AHR and respond to AHR ligands in vitro ( A, B ) Real-time RT-PCR was used to assess: ( A ) TBX21 (TBET), EOMES, RORC and AHR mRNA expression ex vivo in human IL-1R1 hi ILC3s (Lin - CD34 - CD117 + CD94 - IL-1R1 hi ) and stage 4 (Lin - CD34 - CD117 +/- CD94 + ) mature CD56 bright NK cells, FACS-purified from SLT; or ( B ) IL-22, CYP1A1, RORC, EOMES , and TBX21 (TBET) mRNA expression after culture of IL-1R1 hi ILC3s for 14 d in the presence of IL-15 (1 nM; ) or IL-15 + IL-1β (10 ng/ml; ■), plus either carrier alone (DMSO, 1 μl/ml), or carrier containing AHR agonist (FICZ, 300 nM) or AHR antagonist (CH-223191, 3 μM). For ( A, B ), gene expression levels were normalized to 18S mRNA, and relative quantification was performed using the ΔΔCt method. Y axis depicts fold difference in mRNA expression, quantified relative to the condition in which expression was lowest (arbitrarily normalized to 1). ( C ) Absolute number of viable cells generated from culture of IL-1R1 hi ILC3s for 14 d with IL-15 plus DMSO, IL-15 plus AHR agonist FICZ, or IL-15 plus AHR antagonist CH-223191. Data in A, B and C presented as mean ± SEM (for A and B , n ≥ 4; for C , n = 7; * for P

    Journal: Cell reports

    Article Title: AHR prevents human IL-1R1hi ILC3 differentiation to natural killer cells

    doi: 10.1016/j.celrep.2014.05.042

    Figure Lengend Snippet: Human IL-1R1 hi ILC3s express AHR and respond to AHR ligands in vitro ( A, B ) Real-time RT-PCR was used to assess: ( A ) TBX21 (TBET), EOMES, RORC and AHR mRNA expression ex vivo in human IL-1R1 hi ILC3s (Lin - CD34 - CD117 + CD94 - IL-1R1 hi ) and stage 4 (Lin - CD34 - CD117 +/- CD94 + ) mature CD56 bright NK cells, FACS-purified from SLT; or ( B ) IL-22, CYP1A1, RORC, EOMES , and TBX21 (TBET) mRNA expression after culture of IL-1R1 hi ILC3s for 14 d in the presence of IL-15 (1 nM; ) or IL-15 + IL-1β (10 ng/ml; ■), plus either carrier alone (DMSO, 1 μl/ml), or carrier containing AHR agonist (FICZ, 300 nM) or AHR antagonist (CH-223191, 3 μM). For ( A, B ), gene expression levels were normalized to 18S mRNA, and relative quantification was performed using the ΔΔCt method. Y axis depicts fold difference in mRNA expression, quantified relative to the condition in which expression was lowest (arbitrarily normalized to 1). ( C ) Absolute number of viable cells generated from culture of IL-1R1 hi ILC3s for 14 d with IL-15 plus DMSO, IL-15 plus AHR agonist FICZ, or IL-15 plus AHR antagonist CH-223191. Data in A, B and C presented as mean ± SEM (for A and B , n ≥ 4; for C , n = 7; * for P

    Article Snippet: FACS-purified IL-1R1hi ILC3s were cultured in a round-bottom 96-well plate (Costar) at a starting density of 25,000 cells/ml in α-MEM medium containing 10% FBS, penicillin G (100 μg/ml), and streptomycin (100 μg/ml) (Invitrogen), supplemented with recombinant human IL-15 (1 nM; Amgen) with or without IL-1β (10 ng/ml; Peprotech), and either carrier alone (DMSO, 1 μl/ml; Invitrogen) or carrier containing AHR agonist (FICZ, 300 nM; Enzo Life Sciences) or AHR antagonist (CH-223191, 3 μM; Calbiochem) at concentrations previously reported to modulate TH 17 differentiation ( ).

    Techniques: In Vitro, Quantitative RT-PCR, Expressing, Ex Vivo, FACS, Purification, Generated

    AHR prevents IL-1R1 hi ILC3s from acquiring cytotoxic effector function in vitro ( A-D ) IL-1R1 hi ILC3s were FACS-sorted from SLT and cultured under the indicated conditions. ( A, B ) On d 14, flow cytometry was used to assess: ( A ) TRAIL and CD94 surface expression, or ( B ) intracellular perforin and CD94 surface expression. Histograms depict staining in a representative donor after gating on CD94 + lymphocytes (CH-223191, ; DMSO, ; FICZ, dashed line). For A and B , n ≥ 3. ( C, D ) Cytotoxic activity was assessed against the K562 target cell line using an equal number of ( C ) total progeny, or ( D ) FACS-sorted CD94 + and CD94 - cells generated from IL-1R1 hi ILC3s after 14 d in conditions indicated. Cells were plated in triplicate, and target cell lysis was assessed at ( C ) each effector:target (E:T) ratios indicated (n = 3), or ( D ) an E:T ratio of 5:1 (CD94 + ,■; CD94 - , ; n = 4). Data in C, D presented as mean ± SEM, *** for P

    Journal: Cell reports

    Article Title: AHR prevents human IL-1R1hi ILC3 differentiation to natural killer cells

    doi: 10.1016/j.celrep.2014.05.042

    Figure Lengend Snippet: AHR prevents IL-1R1 hi ILC3s from acquiring cytotoxic effector function in vitro ( A-D ) IL-1R1 hi ILC3s were FACS-sorted from SLT and cultured under the indicated conditions. ( A, B ) On d 14, flow cytometry was used to assess: ( A ) TRAIL and CD94 surface expression, or ( B ) intracellular perforin and CD94 surface expression. Histograms depict staining in a representative donor after gating on CD94 + lymphocytes (CH-223191, ; DMSO, ; FICZ, dashed line). For A and B , n ≥ 3. ( C, D ) Cytotoxic activity was assessed against the K562 target cell line using an equal number of ( C ) total progeny, or ( D ) FACS-sorted CD94 + and CD94 - cells generated from IL-1R1 hi ILC3s after 14 d in conditions indicated. Cells were plated in triplicate, and target cell lysis was assessed at ( C ) each effector:target (E:T) ratios indicated (n = 3), or ( D ) an E:T ratio of 5:1 (CD94 + ,■; CD94 - , ; n = 4). Data in C, D presented as mean ± SEM, *** for P

    Article Snippet: FACS-purified IL-1R1hi ILC3s were cultured in a round-bottom 96-well plate (Costar) at a starting density of 25,000 cells/ml in α-MEM medium containing 10% FBS, penicillin G (100 μg/ml), and streptomycin (100 μg/ml) (Invitrogen), supplemented with recombinant human IL-15 (1 nM; Amgen) with or without IL-1β (10 ng/ml; Peprotech), and either carrier alone (DMSO, 1 μl/ml; Invitrogen) or carrier containing AHR agonist (FICZ, 300 nM; Enzo Life Sciences) or AHR antagonist (CH-223191, 3 μM; Calbiochem) at concentrations previously reported to modulate TH 17 differentiation ( ).

    Techniques: In Vitro, FACS, Cell Culture, Flow Cytometry, Cytometry, Expressing, Staining, Activity Assay, Generated, Lysis