17 aag  (Alomone Labs)


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    Structured Review

    Alomone Labs 17 aag
    <t>17-AAG-mediated</t> apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .
    17 Aag, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/17 aag/product/Alomone Labs
    Average 90 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    17 aag - by Bioz Stars, 2022-08
    90/100 stars

    Images

    1) Product Images from "Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia"

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26045

    17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .
    Figure Legend Snippet: 17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .

    Techniques Used: Two Tailed Test

    Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).
    Figure Legend Snippet: Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Techniques Used: Binding Assay, Immunoprecipitation, Incubation, Transfection

    Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).
    Figure Legend Snippet: Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Techniques Used: Staining

    2) Product Images from "Mechanisms of Legionella pneumophila-induced interleukin-8 expression in human lung epithelial cells"

    Article Title: Mechanisms of Legionella pneumophila-induced interleukin-8 expression in human lung epithelial cells

    Journal: BMC Microbiology

    doi: 10.1186/1471-2180-7-102

    Inhibitory effect of 17-AAG on L. pneumophila -induced IL-8 expression .(A) A549 cells were incubated with 1 μM 17-AAG for 16 h prior to infection with varying concentrations of AA100jm strain for 6 h. RT-PCR was performed to check the changes of IL-8 mRNA expression after 17-AAG treatment in L. pneumophila -infected A549 cells. (B) Attenuation of L. pneumophila -induced NF-κB DNA binding by 17-AAG treatment. A549 cells were treated with (+) or without (-) 17-AAG for 16 h prior to infection with varying concentrations of L. pneumophila for 3 h. The nuclear extracts were isolated from A549 cells infected with L. pneumophila and incubated with 32 P-labeled oligonucleotides corresponding to NF-κB. (C) hsp90 protects IKKα and IKKβ from proteasomal degradation. A549 cells either were pretreated with LLnL (20 μM) for 1 h, followed or not followed by addition of 17-AAG (1 μM) and incubation for 16 h, or were treated with 17-AAG for 16 h or left untreated as indicated. Whole cell extracts were immunoblotted with specific antibodies against each protein. Representative results of three similar experiments in each panel are shown.
    Figure Legend Snippet: Inhibitory effect of 17-AAG on L. pneumophila -induced IL-8 expression .(A) A549 cells were incubated with 1 μM 17-AAG for 16 h prior to infection with varying concentrations of AA100jm strain for 6 h. RT-PCR was performed to check the changes of IL-8 mRNA expression after 17-AAG treatment in L. pneumophila -infected A549 cells. (B) Attenuation of L. pneumophila -induced NF-κB DNA binding by 17-AAG treatment. A549 cells were treated with (+) or without (-) 17-AAG for 16 h prior to infection with varying concentrations of L. pneumophila for 3 h. The nuclear extracts were isolated from A549 cells infected with L. pneumophila and incubated with 32 P-labeled oligonucleotides corresponding to NF-κB. (C) hsp90 protects IKKα and IKKβ from proteasomal degradation. A549 cells either were pretreated with LLnL (20 μM) for 1 h, followed or not followed by addition of 17-AAG (1 μM) and incubation for 16 h, or were treated with 17-AAG for 16 h or left untreated as indicated. Whole cell extracts were immunoblotted with specific antibodies against each protein. Representative results of three similar experiments in each panel are shown.

    Techniques Used: Expressing, Incubation, Infection, Reverse Transcription Polymerase Chain Reaction, Binding Assay, Isolation, Labeling

    3) Product Images from "Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia"

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26045

    Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).
    Figure Legend Snippet: Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Techniques Used: Binding Assay, Immunoprecipitation, Incubation, Transfection

    17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C ) Cells were treated with or without 100–1000 nM 17-AAG for 24 h and stained with annexin V-FITC and PI. The cells were then analyz ed by FACS with quadrant statistics. The graphical data of all samples (top) and selected observed data (bottom) are shown. The corresponding raw data of all samples are shown in Supplementary Figure 6 . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p
    Figure Legend Snippet: 17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C ) Cells were treated with or without 100–1000 nM 17-AAG for 24 h and stained with annexin V-FITC and PI. The cells were then analyz ed by FACS with quadrant statistics. The graphical data of all samples (top) and selected observed data (bottom) are shown. The corresponding raw data of all samples are shown in Supplementary Figure 6 . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p

    Techniques Used: Staining, FACS, Two Tailed Test

    Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .
    Figure Legend Snippet: Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .

    Techniques Used: Staining, FACS, Software

    Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .
    Figure Legend Snippet: Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .

    Techniques Used: Mutagenesis, Staining, FACS, Software, Two Tailed Test

    Sensitivities to HSP90 inhibitors in Ba/F3 cells expressing various amino acid substitutions of D835 on FLT3-ITD ( A ) Cells were treated with the increasing concentrations of quizartinib (1–256 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 10 nM quizartinib for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies. ( C ) Cells were treated with increasing concentrations of 17-AAG (upper; 4–1024 nM) or 17-DMAG (lower; 4–1024 nM) for 4 days, after which cell growth inhibition assays were performed as described in ( A ). ( D ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies.
    Figure Legend Snippet: Sensitivities to HSP90 inhibitors in Ba/F3 cells expressing various amino acid substitutions of D835 on FLT3-ITD ( A ) Cells were treated with the increasing concentrations of quizartinib (1–256 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 10 nM quizartinib for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies. ( C ) Cells were treated with increasing concentrations of 17-AAG (upper; 4–1024 nM) or 17-DMAG (lower; 4–1024 nM) for 4 days, after which cell growth inhibition assays were performed as described in ( A ). ( D ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies.

    Techniques Used: Expressing, Inhibition

    Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).
    Figure Legend Snippet: Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Techniques Used: Staining

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    Alomone Labs retaspimycin hydrochloride
    Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), <t>retaspimycin</t> (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .
    Retaspimycin Hydrochloride, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/retaspimycin hydrochloride/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    retaspimycin hydrochloride - by Bioz Stars, 2022-08
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    Alomone Labs 17 aag
    <t>17-AAG-mediated</t> apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .
    17 Aag, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/17 aag/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    17 aag - by Bioz Stars, 2022-08
    90/100 stars
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    Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Staining, FACS, Software

    Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Mutagenesis, Staining, FACS, Software, Two Tailed Test

    17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: 17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p .

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Two Tailed Test

    Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Binding Assay, Immunoprecipitation, Incubation, Transfection

    Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Staining

    Inhibitory effect of 17-AAG on L. pneumophila -induced IL-8 expression .(A) A549 cells were incubated with 1 μM 17-AAG for 16 h prior to infection with varying concentrations of AA100jm strain for 6 h. RT-PCR was performed to check the changes of IL-8 mRNA expression after 17-AAG treatment in L. pneumophila -infected A549 cells. (B) Attenuation of L. pneumophila -induced NF-κB DNA binding by 17-AAG treatment. A549 cells were treated with (+) or without (-) 17-AAG for 16 h prior to infection with varying concentrations of L. pneumophila for 3 h. The nuclear extracts were isolated from A549 cells infected with L. pneumophila and incubated with 32 P-labeled oligonucleotides corresponding to NF-κB. (C) hsp90 protects IKKα and IKKβ from proteasomal degradation. A549 cells either were pretreated with LLnL (20 μM) for 1 h, followed or not followed by addition of 17-AAG (1 μM) and incubation for 16 h, or were treated with 17-AAG for 16 h or left untreated as indicated. Whole cell extracts were immunoblotted with specific antibodies against each protein. Representative results of three similar experiments in each panel are shown.

    Journal: BMC Microbiology

    Article Title: Mechanisms of Legionella pneumophila-induced interleukin-8 expression in human lung epithelial cells

    doi: 10.1186/1471-2180-7-102

    Figure Lengend Snippet: Inhibitory effect of 17-AAG on L. pneumophila -induced IL-8 expression .(A) A549 cells were incubated with 1 μM 17-AAG for 16 h prior to infection with varying concentrations of AA100jm strain for 6 h. RT-PCR was performed to check the changes of IL-8 mRNA expression after 17-AAG treatment in L. pneumophila -infected A549 cells. (B) Attenuation of L. pneumophila -induced NF-κB DNA binding by 17-AAG treatment. A549 cells were treated with (+) or without (-) 17-AAG for 16 h prior to infection with varying concentrations of L. pneumophila for 3 h. The nuclear extracts were isolated from A549 cells infected with L. pneumophila and incubated with 32 P-labeled oligonucleotides corresponding to NF-κB. (C) hsp90 protects IKKα and IKKβ from proteasomal degradation. A549 cells either were pretreated with LLnL (20 μM) for 1 h, followed or not followed by addition of 17-AAG (1 μM) and incubation for 16 h, or were treated with 17-AAG for 16 h or left untreated as indicated. Whole cell extracts were immunoblotted with specific antibodies against each protein. Representative results of three similar experiments in each panel are shown.

    Article Snippet: 17-AAG was purchased from Alomone Labs (Jerusalem, Israel).

    Techniques: Expressing, Incubation, Infection, Reverse Transcription Polymerase Chain Reaction, Binding Assay, Isolation, Labeling

    Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Effect of 17-AAG on FLT3-ITD–HSP90 binding ( A ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h. FLAG-tagged FLT3-ITD proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies. ( B ) HA-tagged HSP90 proteins were immunopurified from HEK293 transfectants, and FLAG-tagged FLT3-ITD proteins bound to affinity gels were prepared from Ba/F3 transfectants. Both proteins were mixed and incubated in immunoprecipitation buffer with or without 1–100 nM 17-AAG by rocking overnight at 4° C. The immunoprecipitants were eluted with FLAG peptides and subjected to immunoblotting using anti-HA or anti-FLAG antibodies. ( C ) Schematic of the primary structures of FLT3-ITD deletion mutants (top). JM, juxtamembrane domain; TKD, tyrosine kinase domain. HEK293 cells were transfected with FLAG-tagged FLT3-ITD or the deletion mutants for 24 h. The proteins were immunoprecipitated with an anti-FLAG antibody, and the immunoprecipitants were subjected to immunoblotting using anti-HSP90 or anti-FLAG antibodies (bottom).

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Binding Assay, Immunoprecipitation, Incubation, Transfection

    17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C ) Cells were treated with or without 100–1000 nM 17-AAG for 24 h and stained with annexin V-FITC and PI. The cells were then analyz ed by FACS with quadrant statistics. The graphical data of all samples (top) and selected observed data (bottom) are shown. The corresponding raw data of all samples are shown in Supplementary Figure 6 . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: 17-AAG-mediated apoptosis in QR1 and QR2 cells ( A and B ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. Typical caspases were examined in ( A ), and mitochondrial apoptosis-related proteins were examined in ( B ). ( C ) Cells were treated with or without 100–1000 nM 17-AAG for 24 h and stained with annexin V-FITC and PI. The cells were then analyz ed by FACS with quadrant statistics. The graphical data of all samples (top) and selected observed data (bottom) are shown. The corresponding raw data of all samples are shown in Supplementary Figure 6 . ( D ) Cells were treated with increasing concentrations of daunorubicin (DNR, 0.25–64 nM) combined with or without 3–30 nM 17-AAG for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The IC 50 values of DNR are presented here as the mean ± SD from three independent experiments. Statistical analyses were performed with two-tailed Student's t -tests. Asterisks indicate p

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Staining, FACS, Two Tailed Test

    Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Sensitivities to 17-AAG in QR1 and QR2 cells ( A ) Cells were treated with increasing concentrations of 17-AAG (2–512 nM), 17-DMAG (4–1024 nM), retaspimycin (4–1024 nM), or luminespid (0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and immunoblotting using the indicated antibodies was performed. ( C ) Cells were treated with or without 30 or 100 nM 17-AAG for 24 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was measured using CellQuest software, and the data are presented in the bar graph as the mean ± SE from two independent experiments. Typical corresponding raw data are shown in Supplementary Figure 5 .

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Staining, FACS, Software

    Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Sensitivities to HSP90 inhibitors in the FLT3-ITD and TKD mutant transfectants ( A ) Cells were treated with increasing concentrations of 17-AAG (upper left; 4–1024 nM), 17-DMAG (upper right; 4–1024 nM), retaspimycin (lower left; 4–1024 nM), or luminespid (lower right; 0.125–32 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The viabilities of 17-AAG- or 17-DMAG-treated cells relative to those of untreated cells were calculated and are presented here as the mean ± SD from three independent experiments. ( B and C ) Cells were treated with or without 100 or 300 nM 17-AAG ( B ) or 10 or 30 nM luminespid ( C ) for 6 h, and immunoblotting using the indicated antibodies was performed. ( D ) Cells were treated with 100–1000 nM 17-AAG for 24 h, and, after staining the cells with PI, the cell cycle ploidy patterns were analyzed by FACS. Each population was calculated using CellQuest software. The ratios of sub-G1 (red) and G0/G1 (blue) phases are presented in the bar graph as the mean ± SD from three independent experiments; statistical analyses were performed with two-tailed Student's t -tests. Typical corresponding raw data are shown in Supplementary Figure 3 .

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Mutagenesis, Staining, FACS, Software, Two Tailed Test

    Sensitivities to HSP90 inhibitors in Ba/F3 cells expressing various amino acid substitutions of D835 on FLT3-ITD ( A ) Cells were treated with the increasing concentrations of quizartinib (1–256 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 10 nM quizartinib for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies. ( C ) Cells were treated with increasing concentrations of 17-AAG (upper; 4–1024 nM) or 17-DMAG (lower; 4–1024 nM) for 4 days, after which cell growth inhibition assays were performed as described in ( A ). ( D ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies.

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Sensitivities to HSP90 inhibitors in Ba/F3 cells expressing various amino acid substitutions of D835 on FLT3-ITD ( A ) Cells were treated with the increasing concentrations of quizartinib (1–256 nM) for 4 days, and the resulting cell viabilities were determined by WST-8 assay. The data are presented here as the mean ± SD from three independent experiments. ( B ) Cells were treated with or without 10 nM quizartinib for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies. ( C ) Cells were treated with increasing concentrations of 17-AAG (upper; 4–1024 nM) or 17-DMAG (lower; 4–1024 nM) for 4 days, after which cell growth inhibition assays were performed as described in ( A ). ( D ) Cells were treated with or without 100 or 300 nM 17-AAG for 6 h, and lysates of these cells were subjected to immunoblotting using the indicated antibodies.

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Expressing, Inhibition

    Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Journal: Oncotarget

    Article Title: Heat shock protein 90 inhibitors overcome the resistance to Fms-like tyrosine kinase 3 inhibitors in acute myeloid leukemia

    doi: 10.18632/oncotarget.26045

    Figure Lengend Snippet: Lysosomal degradation of FLT3-ITD+D835V by 17-AAG Cells were treated with or without 300 nM 17-AAG combined with 100 nM bafilomycin A1 (BAFA1) or bortezomib (BTZ) for 6 h. ( A ) Immunoblotting using the indicated antibodies was performed. ( B – D ) Cells were stained with anti-FLT3 (green signals) and anti-LC3B (red signals) antibodies. Nuclei were counterstained with DAPI. Arrowheads indicate FLT3 merged with LC3B (yellow signals).

    Article Snippet: 17-AAG, 17-DMAG, retaspimycin hydrochloride, and propidium iodide (PI) were obtained from Alomone Labs (Jerusalem, Israel), APExBIO (Houston, TX), and Wako (Tokyo, Japan), respectively.

    Techniques: Staining