bortezomib  (MedChemExpress)


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    Structured Review

    MedChemExpress bortezomib
    EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, <t>bortezomib</t> (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p
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    Images

    1) Product Images from "ALCAM regulates multiple myeloma chemoresistant side population"

    Article Title: ALCAM regulates multiple myeloma chemoresistant side population

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-022-04556-8

    EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, bortezomib (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p
    Figure Legend Snippet: EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, bortezomib (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p

    Techniques Used: In Vivo, Mouse Assay, Injection, Imaging, Luciferase, Activity Assay, Staining

    ALCAM regulates myeloma chemoresistant side population in vitro. A MM cells RPMI8226, either CTR-KD or AL-KD, were treated with melphalan (Mel, 15 μM) or bortezomib (BTZ, 5 nM) for 24 h. The SP cell ratio was examined by Hoechst staining. B The RPMI8226 cells were treated by melphalan as described above. The cell cycle was analyzed after Hoechst staining. C Cell-cycle quantification. D After Hoechst staining, the apoptotic cells were analyzed by annexin V staining. E ALCAM and EGFR expression on MM cells after Mel or BTZ treatment were detected by flow cytometry. MFI mean fluorescence index. F Examination of SP cells after EGFR inhibitor (gefitinib, 200 nM) and melphalan treatment. Data are the mean of three independent experiments in three replicates. * p
    Figure Legend Snippet: ALCAM regulates myeloma chemoresistant side population in vitro. A MM cells RPMI8226, either CTR-KD or AL-KD, were treated with melphalan (Mel, 15 μM) or bortezomib (BTZ, 5 nM) for 24 h. The SP cell ratio was examined by Hoechst staining. B The RPMI8226 cells were treated by melphalan as described above. The cell cycle was analyzed after Hoechst staining. C Cell-cycle quantification. D After Hoechst staining, the apoptotic cells were analyzed by annexin V staining. E ALCAM and EGFR expression on MM cells after Mel or BTZ treatment were detected by flow cytometry. MFI mean fluorescence index. F Examination of SP cells after EGFR inhibitor (gefitinib, 200 nM) and melphalan treatment. Data are the mean of three independent experiments in three replicates. * p

    Techniques Used: In Vitro, Staining, Expressing, Flow Cytometry, Fluorescence

    2) Product Images from "Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome"

    Article Title: Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome

    Journal: eLife

    doi: 10.7554/eLife.38430

    Extended validation of SALL4. ( A ) HEK293T cells were treated with increasing concentrations of thalidomide, lenalidomide, pomalidomide, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( B ) As in ( A ), but with H661 cells. ( C ) As in ( A ), but with SK-N-DZ cells. ( D ) HEK293T cells were treated with increasing concentrations of thalidomide and co-treated with 5 µM bortezomib, 5 µM MLN4924, 0.5 µM MLN7243, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( E ) As in ( D ), but with SK-N-DZ cells. ( F ) Parental HEK293T cells or two independent pools of CRBN -/- HEK293T cells were treated with increasing concentrations of thalidomide. Following 24 h incubation, SALL4, CRBN, and GAPDH protein levels were assessed by western blot analysis. ( G ) Kelly cells were treated with 1 µM pomalidomide or DMSO as a control for 8 h, at which point the compound was washed out. Cells were harvested at 1, 2, 4, 8, 24, and 48 h post-washout, and SALL4 and GAPDH protein levels were assessed by western blot analysis. ( H ) Kelly cells were treated with 1 µM pomalidomide for 1, 2, 4, 8, and 24 h, or with DMSO as a control. Following time course treatment, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( I ) Thalidomide treatment did not influence the expression of SALL4 mRNA. hES cells treated with 10 µM thalidomide or DMSO as a control for 24 h were subjected to quantitative RT-PCR to assess the levels of total SALL4 mRNA. The mRNA levels were normalized to those of GAPDH (housekeeping gene) mRNA. The SALL4 mRNA level remained stable or increased, which is in contrast to the decrease in protein abundance observed in proteomics and western blot analysis. mRNA fold change was determined from n = 2 with three technical replicates. ( J ) To validate the specificity of the antibody used, we transfected Kelly or HEK293T cells with a plasmid expressing mCherry, Cas9, and one of three guide RNAs (sgRNA1, sgRNA2, sgRNA3) targeting the SALL4 gene, or a mock control. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis and for sgRNA1 and sgRNA2 a loss of the specific bands for SALL4 was observed in accordance with the antibody being specific for SALL4. sgRNA3 had no effect, which is likely to be because of an ineffective sgRNA. ( K ) To validate the specificity of the antibody used, we transfected Kelly cells with a plasmid overexpressing Flag-mmSALL4, Flag-hsSALL4, or no transfection. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. One representative experiment is shown in this figure, from three replicates for each of the western blots.
    Figure Legend Snippet: Extended validation of SALL4. ( A ) HEK293T cells were treated with increasing concentrations of thalidomide, lenalidomide, pomalidomide, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( B ) As in ( A ), but with H661 cells. ( C ) As in ( A ), but with SK-N-DZ cells. ( D ) HEK293T cells were treated with increasing concentrations of thalidomide and co-treated with 5 µM bortezomib, 5 µM MLN4924, 0.5 µM MLN7243, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( E ) As in ( D ), but with SK-N-DZ cells. ( F ) Parental HEK293T cells or two independent pools of CRBN -/- HEK293T cells were treated with increasing concentrations of thalidomide. Following 24 h incubation, SALL4, CRBN, and GAPDH protein levels were assessed by western blot analysis. ( G ) Kelly cells were treated with 1 µM pomalidomide or DMSO as a control for 8 h, at which point the compound was washed out. Cells were harvested at 1, 2, 4, 8, 24, and 48 h post-washout, and SALL4 and GAPDH protein levels were assessed by western blot analysis. ( H ) Kelly cells were treated with 1 µM pomalidomide for 1, 2, 4, 8, and 24 h, or with DMSO as a control. Following time course treatment, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( I ) Thalidomide treatment did not influence the expression of SALL4 mRNA. hES cells treated with 10 µM thalidomide or DMSO as a control for 24 h were subjected to quantitative RT-PCR to assess the levels of total SALL4 mRNA. The mRNA levels were normalized to those of GAPDH (housekeeping gene) mRNA. The SALL4 mRNA level remained stable or increased, which is in contrast to the decrease in protein abundance observed in proteomics and western blot analysis. mRNA fold change was determined from n = 2 with three technical replicates. ( J ) To validate the specificity of the antibody used, we transfected Kelly or HEK293T cells with a plasmid expressing mCherry, Cas9, and one of three guide RNAs (sgRNA1, sgRNA2, sgRNA3) targeting the SALL4 gene, or a mock control. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis and for sgRNA1 and sgRNA2 a loss of the specific bands for SALL4 was observed in accordance with the antibody being specific for SALL4. sgRNA3 had no effect, which is likely to be because of an ineffective sgRNA. ( K ) To validate the specificity of the antibody used, we transfected Kelly cells with a plasmid overexpressing Flag-mmSALL4, Flag-hsSALL4, or no transfection. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. One representative experiment is shown in this figure, from three replicates for each of the western blots.

    Techniques Used: Incubation, Western Blot, Expressing, Quantitative RT-PCR, Transfection, Plasmid Preparation

    3) Product Images from "SHP2 Inhibitors Show Anti-Myeloma Activity and Synergize With Bortezomib in the Treatment of Multiple Myeloma"

    Article Title: SHP2 Inhibitors Show Anti-Myeloma Activity and Synergize With Bortezomib in the Treatment of Multiple Myeloma

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2022.841308

    Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 is effective in suppressing the growth and overcoming bortezomib resistance in bortezomib-resistant MM cells. (A) Bortezomib naïve (WT) and resistant (BTZR) myeloma cells (RPMI-8226 and NCI-H929 cells) were treated with various concentrations of bortezomib for 48 h, and the IC 50 was calculated and shown. (B) Protein levels of p-ERK and ERK of the parental and bortezomib-resistant myeloma cells were detected by Western blot analysis. The bar graph illustrates the quantitative comparison of different proteins levels. (C,D) Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 in bortezomib-resistant myeloma cells (BTZR) conferred a similar growth inhibition effect to that of bortezomib-naïve myeloma cells (WT). (E,F) After incubation with 20 µM SHP099 or 10 µM RMC-4550 in RPMI-8226 and NCI-H929 cells for 48 h, Western blots against p-SHP2, SHP2, p-ERK, ERK, P21, BAK, and cleaved caspase-3 were performed and quantified. (G) Bortezomib-resistant (RPMI-8226 BTZR or NCI-H929 BTZR) cells were treated with either bortezomib (50 nM), SHP2 inhibitors (20 μM SHP099 or 10 μM RMC-4550), or the combination for 48 h, followed by assessment for cell viability. (H) Bortezomib-resistant MM cells were incubated with different doses of BTZ and SHP2 inhibitors (SHP099 or RMC-4550) or with the combination of both for 48 h; the synergistic cytotoxic effects were determined using the combination index based on the data from cell viability assays. x-axis, fractional effect concentrations; y-axis, CI. Data were displayed as mean ± SD from three independent experiments. * p
    Figure Legend Snippet: Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 is effective in suppressing the growth and overcoming bortezomib resistance in bortezomib-resistant MM cells. (A) Bortezomib naïve (WT) and resistant (BTZR) myeloma cells (RPMI-8226 and NCI-H929 cells) were treated with various concentrations of bortezomib for 48 h, and the IC 50 was calculated and shown. (B) Protein levels of p-ERK and ERK of the parental and bortezomib-resistant myeloma cells were detected by Western blot analysis. The bar graph illustrates the quantitative comparison of different proteins levels. (C,D) Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 in bortezomib-resistant myeloma cells (BTZR) conferred a similar growth inhibition effect to that of bortezomib-naïve myeloma cells (WT). (E,F) After incubation with 20 µM SHP099 or 10 µM RMC-4550 in RPMI-8226 and NCI-H929 cells for 48 h, Western blots against p-SHP2, SHP2, p-ERK, ERK, P21, BAK, and cleaved caspase-3 were performed and quantified. (G) Bortezomib-resistant (RPMI-8226 BTZR or NCI-H929 BTZR) cells were treated with either bortezomib (50 nM), SHP2 inhibitors (20 μM SHP099 or 10 μM RMC-4550), or the combination for 48 h, followed by assessment for cell viability. (H) Bortezomib-resistant MM cells were incubated with different doses of BTZ and SHP2 inhibitors (SHP099 or RMC-4550) or with the combination of both for 48 h; the synergistic cytotoxic effects were determined using the combination index based on the data from cell viability assays. x-axis, fractional effect concentrations; y-axis, CI. Data were displayed as mean ± SD from three independent experiments. * p

    Techniques Used: Inhibition, Western Blot, Incubation

    Combination of RMC-4550 and BTZ exhibits a synergistic antitumor effect against MM cells. (A) Cytotoxic effects of various doses of RMC-4550 and BTZ in monotherapy and in combination on MM cells determined by the CCK-8 assay. Fa-CI plot analysis of combination treatment of the two on RPMI-8226 and NCI-H929 cell viability was performed. x-axis, fractional effect concentrations; y-axis, CI. RPMI-8226 and NCI-H929 cells were culture in the presence of DMSO, RMC-4550 (10 μM), BTZ (3 nM for RPMI-8226 and 2 nM for NCI-H929 cells), or RMC-4550 plus BTZ for 48 h, and then colony formation (B) , cell apoptosis (C), and cell cycle (D) were measured. The representative flow cytometric profiles of BrdU/Hoechst 33342 are shown. (E) Western blotting shows the levels of P21, BAK, and cleaved caspase-3 in myeloma cells with monotherapy or the combination of bortezomib and RMC4550 for 48 h. GAPDH served as a loading control. The graphs show the density volumes of the indicated proteins normalized to those in the control. Data were displayed as mean ± SD from three independent experiments. * p
    Figure Legend Snippet: Combination of RMC-4550 and BTZ exhibits a synergistic antitumor effect against MM cells. (A) Cytotoxic effects of various doses of RMC-4550 and BTZ in monotherapy and in combination on MM cells determined by the CCK-8 assay. Fa-CI plot analysis of combination treatment of the two on RPMI-8226 and NCI-H929 cell viability was performed. x-axis, fractional effect concentrations; y-axis, CI. RPMI-8226 and NCI-H929 cells were culture in the presence of DMSO, RMC-4550 (10 μM), BTZ (3 nM for RPMI-8226 and 2 nM for NCI-H929 cells), or RMC-4550 plus BTZ for 48 h, and then colony formation (B) , cell apoptosis (C), and cell cycle (D) were measured. The representative flow cytometric profiles of BrdU/Hoechst 33342 are shown. (E) Western blotting shows the levels of P21, BAK, and cleaved caspase-3 in myeloma cells with monotherapy or the combination of bortezomib and RMC4550 for 48 h. GAPDH served as a loading control. The graphs show the density volumes of the indicated proteins normalized to those in the control. Data were displayed as mean ± SD from three independent experiments. * p

    Techniques Used: CCK-8 Assay, Western Blot

    4) Product Images from "Characterization of ROS Metabolic Equilibrium Reclassifies Pan-Cancer Samples and Guides Pathway Targeting Therapy"

    Article Title: Characterization of ROS Metabolic Equilibrium Reclassifies Pan-Cancer Samples and Guides Pathway Targeting Therapy

    Journal: Frontiers in Oncology

    doi: 10.3389/fonc.2020.581197

    Drug efficacy can be modulated by targeting reactive oxygen species (ROS) metabolism. (A) The drug efficacies of bortezomib and docetaxel were assessed by adding a low concentration of H 2 O 2 together as assessed by cell proliferation assay. The antitumor efficacy of these two drugs was diminished by exogenous ROS. Error bars indicate the mean ± SD; ns = no significance, * p
    Figure Legend Snippet: Drug efficacy can be modulated by targeting reactive oxygen species (ROS) metabolism. (A) The drug efficacies of bortezomib and docetaxel were assessed by adding a low concentration of H 2 O 2 together as assessed by cell proliferation assay. The antitumor efficacy of these two drugs was diminished by exogenous ROS. Error bars indicate the mean ± SD; ns = no significance, * p

    Techniques Used: Concentration Assay, Proliferation Assay

    5) Product Images from "The Prognostic Value and Function of HOXB5 in Acute Myeloid Leukemia"

    Article Title: The Prognostic Value and Function of HOXB5 in Acute Myeloid Leukemia

    Journal: Frontiers in Genetics

    doi: 10.3389/fgene.2021.678368

    Downstream function analysis. (A) GO analysis showing the top 10 functions associated with HOXB5 positive-correlated genes in AML. (B) The result of GSEA verified HOXB5 acted in the HSC signature. (C) The results of GSEA verified HOXB5 acted in regulation of myeloid cells differentiation. (D) The difference of LSC score classified by HOXB5 expression. (E) The results of GSEA verified HOXB5 acted in the TNF/NF-κB pathway. (F) The correlation between HOXB5 expression and the IC50 of bortezomib in AML cell lines (with Pearson correlation analysis). *** P
    Figure Legend Snippet: Downstream function analysis. (A) GO analysis showing the top 10 functions associated with HOXB5 positive-correlated genes in AML. (B) The result of GSEA verified HOXB5 acted in the HSC signature. (C) The results of GSEA verified HOXB5 acted in regulation of myeloid cells differentiation. (D) The difference of LSC score classified by HOXB5 expression. (E) The results of GSEA verified HOXB5 acted in the TNF/NF-κB pathway. (F) The correlation between HOXB5 expression and the IC50 of bortezomib in AML cell lines (with Pearson correlation analysis). *** P

    Techniques Used: Expressing

    HOXB5 participates in myeloid cells differentiation by regulating TNF/NF-κB pathway. (A) HOXB5 expression differences in four AML cell lines. (B) The expression changes of TNF/NF-κB pathway related genes after HOXB5 knockdown confirmed by Western blot in THP1. (C) The expression changes of NF-κB–targeted genes after HOXB5 knockdown confirmed by RT-qPCR in THP1. (D) The cell differentiation changes of THP1 after PMA treatment between NC and siHOXB5 group. (E) The sensitivities of bortezomib in THP1 and KASUMI-1 (48 h). (F) The synergism effect of bortezomib and chemotherapy agents (daunomycin and cytarabine) in THP1 cells (48 h). ** P
    Figure Legend Snippet: HOXB5 participates in myeloid cells differentiation by regulating TNF/NF-κB pathway. (A) HOXB5 expression differences in four AML cell lines. (B) The expression changes of TNF/NF-κB pathway related genes after HOXB5 knockdown confirmed by Western blot in THP1. (C) The expression changes of NF-κB–targeted genes after HOXB5 knockdown confirmed by RT-qPCR in THP1. (D) The cell differentiation changes of THP1 after PMA treatment between NC and siHOXB5 group. (E) The sensitivities of bortezomib in THP1 and KASUMI-1 (48 h). (F) The synergism effect of bortezomib and chemotherapy agents (daunomycin and cytarabine) in THP1 cells (48 h). ** P

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

    6) Product Images from "Non-oncology drugs are a source of previously unappreciated anti-cancer activity"

    Article Title: Non-oncology drugs are a source of previously unappreciated anti-cancer activity

    Journal: bioRxiv

    doi: 10.1101/730119

    Generation of MTF-1 and SLC26A2 knockout cell lines a , SF295 cells were transduced with multiple guides targeting the MTF-1 gene. Following selection, genomic DNA was isolated and the targeted region was amplified by PCR. Results from the NGS CRISPR assay are shown as percent indel formation. b , Differentially expressed genes in SF295 glioma cells following MTF-1 knockout by CRISPR/Cas9. Loss of MT1E, MT1X, and MT2A expression was observed upon MTF-1 knockout. Gene expression was measured by mRNA sequencing and differential gene expression was calculated by DESeq2. c , Drug sensitivity of SF295 cells with and without MTF-1 knockout. MTF-1 does not alter sensitivity to control chemotherapeutic bortezomib. Standard deviation across three replicates is shown with error bars. d , Western immunoblot validation of SLC26A2 knockout in OVISE ovarian and A2058 melanoma cancer cell lines. The SLC26A2 protein is known to migrate across a range of molecular weights due to glycosylation. e , OVISE cells were transduced with multiple guides targeting the SLC26A2 gene. Indel frequency at the SLC26A2 CRISPR Cas9 cut sites was assessed by NGS CRISPR assay.
    Figure Legend Snippet: Generation of MTF-1 and SLC26A2 knockout cell lines a , SF295 cells were transduced with multiple guides targeting the MTF-1 gene. Following selection, genomic DNA was isolated and the targeted region was amplified by PCR. Results from the NGS CRISPR assay are shown as percent indel formation. b , Differentially expressed genes in SF295 glioma cells following MTF-1 knockout by CRISPR/Cas9. Loss of MT1E, MT1X, and MT2A expression was observed upon MTF-1 knockout. Gene expression was measured by mRNA sequencing and differential gene expression was calculated by DESeq2. c , Drug sensitivity of SF295 cells with and without MTF-1 knockout. MTF-1 does not alter sensitivity to control chemotherapeutic bortezomib. Standard deviation across three replicates is shown with error bars. d , Western immunoblot validation of SLC26A2 knockout in OVISE ovarian and A2058 melanoma cancer cell lines. The SLC26A2 protein is known to migrate across a range of molecular weights due to glycosylation. e , OVISE cells were transduced with multiple guides targeting the SLC26A2 gene. Indel frequency at the SLC26A2 CRISPR Cas9 cut sites was assessed by NGS CRISPR assay.

    Techniques Used: Knock-Out, Transduction, Selection, Isolation, Amplification, Polymerase Chain Reaction, Next-Generation Sequencing, CRISPR, Expressing, Sequencing, Standard Deviation, Western Blot

    7) Product Images from "The proton pump inhibitor pantoprazole disrupts protein degradation systems and sensitizes cancer cells to death under various stresses"

    Article Title: The proton pump inhibitor pantoprazole disrupts protein degradation systems and sensitizes cancer cells to death under various stresses

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-018-0642-6

    Proteasome inhibitors aggravated while protein synthesis suppression ameliorated the UPR and cell death by PPI. a , b AGS cells were pretreated with PPI (100 μg/ml) for 24 h in pH 7.4 condition, followed by combination with or without 50 nM Bortezomib or 0.1 μM MG132 for another 24 h. Western blot analysis of apoptosis related protein cleaved-PARP levels ( a ) and poly-ubiquitinated proteins ( b ). c , d AGS and HeLa cells were pretreated with CHX (250 ng/ml) for 2 h, and then incubated with PPI (100 μg/ml or 120 μg/ml) for 48 h in pH 7.4 condition. Levels of apoptosis related protein cleaved-PARP, UPR marker CHOP ( c ), and poly-ubiquitinated proteins ( d ) were analyzed. e AGS and HeLa cells were pretreated with torin 1 (500 nM) for 2 h, and then incubated with PPI (100 μg/ml or 120 μg/ml) for 48 h in pH 7.4 condition. Indicated proteins were analyzed by western blot. f AGS cells were treated as described in ( a ). The cell viability was determined by CCK8 assay (left) (** p
    Figure Legend Snippet: Proteasome inhibitors aggravated while protein synthesis suppression ameliorated the UPR and cell death by PPI. a , b AGS cells were pretreated with PPI (100 μg/ml) for 24 h in pH 7.4 condition, followed by combination with or without 50 nM Bortezomib or 0.1 μM MG132 for another 24 h. Western blot analysis of apoptosis related protein cleaved-PARP levels ( a ) and poly-ubiquitinated proteins ( b ). c , d AGS and HeLa cells were pretreated with CHX (250 ng/ml) for 2 h, and then incubated with PPI (100 μg/ml or 120 μg/ml) for 48 h in pH 7.4 condition. Levels of apoptosis related protein cleaved-PARP, UPR marker CHOP ( c ), and poly-ubiquitinated proteins ( d ) were analyzed. e AGS and HeLa cells were pretreated with torin 1 (500 nM) for 2 h, and then incubated with PPI (100 μg/ml or 120 μg/ml) for 48 h in pH 7.4 condition. Indicated proteins were analyzed by western blot. f AGS cells were treated as described in ( a ). The cell viability was determined by CCK8 assay (left) (** p

    Techniques Used: Western Blot, Incubation, Marker, CCK-8 Assay

    PPI-induced accumulation of exogenous SQSTM1 via ubiquitin-proteasome pathway. a AGS cells were transfected with HA-tagged SQSTM1 plasmid for 48 h, and then treated with PPI for another 48 h in both pH 6.5 and pH 7.4 conditions. The exogenous SQSTM1 protein was detected with antibody for HA. b AGS cells were treated with baf A1 (50 and 100 nM) and HCQ (10, 50, and 100 μM) for 24 h. c AGS cells were pretreated with baf A1 (100 nM) for 30 min, followed with 1 μM rapamycin or amino acid starvation by HBSS for another 24 h. d Different concentrations of two classical proteasome inhibitors Bortezomib and MG132 were added. e AGS cells were either untreated or treated with Bortezomib (25 nM) or MG132 (0.1 μM) for 24 h in the absence or presence of baf A1 (100 nM). f AGS cells transfected with HA-tagged SQSTM1 plasmid, were treated with 25 μg/ml cycloheximide (CHX) over a 240-min time period (left) or treated with 100 μg/ml PPI for 48 h in pH 7.4 conditions, and then followed by 25 μg/ml CHX over a 240-min time period (right). Cells were lysed at the indicated time points (0, 60, 120, and 240 min). Right panel showed the half-life of HA, which reflected the stability of exogenous SQSTM1 protein. g – i The accumulated SQSTM1 by either proteasome inhibitors or PPI was sensitive to autophagy mediated degradation. AGS cells were pretreated with 25 and 50 nM bortezomib for 1 h, and then incubated with 500 nM torin 1 for 24 h ( g ). After pretreatment with PPI for 24 h in pH 7.4 or pH 6.5 condition, rapamycin (1 μM) or torin 1 (500 nM) was added for another 24 h ( h ). The protein level of SQSTM1 was measured by western blot analysis ( g , h ), and the change pattern of SQSTM1 mRNA was confirmed by qRT-PCR (i) (** p
    Figure Legend Snippet: PPI-induced accumulation of exogenous SQSTM1 via ubiquitin-proteasome pathway. a AGS cells were transfected with HA-tagged SQSTM1 plasmid for 48 h, and then treated with PPI for another 48 h in both pH 6.5 and pH 7.4 conditions. The exogenous SQSTM1 protein was detected with antibody for HA. b AGS cells were treated with baf A1 (50 and 100 nM) and HCQ (10, 50, and 100 μM) for 24 h. c AGS cells were pretreated with baf A1 (100 nM) for 30 min, followed with 1 μM rapamycin or amino acid starvation by HBSS for another 24 h. d Different concentrations of two classical proteasome inhibitors Bortezomib and MG132 were added. e AGS cells were either untreated or treated with Bortezomib (25 nM) or MG132 (0.1 μM) for 24 h in the absence or presence of baf A1 (100 nM). f AGS cells transfected with HA-tagged SQSTM1 plasmid, were treated with 25 μg/ml cycloheximide (CHX) over a 240-min time period (left) or treated with 100 μg/ml PPI for 48 h in pH 7.4 conditions, and then followed by 25 μg/ml CHX over a 240-min time period (right). Cells were lysed at the indicated time points (0, 60, 120, and 240 min). Right panel showed the half-life of HA, which reflected the stability of exogenous SQSTM1 protein. g – i The accumulated SQSTM1 by either proteasome inhibitors or PPI was sensitive to autophagy mediated degradation. AGS cells were pretreated with 25 and 50 nM bortezomib for 1 h, and then incubated with 500 nM torin 1 for 24 h ( g ). After pretreatment with PPI for 24 h in pH 7.4 or pH 6.5 condition, rapamycin (1 μM) or torin 1 (500 nM) was added for another 24 h ( h ). The protein level of SQSTM1 was measured by western blot analysis ( g , h ), and the change pattern of SQSTM1 mRNA was confirmed by qRT-PCR (i) (** p

    Techniques Used: Transfection, Plasmid Preparation, Incubation, Western Blot, Quantitative RT-PCR

    8) Product Images from "pSILAC mass spectrometry reveals ZFP91 as IMiD-dependent substrate of the CRL4CRBN ubiquitin ligase"

    Article Title: pSILAC mass spectrometry reveals ZFP91 as IMiD-dependent substrate of the CRL4CRBN ubiquitin ligase

    Journal: Nature Communications

    doi: 10.1038/ncomms15398

    Validation of ZFP91 as bona fide lenalidomide-induced CRL4 CRBN substrate. ( a ) MM.1S cells were treated with increasing concentrations of lenalidomide or with DMSO. Following 24 h of incubation, ZFP91 and GAPDH levels were detected by anti-ZFP91 and anti-GAPDH western blot (shown is one representative experiment out of three replicates). ( b ) HEK293T cells were treated with 50μg ml −1 cycloheximide and increasing concentrations of lenalidomide, thalidomide or with DMSO, and cells were incubated for 6 h. ZFP91 and GAPDH levels were detected using anti-ZFP91 or anti-GAPDH immunoblotting (shown is one representative experiment out of five replicates). ( c ) as in ( b ) but using SK-N-DZ cells instead (shown is one representative experiment out of three replicates). ( d ) as in ( b ) but with co-treatment of bortezomib (proteasome inhibitor, lanes 4, 5) or MLN4924 (inhibitor of the NEDD8-activating enzyme, lanes 6,7). Shown is one representative experiment out of three replicates. ( e ) as in ( b ) using parental HEK293T (lane 1–3) or two independent pools of HEK293T cells with genetic inactivation of CRBN by CRISPR/Cas9 (shown is one representative experiment out of two replicates).
    Figure Legend Snippet: Validation of ZFP91 as bona fide lenalidomide-induced CRL4 CRBN substrate. ( a ) MM.1S cells were treated with increasing concentrations of lenalidomide or with DMSO. Following 24 h of incubation, ZFP91 and GAPDH levels were detected by anti-ZFP91 and anti-GAPDH western blot (shown is one representative experiment out of three replicates). ( b ) HEK293T cells were treated with 50μg ml −1 cycloheximide and increasing concentrations of lenalidomide, thalidomide or with DMSO, and cells were incubated for 6 h. ZFP91 and GAPDH levels were detected using anti-ZFP91 or anti-GAPDH immunoblotting (shown is one representative experiment out of five replicates). ( c ) as in ( b ) but using SK-N-DZ cells instead (shown is one representative experiment out of three replicates). ( d ) as in ( b ) but with co-treatment of bortezomib (proteasome inhibitor, lanes 4, 5) or MLN4924 (inhibitor of the NEDD8-activating enzyme, lanes 6,7). Shown is one representative experiment out of three replicates. ( e ) as in ( b ) using parental HEK293T (lane 1–3) or two independent pools of HEK293T cells with genetic inactivation of CRBN by CRISPR/Cas9 (shown is one representative experiment out of two replicates).

    Techniques Used: Incubation, Western Blot, CRISPR

    ZFP91 and IKZF1/3 share a common sequence motif. ( a ) In vitro ubiquitination of recombinant ZFP91 by recombinant N8 CRL4A CRBN is facilitated by lenalidomide (lanes 5–7), thalidomide (lane 8) and pomalidomide (lane 9). Shown is one representative experiment out of two replicates. ( b ) Alexa488-N8 CRL4A CRBN titrated to biotinylated wild-type ZFP91 at 100 nM in the presence of lenalidomide or DMSO as a control in presence of tracer Tb-streptavidin at 2 nM. Data are presented as means±s.d. ( n =3). ( c ) Multiple sequence alignment of the putative ZFP91, IKZF1 and IKZF3 degron motifs 11 . Identical amino acids, and structural residues of the ZnF motif, are highlighted in black and grey, respectively. ( d ) Titration of thalidomide, lenalidomide and pomalidomide to Alexa488-N8 CRL4A CRBN at 0.2 μM, biotin-ZFP91 at 0.1 μM and Tb-streptavidin at 2 nM. EC50 values are shown and indicate preference for pomalidomide in vitro . Data are presented as individual data points for one representative experiment out of four replicates. ( e ) MM.1S cells were treated with increasing concentrations of lenalidomide, thalidomide, pomalidomide or a DMSO control for 12 h. Co-treatment with the proteasome inhibitor bortezomib was included as an additional control. ZFP91 and GAPDH levels were detected using anti-ZFP91 or anti-GAPDH immunoblotting (shown is the data for one representative experiment).
    Figure Legend Snippet: ZFP91 and IKZF1/3 share a common sequence motif. ( a ) In vitro ubiquitination of recombinant ZFP91 by recombinant N8 CRL4A CRBN is facilitated by lenalidomide (lanes 5–7), thalidomide (lane 8) and pomalidomide (lane 9). Shown is one representative experiment out of two replicates. ( b ) Alexa488-N8 CRL4A CRBN titrated to biotinylated wild-type ZFP91 at 100 nM in the presence of lenalidomide or DMSO as a control in presence of tracer Tb-streptavidin at 2 nM. Data are presented as means±s.d. ( n =3). ( c ) Multiple sequence alignment of the putative ZFP91, IKZF1 and IKZF3 degron motifs 11 . Identical amino acids, and structural residues of the ZnF motif, are highlighted in black and grey, respectively. ( d ) Titration of thalidomide, lenalidomide and pomalidomide to Alexa488-N8 CRL4A CRBN at 0.2 μM, biotin-ZFP91 at 0.1 μM and Tb-streptavidin at 2 nM. EC50 values are shown and indicate preference for pomalidomide in vitro . Data are presented as individual data points for one representative experiment out of four replicates. ( e ) MM.1S cells were treated with increasing concentrations of lenalidomide, thalidomide, pomalidomide or a DMSO control for 12 h. Co-treatment with the proteasome inhibitor bortezomib was included as an additional control. ZFP91 and GAPDH levels were detected using anti-ZFP91 or anti-GAPDH immunoblotting (shown is the data for one representative experiment).

    Techniques Used: Sequencing, In Vitro, Recombinant, Titration

    9) Product Images from "Aqueous Extract of Cimicifuga dahurica Reprogramming Macrophage Polarization by Activating TLR4-NF-κB Signaling Pathway"

    Article Title: Aqueous Extract of Cimicifuga dahurica Reprogramming Macrophage Polarization by Activating TLR4-NF-κB Signaling Pathway

    Journal: Journal of Inflammation Research

    doi: 10.2147/JIR.S345497

    CRAE demonstrated its anti-tumor activity in the mouse xenograft model. ( A ) Time schedule of tumor implantation and drug therapy. ( B ) Measurement of tumor size. ( C ) Tumor volume and tumor weight. ( D ) Survival curves and body weight of different treatment types, such as Vehicle, CRAE, Bortezomib, or Combo treatment in SP2/0 xenograft mouse model (n = 8, one-way ANOVA or two-way ANOVA, * P
    Figure Legend Snippet: CRAE demonstrated its anti-tumor activity in the mouse xenograft model. ( A ) Time schedule of tumor implantation and drug therapy. ( B ) Measurement of tumor size. ( C ) Tumor volume and tumor weight. ( D ) Survival curves and body weight of different treatment types, such as Vehicle, CRAE, Bortezomib, or Combo treatment in SP2/0 xenograft mouse model (n = 8, one-way ANOVA or two-way ANOVA, * P

    Techniques Used: Activity Assay, Tumor Implantation

    10) Product Images from "BRD4 inhibitor and histone deacetylase inhibitor synergistically inhibit the proliferation of gallbladder cancer in vitro and in vivo, et al. BRD4 inhibitor and histone deacetylase inhibitor synergistically inhibit the proliferation of gallbladder cancer in vitro and in vivo"

    Article Title: BRD4 inhibitor and histone deacetylase inhibitor synergistically inhibit the proliferation of gallbladder cancer in vitro and in vivo, et al. BRD4 inhibitor and histone deacetylase inhibitor synergistically inhibit the proliferation of gallbladder cancer in vitro and in vivo

    Journal: Cancer Science

    doi: 10.1111/cas.14102

    JQ1 and suberoylanilide hydroxamic acid (SAHA) exerted anticancer effects through downregulation of BRD4 and suppression of PI3K/AKT and MAPK/ERK pathways. A, The BRD4 mRNA expression was determined by quantitative RT‐PCR. B, BRD4, histone deacetylases (HDAC), histone acetylation and autophagy level were detected by western blot. C, Expression levels of BRD4 and HDAC after pretreatment with bortezomib and then JQ1 and/or SAHA. D, Expression levels of PI3K/AKT and MAPK/ERK pathway proteins were determined by western blot. Significant differences are indicated by * P
    Figure Legend Snippet: JQ1 and suberoylanilide hydroxamic acid (SAHA) exerted anticancer effects through downregulation of BRD4 and suppression of PI3K/AKT and MAPK/ERK pathways. A, The BRD4 mRNA expression was determined by quantitative RT‐PCR. B, BRD4, histone deacetylases (HDAC), histone acetylation and autophagy level were detected by western blot. C, Expression levels of BRD4 and HDAC after pretreatment with bortezomib and then JQ1 and/or SAHA. D, Expression levels of PI3K/AKT and MAPK/ERK pathway proteins were determined by western blot. Significant differences are indicated by * P

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot

    11) Product Images from "ΔNp63α promotes Bortezomib resistance via the CYGB–ROS axis in head and neck squamous cell carcinoma"

    Article Title: ΔNp63α promotes Bortezomib resistance via the CYGB–ROS axis in head and neck squamous cell carcinoma

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-022-04790-0

    ΔNp63α regulates HNSCC cell to bortezomib resistance via ROS. A . Four strain cells were exposed to 10 nM bortezomib or to the same volume of PBS solution as a control. At the indicated times, cells were taken from culture and incubated in the presence of 10uM DCFH-DA for the determination of ROS generation. B . NAC was used to pre-protect UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 before exposure to bortezomib. IC50 was calculated using the CCK-8 assay. C . The histograms showed the DCF fluorescence intensity for evaluating ROS levels following bortezomib treatment (4 h) in HNSCC cells. The values reported are the mean±sd of three independent transfections. Comparisons were carried out between HN31-shΔNp63α and HN31-shNon, 17B-LvΔNp63α and 17B-LvNon, and 17B-R-5nM and 17B-R-10nM. * P
    Figure Legend Snippet: ΔNp63α regulates HNSCC cell to bortezomib resistance via ROS. A . Four strain cells were exposed to 10 nM bortezomib or to the same volume of PBS solution as a control. At the indicated times, cells were taken from culture and incubated in the presence of 10uM DCFH-DA for the determination of ROS generation. B . NAC was used to pre-protect UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 before exposure to bortezomib. IC50 was calculated using the CCK-8 assay. C . The histograms showed the DCF fluorescence intensity for evaluating ROS levels following bortezomib treatment (4 h) in HNSCC cells. The values reported are the mean±sd of three independent transfections. Comparisons were carried out between HN31-shΔNp63α and HN31-shNon, 17B-LvΔNp63α and 17B-LvNon, and 17B-R-5nM and 17B-R-10nM. * P

    Techniques Used: Incubation, CCK-8 Assay, Fluorescence, Transfection

    ΔNp63α regulates ROS of HNSCC cells via CYGB to affect drug resistance of HNSCC cells. A . The HN31 cell line was transfected with siRNA. After 24 h of transfection, Western-Blot verified the CYGB expression efficiency of three sequences (#298, #433, and#524). B . IC50 was calculated in HN31-siCYGB, HN31-siNon, 17BLvΔNp63α-siCYGB and 17BLvΔNp63α-siNon using CCK-8 assay. C . The histograms showed the DCF fluorescence intensity for evaluating ROS levels after bortezomib treatment (4 h) in HNSCC cells. Comparisons were performed between groups of HN31-siCYGB and HN31-siNon and between groups of 17BLvΔNp63α-siCYGB and 17BLvΔNp63α-siNon. * P
    Figure Legend Snippet: ΔNp63α regulates ROS of HNSCC cells via CYGB to affect drug resistance of HNSCC cells. A . The HN31 cell line was transfected with siRNA. After 24 h of transfection, Western-Blot verified the CYGB expression efficiency of three sequences (#298, #433, and#524). B . IC50 was calculated in HN31-siCYGB, HN31-siNon, 17BLvΔNp63α-siCYGB and 17BLvΔNp63α-siNon using CCK-8 assay. C . The histograms showed the DCF fluorescence intensity for evaluating ROS levels after bortezomib treatment (4 h) in HNSCC cells. Comparisons were performed between groups of HN31-siCYGB and HN31-siNon and between groups of 17BLvΔNp63α-siCYGB and 17BLvΔNp63α-siNon. * P

    Techniques Used: Transfection, Western Blot, Expressing, CCK-8 Assay, Fluorescence

    The bortezomib sensitivity of HNSCC is associated with the expression level of ΔNp63α. A UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 cells were treated with increasing concentrations of bortezomib (0.01–10000 nM) for 24 h, viable cells were quantified using the CCK-8 assay. Each data point represents the means ± SD of three separate experiments. B . Western blot was performed to analyze ΔNp63α proteins levels of UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 cells. C . Four cells were observed for ΔNp63α by immunostaining with antibody (green). Nuclei are counterstained with DAPI (blue). Scale bar: 20 μm. D . After “step-wise” inducing drug-resistance cell culture, 17B-R-10nM drug-resistant cell line that can proliferate in culture medium containing 10 nM bortezomib was obtained. IC50 of 17B-R-5nM and 17B-R-10nM were calculated using, CCK-8 assay. E . UMSCC-17B, 17B-R-5nM, and 17B-R-10nM were observed for ΔNp63α by immunostaining with antibody (green) Scale bar: 20 μm. F . Altered expressions of ΔNp63α were evaluated by western blot analysis in UMSCC-17B, 17B-R-5nM, and 17B-R-10nM.
    Figure Legend Snippet: The bortezomib sensitivity of HNSCC is associated with the expression level of ΔNp63α. A UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 cells were treated with increasing concentrations of bortezomib (0.01–10000 nM) for 24 h, viable cells were quantified using the CCK-8 assay. Each data point represents the means ± SD of three separate experiments. B . Western blot was performed to analyze ΔNp63α proteins levels of UMSCC-17B, UMSCC-11, UMSCC-17A, and HN31 cells. C . Four cells were observed for ΔNp63α by immunostaining with antibody (green). Nuclei are counterstained with DAPI (blue). Scale bar: 20 μm. D . After “step-wise” inducing drug-resistance cell culture, 17B-R-10nM drug-resistant cell line that can proliferate in culture medium containing 10 nM bortezomib was obtained. IC50 of 17B-R-5nM and 17B-R-10nM were calculated using, CCK-8 assay. E . UMSCC-17B, 17B-R-5nM, and 17B-R-10nM were observed for ΔNp63α by immunostaining with antibody (green) Scale bar: 20 μm. F . Altered expressions of ΔNp63α were evaluated by western blot analysis in UMSCC-17B, 17B-R-5nM, and 17B-R-10nM.

    Techniques Used: Expressing, CCK-8 Assay, Western Blot, Immunostaining, Cell Culture

    ΔNp63α knockdown causes HNSCC more sensitive to bortezomib and vice versa for ΔNp63α overexpression. A . After three interfering sequence lentiviruses were transfected into HN31 cells, ΔNp63α mRNA levels of these three cell strains were detected by qPCR, indicating that the knockdown efficiency of sequence 2 was the most obvious. And the results were verified by western blot. ** P
    Figure Legend Snippet: ΔNp63α knockdown causes HNSCC more sensitive to bortezomib and vice versa for ΔNp63α overexpression. A . After three interfering sequence lentiviruses were transfected into HN31 cells, ΔNp63α mRNA levels of these three cell strains were detected by qPCR, indicating that the knockdown efficiency of sequence 2 was the most obvious. And the results were verified by western blot. ** P

    Techniques Used: Over Expression, Sequencing, Transfection, Real-time Polymerase Chain Reaction, Western Blot

    ΔNp63α exerts a promotional effect on tumorigenesis and drug-resistance in vivo. A . BALB/c nude mice subcutaneous HNSCC tumors were given tail vein injections of bortezomib (Btz) or saline. The injection dose of bortezomib injection is 0.3 mg/kg, and they were injected every three days for 6 consecutive weeks. Mice of groups (HN31-shΔNp63α + Btz, HN31-shΔNp63α + Saline, HN31-shNon + Btz, and HN31-shNon + Saline) of the 38th day were shown above. B . Larger diameters and smaller diameters of the tumors were measured and the volume of the tumors was calculated in the following groups (HN31-shΔNp63α + Btz, HN31-shΔNp63α + Saline, HN31-shNon + Btz, HN31-shNon + Saline, 17B-LvΔNp63α + Btz, 17B-LvΔNp63α + Saline, 17B-LvNon + Btz, 17B-LvNon + saline, 17B-R-10nM + Btz, 17B-R-10nM + Saline, 17B-P + Saline, and 17B-P + Btz). * P
    Figure Legend Snippet: ΔNp63α exerts a promotional effect on tumorigenesis and drug-resistance in vivo. A . BALB/c nude mice subcutaneous HNSCC tumors were given tail vein injections of bortezomib (Btz) or saline. The injection dose of bortezomib injection is 0.3 mg/kg, and they were injected every three days for 6 consecutive weeks. Mice of groups (HN31-shΔNp63α + Btz, HN31-shΔNp63α + Saline, HN31-shNon + Btz, and HN31-shNon + Saline) of the 38th day were shown above. B . Larger diameters and smaller diameters of the tumors were measured and the volume of the tumors was calculated in the following groups (HN31-shΔNp63α + Btz, HN31-shΔNp63α + Saline, HN31-shNon + Btz, HN31-shNon + Saline, 17B-LvΔNp63α + Btz, 17B-LvΔNp63α + Saline, 17B-LvNon + Btz, 17B-LvNon + saline, 17B-R-10nM + Btz, 17B-R-10nM + Saline, 17B-P + Saline, and 17B-P + Btz). * P

    Techniques Used: In Vivo, Mouse Assay, Injection

    12) Product Images from "Chorioallantoic membrane (CAM) assay to study treatment effects in diffuse intrinsic pontine glioma"

    Article Title: Chorioallantoic membrane (CAM) assay to study treatment effects in diffuse intrinsic pontine glioma

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0263822

    Analysis of tumor vascularity of DIPGXIIIp* and DIPGIV CAM tumors following drug treatment. DIPGXIIIp* (A) and DIPGIV (B) CAM tumors were treated with alisertib, bortezomib, MSN1-Leu, panobinostat, ponatinib and bevacizumab on embryonic development days 11, 13 and 15. Tumor vascularity was assessed following 3-D ultrasound on embryonic development day 16. Vehicle is 0.5% DMSO in sterile PBS. PBS control is 100% sterile PBS. Differences were determined with one-way ANOVA and Dunnett’s test for multiple comparisons where P
    Figure Legend Snippet: Analysis of tumor vascularity of DIPGXIIIp* and DIPGIV CAM tumors following drug treatment. DIPGXIIIp* (A) and DIPGIV (B) CAM tumors were treated with alisertib, bortezomib, MSN1-Leu, panobinostat, ponatinib and bevacizumab on embryonic development days 11, 13 and 15. Tumor vascularity was assessed following 3-D ultrasound on embryonic development day 16. Vehicle is 0.5% DMSO in sterile PBS. PBS control is 100% sterile PBS. Differences were determined with one-way ANOVA and Dunnett’s test for multiple comparisons where P

    Techniques Used: Chick Chorioallantoic Membrane Assay

    Volumetric analysis of DIPGXIIIp* and DIPGIV CAM tumors following drug treatment. DIPGXIIIp* (A) and DIPGIV (B) CAM tumors were treated with alisertib, bortezomib, MSN1-Leu, panobinostat, ponatinib and bevacizumab on embryonic development days 11, 13 and 15. Tumor volume was determined following 3-D ultrasound on embryonic development day 16. Vehicle is 0.5% DMSO in sterile PBS. PBS control is 100% sterile PBS. Differences were determined with one-way ANOVA and Dunnett’s test for multiple comparisons where P
    Figure Legend Snippet: Volumetric analysis of DIPGXIIIp* and DIPGIV CAM tumors following drug treatment. DIPGXIIIp* (A) and DIPGIV (B) CAM tumors were treated with alisertib, bortezomib, MSN1-Leu, panobinostat, ponatinib and bevacizumab on embryonic development days 11, 13 and 15. Tumor volume was determined following 3-D ultrasound on embryonic development day 16. Vehicle is 0.5% DMSO in sterile PBS. PBS control is 100% sterile PBS. Differences were determined with one-way ANOVA and Dunnett’s test for multiple comparisons where P

    Techniques Used: Chick Chorioallantoic Membrane Assay

    13) Product Images from "Fragment-Sized and Bidentate (Immuno)Proteasome Inhibitors Derived from Cysteine and Threonine Targeting Warheads"

    Article Title: Fragment-Sized and Bidentate (Immuno)Proteasome Inhibitors Derived from Cysteine and Threonine Targeting Warheads

    Journal: Cells

    doi: 10.3390/cells10123431

    Structure of 2-vinylthiazole ( XXI ), bortezomib ( XXII ), and the designed compound 28 . The boron-bearing warhead is marked with green circle and the 2-vinylthiazole is marked with red circle.
    Figure Legend Snippet: Structure of 2-vinylthiazole ( XXI ), bortezomib ( XXII ), and the designed compound 28 . The boron-bearing warhead is marked with green circle and the 2-vinylthiazole is marked with red circle.

    Techniques Used:

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    MedChemExpress bortezomib
    EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, <t>bortezomib</t> (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p
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    EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, bortezomib (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p

    Journal: Cell Death & Disease

    Article Title: ALCAM regulates multiple myeloma chemoresistant side population

    doi: 10.1038/s41419-022-04556-8

    Figure Lengend Snippet: EGFR-targeting therapy attenuates side population conferred myeloma chemoresistance in vivo. A Scheme graph showing the animal study to evaluate the efficacy of the combination therapy (Mel and EGFR inhibitor) in vivo. The mice were treated by intraperitoneal injection of melphalan (60 μg/mouse per time, 4 times within 10 days) or gefitinib (500 μg/mouse per time, 4 times within 10 days), or a combination of both. Each group contained 8 mice. B Tumor-bearing mice were subjected to in vivo bioluminescent imaging (IVIS) before and after treatment. Five out of seven representative results are shown. C The relative luciferase activity of IVIS was calculated. D The tumor-bearing mice were treated twice as described above. Then, mice BM cells were analyzed by Hoechst staining for MM SP in vivo. Two out of three representative results are shown in the left panel, and result quantification is shown in the right panel. E Tumor burden was evaluated by circulating IgG2b. F Treatment efficacy was evaluated by mouse survival. G MM tumor-bearing mice were treated by intraperitoneal injection of PBS, bortezomib (15 μg/mouse per time, 4 times within 10 days), or a combination of bortezomib and gefitinib (500 μg/mouse per time, 4 times within 10 days). The PBS group contained 4 mice; the other treated group each contained 6 mice. Tumor burden was evaluated by circulating IgG2b. H Treatment efficacy was evaluated by mouse survival (* p

    Article Snippet: Melphalan (#148-82-3) and bortezomib (#179324-69-7) were ordered from MedChemExpress.

    Techniques: In Vivo, Mouse Assay, Injection, Imaging, Luciferase, Activity Assay, Staining

    ALCAM regulates myeloma chemoresistant side population in vitro. A MM cells RPMI8226, either CTR-KD or AL-KD, were treated with melphalan (Mel, 15 μM) or bortezomib (BTZ, 5 nM) for 24 h. The SP cell ratio was examined by Hoechst staining. B The RPMI8226 cells were treated by melphalan as described above. The cell cycle was analyzed after Hoechst staining. C Cell-cycle quantification. D After Hoechst staining, the apoptotic cells were analyzed by annexin V staining. E ALCAM and EGFR expression on MM cells after Mel or BTZ treatment were detected by flow cytometry. MFI mean fluorescence index. F Examination of SP cells after EGFR inhibitor (gefitinib, 200 nM) and melphalan treatment. Data are the mean of three independent experiments in three replicates. * p

    Journal: Cell Death & Disease

    Article Title: ALCAM regulates multiple myeloma chemoresistant side population

    doi: 10.1038/s41419-022-04556-8

    Figure Lengend Snippet: ALCAM regulates myeloma chemoresistant side population in vitro. A MM cells RPMI8226, either CTR-KD or AL-KD, were treated with melphalan (Mel, 15 μM) or bortezomib (BTZ, 5 nM) for 24 h. The SP cell ratio was examined by Hoechst staining. B The RPMI8226 cells were treated by melphalan as described above. The cell cycle was analyzed after Hoechst staining. C Cell-cycle quantification. D After Hoechst staining, the apoptotic cells were analyzed by annexin V staining. E ALCAM and EGFR expression on MM cells after Mel or BTZ treatment were detected by flow cytometry. MFI mean fluorescence index. F Examination of SP cells after EGFR inhibitor (gefitinib, 200 nM) and melphalan treatment. Data are the mean of three independent experiments in three replicates. * p

    Article Snippet: Melphalan (#148-82-3) and bortezomib (#179324-69-7) were ordered from MedChemExpress.

    Techniques: In Vitro, Staining, Expressing, Flow Cytometry, Fluorescence

    Extended validation of SALL4. ( A ) HEK293T cells were treated with increasing concentrations of thalidomide, lenalidomide, pomalidomide, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( B ) As in ( A ), but with H661 cells. ( C ) As in ( A ), but with SK-N-DZ cells. ( D ) HEK293T cells were treated with increasing concentrations of thalidomide and co-treated with 5 µM bortezomib, 5 µM MLN4924, 0.5 µM MLN7243, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( E ) As in ( D ), but with SK-N-DZ cells. ( F ) Parental HEK293T cells or two independent pools of CRBN -/- HEK293T cells were treated with increasing concentrations of thalidomide. Following 24 h incubation, SALL4, CRBN, and GAPDH protein levels were assessed by western blot analysis. ( G ) Kelly cells were treated with 1 µM pomalidomide or DMSO as a control for 8 h, at which point the compound was washed out. Cells were harvested at 1, 2, 4, 8, 24, and 48 h post-washout, and SALL4 and GAPDH protein levels were assessed by western blot analysis. ( H ) Kelly cells were treated with 1 µM pomalidomide for 1, 2, 4, 8, and 24 h, or with DMSO as a control. Following time course treatment, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( I ) Thalidomide treatment did not influence the expression of SALL4 mRNA. hES cells treated with 10 µM thalidomide or DMSO as a control for 24 h were subjected to quantitative RT-PCR to assess the levels of total SALL4 mRNA. The mRNA levels were normalized to those of GAPDH (housekeeping gene) mRNA. The SALL4 mRNA level remained stable or increased, which is in contrast to the decrease in protein abundance observed in proteomics and western blot analysis. mRNA fold change was determined from n = 2 with three technical replicates. ( J ) To validate the specificity of the antibody used, we transfected Kelly or HEK293T cells with a plasmid expressing mCherry, Cas9, and one of three guide RNAs (sgRNA1, sgRNA2, sgRNA3) targeting the SALL4 gene, or a mock control. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis and for sgRNA1 and sgRNA2 a loss of the specific bands for SALL4 was observed in accordance with the antibody being specific for SALL4. sgRNA3 had no effect, which is likely to be because of an ineffective sgRNA. ( K ) To validate the specificity of the antibody used, we transfected Kelly cells with a plasmid overexpressing Flag-mmSALL4, Flag-hsSALL4, or no transfection. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. One representative experiment is shown in this figure, from three replicates for each of the western blots.

    Journal: eLife

    Article Title: Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome

    doi: 10.7554/eLife.38430

    Figure Lengend Snippet: Extended validation of SALL4. ( A ) HEK293T cells were treated with increasing concentrations of thalidomide, lenalidomide, pomalidomide, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( B ) As in ( A ), but with H661 cells. ( C ) As in ( A ), but with SK-N-DZ cells. ( D ) HEK293T cells were treated with increasing concentrations of thalidomide and co-treated with 5 µM bortezomib, 5 µM MLN4924, 0.5 µM MLN7243, or DMSO as a control. Following 24 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( E ) As in ( D ), but with SK-N-DZ cells. ( F ) Parental HEK293T cells or two independent pools of CRBN -/- HEK293T cells were treated with increasing concentrations of thalidomide. Following 24 h incubation, SALL4, CRBN, and GAPDH protein levels were assessed by western blot analysis. ( G ) Kelly cells were treated with 1 µM pomalidomide or DMSO as a control for 8 h, at which point the compound was washed out. Cells were harvested at 1, 2, 4, 8, 24, and 48 h post-washout, and SALL4 and GAPDH protein levels were assessed by western blot analysis. ( H ) Kelly cells were treated with 1 µM pomalidomide for 1, 2, 4, 8, and 24 h, or with DMSO as a control. Following time course treatment, SALL4 and GAPDH protein levels were assessed by western blot analysis. ( I ) Thalidomide treatment did not influence the expression of SALL4 mRNA. hES cells treated with 10 µM thalidomide or DMSO as a control for 24 h were subjected to quantitative RT-PCR to assess the levels of total SALL4 mRNA. The mRNA levels were normalized to those of GAPDH (housekeeping gene) mRNA. The SALL4 mRNA level remained stable or increased, which is in contrast to the decrease in protein abundance observed in proteomics and western blot analysis. mRNA fold change was determined from n = 2 with three technical replicates. ( J ) To validate the specificity of the antibody used, we transfected Kelly or HEK293T cells with a plasmid expressing mCherry, Cas9, and one of three guide RNAs (sgRNA1, sgRNA2, sgRNA3) targeting the SALL4 gene, or a mock control. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis and for sgRNA1 and sgRNA2 a loss of the specific bands for SALL4 was observed in accordance with the antibody being specific for SALL4. sgRNA3 had no effect, which is likely to be because of an ineffective sgRNA. ( K ) To validate the specificity of the antibody used, we transfected Kelly cells with a plasmid overexpressing Flag-mmSALL4, Flag-hsSALL4, or no transfection. Following 48 h incubation, SALL4 and GAPDH protein levels were assessed by western blot analysis. One representative experiment is shown in this figure, from three replicates for each of the western blots.

    Article Snippet: Compounds, enzymes, and antibodiesThalidomide (HY-14658, MedChemExpress), lenalidomide (HY-A0003, MedChemExpress), pomalidomide (HY-10984, MedChemExpress), CC-220 (HY-101291, MedChemExpress), CC-885 (19966, Cayman chemical), dBET57 , bortezomib (HY-10227, MedChemExpress), MLN4924 (HY-70062, MedChemExpress), and MLN7243 (A1384, Active Biochem) were purchased from the indicated vendors and subjected to in-house LC-MS for quality control.

    Techniques: Incubation, Western Blot, Expressing, Quantitative RT-PCR, Transfection, Plasmid Preparation

    Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 is effective in suppressing the growth and overcoming bortezomib resistance in bortezomib-resistant MM cells. (A) Bortezomib naïve (WT) and resistant (BTZR) myeloma cells (RPMI-8226 and NCI-H929 cells) were treated with various concentrations of bortezomib for 48 h, and the IC 50 was calculated and shown. (B) Protein levels of p-ERK and ERK of the parental and bortezomib-resistant myeloma cells were detected by Western blot analysis. The bar graph illustrates the quantitative comparison of different proteins levels. (C,D) Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 in bortezomib-resistant myeloma cells (BTZR) conferred a similar growth inhibition effect to that of bortezomib-naïve myeloma cells (WT). (E,F) After incubation with 20 µM SHP099 or 10 µM RMC-4550 in RPMI-8226 and NCI-H929 cells for 48 h, Western blots against p-SHP2, SHP2, p-ERK, ERK, P21, BAK, and cleaved caspase-3 were performed and quantified. (G) Bortezomib-resistant (RPMI-8226 BTZR or NCI-H929 BTZR) cells were treated with either bortezomib (50 nM), SHP2 inhibitors (20 μM SHP099 or 10 μM RMC-4550), or the combination for 48 h, followed by assessment for cell viability. (H) Bortezomib-resistant MM cells were incubated with different doses of BTZ and SHP2 inhibitors (SHP099 or RMC-4550) or with the combination of both for 48 h; the synergistic cytotoxic effects were determined using the combination index based on the data from cell viability assays. x-axis, fractional effect concentrations; y-axis, CI. Data were displayed as mean ± SD from three independent experiments. * p

    Journal: Frontiers in Pharmacology

    Article Title: SHP2 Inhibitors Show Anti-Myeloma Activity and Synergize With Bortezomib in the Treatment of Multiple Myeloma

    doi: 10.3389/fphar.2022.841308

    Figure Lengend Snippet: Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 is effective in suppressing the growth and overcoming bortezomib resistance in bortezomib-resistant MM cells. (A) Bortezomib naïve (WT) and resistant (BTZR) myeloma cells (RPMI-8226 and NCI-H929 cells) were treated with various concentrations of bortezomib for 48 h, and the IC 50 was calculated and shown. (B) Protein levels of p-ERK and ERK of the parental and bortezomib-resistant myeloma cells were detected by Western blot analysis. The bar graph illustrates the quantitative comparison of different proteins levels. (C,D) Pharmacological inhibition of SHP2 with SHP099 or RMC-4550 in bortezomib-resistant myeloma cells (BTZR) conferred a similar growth inhibition effect to that of bortezomib-naïve myeloma cells (WT). (E,F) After incubation with 20 µM SHP099 or 10 µM RMC-4550 in RPMI-8226 and NCI-H929 cells for 48 h, Western blots against p-SHP2, SHP2, p-ERK, ERK, P21, BAK, and cleaved caspase-3 were performed and quantified. (G) Bortezomib-resistant (RPMI-8226 BTZR or NCI-H929 BTZR) cells were treated with either bortezomib (50 nM), SHP2 inhibitors (20 μM SHP099 or 10 μM RMC-4550), or the combination for 48 h, followed by assessment for cell viability. (H) Bortezomib-resistant MM cells were incubated with different doses of BTZ and SHP2 inhibitors (SHP099 or RMC-4550) or with the combination of both for 48 h; the synergistic cytotoxic effects were determined using the combination index based on the data from cell viability assays. x-axis, fractional effect concentrations; y-axis, CI. Data were displayed as mean ± SD from three independent experiments. * p

    Article Snippet: SHP099 (HY-100388A) and bortezomib (HY-10227) were purchased from MedChemExpress (Princeton, NJ, United States).

    Techniques: Inhibition, Western Blot, Incubation

    Combination of RMC-4550 and BTZ exhibits a synergistic antitumor effect against MM cells. (A) Cytotoxic effects of various doses of RMC-4550 and BTZ in monotherapy and in combination on MM cells determined by the CCK-8 assay. Fa-CI plot analysis of combination treatment of the two on RPMI-8226 and NCI-H929 cell viability was performed. x-axis, fractional effect concentrations; y-axis, CI. RPMI-8226 and NCI-H929 cells were culture in the presence of DMSO, RMC-4550 (10 μM), BTZ (3 nM for RPMI-8226 and 2 nM for NCI-H929 cells), or RMC-4550 plus BTZ for 48 h, and then colony formation (B) , cell apoptosis (C), and cell cycle (D) were measured. The representative flow cytometric profiles of BrdU/Hoechst 33342 are shown. (E) Western blotting shows the levels of P21, BAK, and cleaved caspase-3 in myeloma cells with monotherapy or the combination of bortezomib and RMC4550 for 48 h. GAPDH served as a loading control. The graphs show the density volumes of the indicated proteins normalized to those in the control. Data were displayed as mean ± SD from three independent experiments. * p

    Journal: Frontiers in Pharmacology

    Article Title: SHP2 Inhibitors Show Anti-Myeloma Activity and Synergize With Bortezomib in the Treatment of Multiple Myeloma

    doi: 10.3389/fphar.2022.841308

    Figure Lengend Snippet: Combination of RMC-4550 and BTZ exhibits a synergistic antitumor effect against MM cells. (A) Cytotoxic effects of various doses of RMC-4550 and BTZ in monotherapy and in combination on MM cells determined by the CCK-8 assay. Fa-CI plot analysis of combination treatment of the two on RPMI-8226 and NCI-H929 cell viability was performed. x-axis, fractional effect concentrations; y-axis, CI. RPMI-8226 and NCI-H929 cells were culture in the presence of DMSO, RMC-4550 (10 μM), BTZ (3 nM for RPMI-8226 and 2 nM for NCI-H929 cells), or RMC-4550 plus BTZ for 48 h, and then colony formation (B) , cell apoptosis (C), and cell cycle (D) were measured. The representative flow cytometric profiles of BrdU/Hoechst 33342 are shown. (E) Western blotting shows the levels of P21, BAK, and cleaved caspase-3 in myeloma cells with monotherapy or the combination of bortezomib and RMC4550 for 48 h. GAPDH served as a loading control. The graphs show the density volumes of the indicated proteins normalized to those in the control. Data were displayed as mean ± SD from three independent experiments. * p

    Article Snippet: SHP099 (HY-100388A) and bortezomib (HY-10227) were purchased from MedChemExpress (Princeton, NJ, United States).

    Techniques: CCK-8 Assay, Western Blot

    Drug efficacy can be modulated by targeting reactive oxygen species (ROS) metabolism. (A) The drug efficacies of bortezomib and docetaxel were assessed by adding a low concentration of H 2 O 2 together as assessed by cell proliferation assay. The antitumor efficacy of these two drugs was diminished by exogenous ROS. Error bars indicate the mean ± SD; ns = no significance, * p

    Journal: Frontiers in Oncology

    Article Title: Characterization of ROS Metabolic Equilibrium Reclassifies Pan-Cancer Samples and Guides Pathway Targeting Therapy

    doi: 10.3389/fonc.2020.581197

    Figure Lengend Snippet: Drug efficacy can be modulated by targeting reactive oxygen species (ROS) metabolism. (A) The drug efficacies of bortezomib and docetaxel were assessed by adding a low concentration of H 2 O 2 together as assessed by cell proliferation assay. The antitumor efficacy of these two drugs was diminished by exogenous ROS. Error bars indicate the mean ± SD; ns = no significance, * p

    Article Snippet: Bortezomib (MCE, NJ, USA) was administered (0.40 mg/kg) i.p. every 3 days after the animals were assigned to different groups.

    Techniques: Concentration Assay, Proliferation Assay