sb202190  (Cell Signaling Technology Inc)

 
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    Name:
    SB202190
    Description:
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    Catalog Number:
    8158
    Price:
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    Category:
    Activators Inhibitors
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    Structured Review

    Cell Signaling Technology Inc sb202190
    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor <t>SB202190.</t> The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Molecular Weight
    https://www.bioz.com/result/sb202190/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
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    sb202190 - by Bioz Stars, 2021-03
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    Images

    1) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    2) Product Images from "Autophagy down regulates pro-inflammatory mediators in BV2 microglial cells and rescues both LPS and alpha-synuclein induced neuronal cell death"

    Article Title: Autophagy down regulates pro-inflammatory mediators in BV2 microglial cells and rescues both LPS and alpha-synuclein induced neuronal cell death

    Journal: Scientific Reports

    doi: 10.1038/srep43153

    Autophagy modulation of p38 and ERK signalling in LPS and α-synuclein-stimulated BV2 microglial cells. ( A ) BV2 cells were stimulated with LPS (0,5 ug/mL) or alpha-synuclein fibers (10 uM) for 15 to 120 minutes. ( B ) BV2 cells were cultured in the presence or absence of PD98059 (50 uM) SB202190 (20 uM) for 1 h or treated with rapamycin (100 nm) or trehalose (30 mM) for 24 h. After that, microglial cells were stimulated with LPS (0,5 ug/mL) or alpha-synuclein fibers (10 uM) for 30 and 60 minutes, respectively. Cells were lysed and p38, p-p38, ERK1/2, p-ERK1/2 and b-actin levels were analysed by Western immunoblotting. Quantification by densitometry of p-p38 ( C ) or p-ERK1/2 ( D ) from B relative to p38 or ERK1/2, respectively. (One-way ANOVA followed by Post-Hoc Dunnet’s test; n = 3). Error bars represent SEM (*P
    Figure Legend Snippet: Autophagy modulation of p38 and ERK signalling in LPS and α-synuclein-stimulated BV2 microglial cells. ( A ) BV2 cells were stimulated with LPS (0,5 ug/mL) or alpha-synuclein fibers (10 uM) for 15 to 120 minutes. ( B ) BV2 cells were cultured in the presence or absence of PD98059 (50 uM) SB202190 (20 uM) for 1 h or treated with rapamycin (100 nm) or trehalose (30 mM) for 24 h. After that, microglial cells were stimulated with LPS (0,5 ug/mL) or alpha-synuclein fibers (10 uM) for 30 and 60 minutes, respectively. Cells were lysed and p38, p-p38, ERK1/2, p-ERK1/2 and b-actin levels were analysed by Western immunoblotting. Quantification by densitometry of p-p38 ( C ) or p-ERK1/2 ( D ) from B relative to p38 or ERK1/2, respectively. (One-way ANOVA followed by Post-Hoc Dunnet’s test; n = 3). Error bars represent SEM (*P

    Techniques Used: Cell Culture, Western Blot

    Modulation of LPS-induced neuronal cell death by inducing microglial autophagy. ( A ) BV2 and N2A cells were co-cultured in a 1:1 ratio and left untreated or stimulated with LPS for 48 h. Firstly, BV2 microglial cells were treated with rapamycin, trehalose, SB202190 (20 uM) or PD98059 (50 uM). After 24 h, BV2 cells were co-cultured with N2A cells and stimulated with LPS for 48 h. After that, cell death was evaluated using propidium iodide (PI) combined with anti-CD11b staining and subsequent flow cytometric analysis. ( B–D ) Percentages of neuronal CD11b−/IP+ and microglial CD11b+/IP+ cell death were determined and analyzed statistically by one-way ANOVA followed by Post-Hoc Dunnet’s test; n = 3. Error bars represent SEM (***P
    Figure Legend Snippet: Modulation of LPS-induced neuronal cell death by inducing microglial autophagy. ( A ) BV2 and N2A cells were co-cultured in a 1:1 ratio and left untreated or stimulated with LPS for 48 h. Firstly, BV2 microglial cells were treated with rapamycin, trehalose, SB202190 (20 uM) or PD98059 (50 uM). After 24 h, BV2 cells were co-cultured with N2A cells and stimulated with LPS for 48 h. After that, cell death was evaluated using propidium iodide (PI) combined with anti-CD11b staining and subsequent flow cytometric analysis. ( B–D ) Percentages of neuronal CD11b−/IP+ and microglial CD11b+/IP+ cell death were determined and analyzed statistically by one-way ANOVA followed by Post-Hoc Dunnet’s test; n = 3. Error bars represent SEM (***P

    Techniques Used: Cell Culture, Staining, Flow Cytometry

    3) Product Images from "6-Shogaol-Rich Extract from Ginger Up-Regulates the Antioxidant Defense Systems in Cells and Mice "

    Article Title: 6-Shogaol-Rich Extract from Ginger Up-Regulates the Antioxidant Defense Systems in Cells and Mice

    Journal: Molecules

    doi: 10.3390/molecules17078037

    Effects of ginger extracts on the phosphorylations of upstream targets in HepG2 cells. ( A ) Effect of ginger extracts on phosphorylation of MAPKs and Akt. HepG2 cells were treated with 50 µg/mL ginger extracts for 1 h; ( B ) Influence of MAPK inhibitors on GEE8080-induced Nrf2 and HO-1 expression. HepG2 cells pretreated with vehicle or 50 μM U0126 (MEK1/2 inhibitor), SP600125 (JNK inhibitor), SB202190 (p38 inhibitor), and LY294002 (Akt inhibitor) for 1 h prior to treatment with 50 μg/mL GEE8080 for 1 h. The blots are shown representative of three independent experiments with similar results and data represent the means ± S.D. Locations for each concentration marked letters are significantly different at * p
    Figure Legend Snippet: Effects of ginger extracts on the phosphorylations of upstream targets in HepG2 cells. ( A ) Effect of ginger extracts on phosphorylation of MAPKs and Akt. HepG2 cells were treated with 50 µg/mL ginger extracts for 1 h; ( B ) Influence of MAPK inhibitors on GEE8080-induced Nrf2 and HO-1 expression. HepG2 cells pretreated with vehicle or 50 μM U0126 (MEK1/2 inhibitor), SP600125 (JNK inhibitor), SB202190 (p38 inhibitor), and LY294002 (Akt inhibitor) for 1 h prior to treatment with 50 μg/mL GEE8080 for 1 h. The blots are shown representative of three independent experiments with similar results and data represent the means ± S.D. Locations for each concentration marked letters are significantly different at * p

    Techniques Used: Expressing, Concentration Assay

    4) Product Images from "The Apparent Requirement for Protein Synthesis during G2 Phase Is due to Checkpoint Activation"

    Article Title: The Apparent Requirement for Protein Synthesis during G2 Phase Is due to Checkpoint Activation

    Journal: Cell reports

    doi: 10.1016/j.celrep.2020.107901

    Measuring the Duration of Cell Cycle Phases Using Fluorescently Labeled PCNA and Histone H2B in MCF10A Cells (A) Schematic of the regulation of Cdk1 activity at the G2/M transition by cyclins and multiple feedback loops. The protein synthesis inhibitor cycloheximide (CHX) can block cyclin accumulation; it also activates p38 MAPK, which can delay G2/M progression by inhibiting Cdc25 and/or potentially activating Wee1/Myt1 ( Reinhardt and Yaffe, 2009 ). The small-molecule inhibitors SB202190 and SB203580 and PD0166285 and MK-1775 have been used in this study to inhibit p38 MAPK or Wee1/Myt1 activity, respectively. (B) eYFP-PCNA can be used to determine the onset of S phase, the completion of S phase, and the onset of mitosis (nuclear envelope breakdown); histone H2B-mTurquoise (used here) or histone H2B-mCherry can be used to determine anaphase onset. Scale bars: 10 μm. (C) Three examples of cells showing the disappearance of eYFP-PCNA foci (yellow arrows) at the end of S phase. Times (in the format h:min) were aligned to the time of entry into G2 phase. Scale bars: 10 μm. (D) Frequency distributions of G2 phase duration measured in MCF10A cells expressing H2B-mCherry and eYFP-PCNA either in the absence (“medium,” gray; n = 104) or presence of 0.1% DMSO (blue; n = 100). Means and standard deviations are indicated.
    Figure Legend Snippet: Measuring the Duration of Cell Cycle Phases Using Fluorescently Labeled PCNA and Histone H2B in MCF10A Cells (A) Schematic of the regulation of Cdk1 activity at the G2/M transition by cyclins and multiple feedback loops. The protein synthesis inhibitor cycloheximide (CHX) can block cyclin accumulation; it also activates p38 MAPK, which can delay G2/M progression by inhibiting Cdc25 and/or potentially activating Wee1/Myt1 ( Reinhardt and Yaffe, 2009 ). The small-molecule inhibitors SB202190 and SB203580 and PD0166285 and MK-1775 have been used in this study to inhibit p38 MAPK or Wee1/Myt1 activity, respectively. (B) eYFP-PCNA can be used to determine the onset of S phase, the completion of S phase, and the onset of mitosis (nuclear envelope breakdown); histone H2B-mTurquoise (used here) or histone H2B-mCherry can be used to determine anaphase onset. Scale bars: 10 μm. (C) Three examples of cells showing the disappearance of eYFP-PCNA foci (yellow arrows) at the end of S phase. Times (in the format h:min) were aligned to the time of entry into G2 phase. Scale bars: 10 μm. (D) Frequency distributions of G2 phase duration measured in MCF10A cells expressing H2B-mCherry and eYFP-PCNA either in the absence (“medium,” gray; n = 104) or presence of 0.1% DMSO (blue; n = 100). Means and standard deviations are indicated.

    Techniques Used: Labeling, Activity Assay, Blocking Assay, Expressing

    p38 MAPK Inhibition Allows Cells to Enter Mitosis in the Presence of Cycloheximide (A) Asynchronously growing cells were treated for 6 h with DMSO, cycloheximide, or cycloheximide plus either of the p38 MAPK inhibitors SB202190 or SB203580. The phosphorylation state of p38 as well as the phosphorylation state of the p38 substrate Hsp27 was analyzed by immunoblotting to assess the activation state of p38. Uncropped immunoblots are shown in Figure S6B . (B) Montages of MCF10A cells expressing H2B-mCherry and eYFP-PCNA followed over the time course of the experiment described in Figure 3A treated with cycloheximide or cycloheximide plus either SB202190 or SB203580. Times (in the format h:min) were aligned to the point of drug addition. (C) Cell cycle progression for MCF10A cells expressing H2B-mCherry and eYFP-PCNA treated with DMSO (n = 99), CHX (n = 100), SB202190 (n = 92), SB203580 (n = 90), CHX+SB202190 (n = 95), or CHX+SB203580 (n = 91). Each row represents timing data from a single cell. The majority of cells treated with cycloheximide arrested in G2 phase, whereas cells treated with CHX plus SB202190 or SB203580 (50 μM) progressed into mitosis in most cases. Rows marked with a purple square denote cells that underwent abnormal mitoses, often lacking proper metaphase and cytokinesis. (D) Logistic regression analysis. Probability of a cell to enter mitosis as a function of how long the cell has already been in G2 phase at the time of drug addition for the experiment shown in (C). Circles indicate the fraction of cells that entered mitosis by 5 h after entry into G2 phase; this cutoff was the time at which 95% of the DMSO-treated control cells had entered mitosis. The solid lines show the logistic fit for the data, and the lightly colored areas indicate the 95% confidence intervals. (E) Mitotic indices for MCF10A cells expressing H2B-mCherry and eYFP-PCNA cells treated with DMSO, CHX, SB202190, SB203580, CHX+SB202190, or CHX+SB203580. At least 3,672 cells were counted for each time point. An additional similar experiment is shown in Figures S4A and S4B .
    Figure Legend Snippet: p38 MAPK Inhibition Allows Cells to Enter Mitosis in the Presence of Cycloheximide (A) Asynchronously growing cells were treated for 6 h with DMSO, cycloheximide, or cycloheximide plus either of the p38 MAPK inhibitors SB202190 or SB203580. The phosphorylation state of p38 as well as the phosphorylation state of the p38 substrate Hsp27 was analyzed by immunoblotting to assess the activation state of p38. Uncropped immunoblots are shown in Figure S6B . (B) Montages of MCF10A cells expressing H2B-mCherry and eYFP-PCNA followed over the time course of the experiment described in Figure 3A treated with cycloheximide or cycloheximide plus either SB202190 or SB203580. Times (in the format h:min) were aligned to the point of drug addition. (C) Cell cycle progression for MCF10A cells expressing H2B-mCherry and eYFP-PCNA treated with DMSO (n = 99), CHX (n = 100), SB202190 (n = 92), SB203580 (n = 90), CHX+SB202190 (n = 95), or CHX+SB203580 (n = 91). Each row represents timing data from a single cell. The majority of cells treated with cycloheximide arrested in G2 phase, whereas cells treated with CHX plus SB202190 or SB203580 (50 μM) progressed into mitosis in most cases. Rows marked with a purple square denote cells that underwent abnormal mitoses, often lacking proper metaphase and cytokinesis. (D) Logistic regression analysis. Probability of a cell to enter mitosis as a function of how long the cell has already been in G2 phase at the time of drug addition for the experiment shown in (C). Circles indicate the fraction of cells that entered mitosis by 5 h after entry into G2 phase; this cutoff was the time at which 95% of the DMSO-treated control cells had entered mitosis. The solid lines show the logistic fit for the data, and the lightly colored areas indicate the 95% confidence intervals. (E) Mitotic indices for MCF10A cells expressing H2B-mCherry and eYFP-PCNA cells treated with DMSO, CHX, SB202190, SB203580, CHX+SB202190, or CHX+SB203580. At least 3,672 cells were counted for each time point. An additional similar experiment is shown in Figures S4A and S4B .

    Techniques Used: Inhibition, Activation Assay, Western Blot, Expressing

    5) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    6) Product Images from "Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases"

    Article Title: Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2016.417

    Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.

    Techniques Used: Staining

    Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.

    Techniques Used: Inhibition, Mouse Assay, Injection

    7) Product Images from "Inhibition of leptin-induced vascular extracellular matrix remodelling by adiponectin"

    Article Title: Inhibition of leptin-induced vascular extracellular matrix remodelling by adiponectin

    Journal: Journal of Molecular Endocrinology

    doi: 10.1530/JME-14-0027

    Effects of different blockers on the expression of SOCS3 in 3D models pre-treated with leptin and adiponectin. When compared with the control, the relative protein levels of SOCS3 in the compound C group, PD98059 group, okadaic acid group and SB202190 group were 0.41, 0.94, 0.98 and 0.93 respectively. n =6. * P
    Figure Legend Snippet: Effects of different blockers on the expression of SOCS3 in 3D models pre-treated with leptin and adiponectin. When compared with the control, the relative protein levels of SOCS3 in the compound C group, PD98059 group, okadaic acid group and SB202190 group were 0.41, 0.94, 0.98 and 0.93 respectively. n =6. * P

    Techniques Used: Expressing

    8) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    9) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    10) Product Images from "Targeting steroid receptor RNA activator (SRA), a long non-coding RNA, enhances melanogenesis through activation of TRP1 and inhibition of p38 phosphorylation"

    Article Title: Targeting steroid receptor RNA activator (SRA), a long non-coding RNA, enhances melanogenesis through activation of TRP1 and inhibition of p38 phosphorylation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0237577

    (A) Constitutive activation of p38 was obliterated in SRA-deficient B16 cells. The expression of total and phosphorylated p38 as well as cleaved Notch-1, were measured by western blot. Three repeated experiments with one representative blot. (B) Inhibition of p38 in control B16 cells (B16-shCtrl) enhanced pigmentations. SB202190, a p38 inhibitor, at 10 μM, was incubated with B16 cells for 24 h. Melanin concentration was then measured (n = 3 and 3, respectively, for B16-shCtrl cells and B16-SRAi cells; error bars represent standard errors; * indicates p
    Figure Legend Snippet: (A) Constitutive activation of p38 was obliterated in SRA-deficient B16 cells. The expression of total and phosphorylated p38 as well as cleaved Notch-1, were measured by western blot. Three repeated experiments with one representative blot. (B) Inhibition of p38 in control B16 cells (B16-shCtrl) enhanced pigmentations. SB202190, a p38 inhibitor, at 10 μM, was incubated with B16 cells for 24 h. Melanin concentration was then measured (n = 3 and 3, respectively, for B16-shCtrl cells and B16-SRAi cells; error bars represent standard errors; * indicates p

    Techniques Used: Activation Assay, Expressing, Western Blot, Inhibition, Incubation, Concentration Assay

    11) Product Images from "Peptidoglycan Up-Regulates CXCL8 Expression via Multiple Pathways in Monocytes/Macrophages"

    Article Title: Peptidoglycan Up-Regulates CXCL8 Expression via Multiple Pathways in Monocytes/Macrophages

    Journal: Biomolecules & Therapeutics

    doi: 10.4062/biomolther.2015.053

    The effects of MAPK inhibitors on PG-induced CXCL8 expression. (A) THP-1 cells were treated with medium alone (control) or pre-incubated for 2 hr in the absence or presence of U0126, SB202190 or SP600125 (10 μM each) and stimulated for 6 hr with PG (1 μg/ml). Transcript of il8 gene was quantified by realtime PCR. Data are expressed as mean±SD (n=3 replicates for each group). *** p
    Figure Legend Snippet: The effects of MAPK inhibitors on PG-induced CXCL8 expression. (A) THP-1 cells were treated with medium alone (control) or pre-incubated for 2 hr in the absence or presence of U0126, SB202190 or SP600125 (10 μM each) and stimulated for 6 hr with PG (1 μg/ml). Transcript of il8 gene was quantified by realtime PCR. Data are expressed as mean±SD (n=3 replicates for each group). *** p

    Techniques Used: Expressing, Incubation, Polymerase Chain Reaction

    12) Product Images from "Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases"

    Article Title: Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2016.417

    Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.

    Techniques Used: Staining

    Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.

    Techniques Used: Inhibition, Mouse Assay, Injection

    13) Product Images from "Cytosolic phospholipase A2 plays a crucial role in ROS/NO signaling during microglial activation through the lipoxygenase pathway"

    Article Title: Cytosolic phospholipase A2 plays a crucial role in ROS/NO signaling during microglial activation through the lipoxygenase pathway

    Journal: Journal of Neuroinflammation

    doi: 10.1186/s12974-015-0419-0

    ERK1/2 contributed to cPLA 2 phosphorylation after LPS/IFNγ stimulation. BV-2 cells were starved for 3 h in serum-free DMEM. One hour prior to stimulation, cells were pretreated with indicated concentrations of MAPK inhibitors: U0126 (U) for ERK1/2 inhibition, SB202190 (SB) for p38 MAPK inhibition, and SP600125 (SP) for JNK inhibition. Cells were then stimulated with a , c 200 ng/mL LPS or b , d 20 ng/mL IFNγ. Cells were lysed and proteins were collected and processed 2 h after LPS stimulation or 8 h after IFNγ stimulation for Western blot analyses. a , b Representative blots. Protein expression was quantified with QuantityOne software for three separate experiments for c LPS-stimulated BV-2 cells and d IFNγ-stimulated BV-2 cells. Results were expressed as the mean ± SEM ( n = 3) and significant difference from the respective group was determined by one-way ANOVA followed by Dunnett’s post-tests, * P
    Figure Legend Snippet: ERK1/2 contributed to cPLA 2 phosphorylation after LPS/IFNγ stimulation. BV-2 cells were starved for 3 h in serum-free DMEM. One hour prior to stimulation, cells were pretreated with indicated concentrations of MAPK inhibitors: U0126 (U) for ERK1/2 inhibition, SB202190 (SB) for p38 MAPK inhibition, and SP600125 (SP) for JNK inhibition. Cells were then stimulated with a , c 200 ng/mL LPS or b , d 20 ng/mL IFNγ. Cells were lysed and proteins were collected and processed 2 h after LPS stimulation or 8 h after IFNγ stimulation for Western blot analyses. a , b Representative blots. Protein expression was quantified with QuantityOne software for three separate experiments for c LPS-stimulated BV-2 cells and d IFNγ-stimulated BV-2 cells. Results were expressed as the mean ± SEM ( n = 3) and significant difference from the respective group was determined by one-way ANOVA followed by Dunnett’s post-tests, * P

    Techniques Used: Inhibition, Western Blot, Expressing, Software

    14) Product Images from "Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases"

    Article Title: Senescent peritoneal mesothelium creates a niche for ovarian cancer metastases

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2016.417

    Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Role of p38 MAPK as a mediator of HPMC senescence replication ( a ), the level of γ -H2A.X foci ( b ) and SA- β -Gal ( c - d ), and the secretion of proteins ( e ) were compared in HPMCs undergoing senescence in standard culture conditions (control cells) and in cells exposed to the p38 MAPK inhibitor – SB202190. The frame located in panel ( a ) indicates a time point at which HPMCs propagated in standard conditions reached senescence. The results shown in panels ( b , c , d , and e ) refer to this moment. Panel ( d ) shows representative results of staining against SA- β -Gal (positive cells are green; × 100; bar, 100 μ m). The asterisks indicate significant differences as compared with senescent HPMCs. The experiments were performed by using HPMCs obtained from 12 different donors. The results are expressed as mean±S.D.

    Techniques Used: Staining

    Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.
    Figure Legend Snippet: Effect of HPMC rejuvenation by p38 MAPK inhibition on the intraperitoneal development of ovarian tumors in mice. Representative pictures showing bioluminescence intensity of A2780 cells co-injected i.p. with senescent HPMCs or with middle-aged HPMCs treated with SB202190 ( a ). The dynamics of xenograft development, estimated according to the difference between the highest bioluminescence intensity recorded throughout the experiment and the initial value, were recorded 2 days after cell implantation ( b ). Comparison of masses of tumors excised from a mouse peritoneum at the end of the experiment ( c ). The asterisks indicate a significant difference as compared with xenografts established in the presence of senescent HPMCs. Experiments were performed on five animals per group with HPMCs established from five different donors. The results are expressed as mean±S.D.

    Techniques Used: Inhibition, Mouse Assay, Injection

    15) Product Images from "Endothelium-Derived 5-Methoxytryptophan Protects Endothelial Barrier Function by Blocking p38 MAPK Activation"

    Article Title: Endothelium-Derived 5-Methoxytryptophan Protects Endothelial Barrier Function by Blocking p38 MAPK Activation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0152166

    SB202190 protects HUVEC barrier function. (A) Pretreatment with SB202190 (10 μmol/L), a p38 inhibitor, attenuated VEGF- or pro-inflammatory cytokines-induced HUVECs permeability. Error bars denote mean ± SD (n = 3). * indicates P
    Figure Legend Snippet: SB202190 protects HUVEC barrier function. (A) Pretreatment with SB202190 (10 μmol/L), a p38 inhibitor, attenuated VEGF- or pro-inflammatory cytokines-induced HUVECs permeability. Error bars denote mean ± SD (n = 3). * indicates P

    Techniques Used: Permeability

    16) Product Images from "TGFβ-induced Lung Cancer Cell Migration is NR4A1-dependent"

    Article Title: TGFβ-induced Lung Cancer Cell Migration is NR4A1-dependent

    Journal: Molecular cancer research : MCR

    doi: 10.1158/1541-7786.MCR-18-0366

    Effects of kinase inhibitors on TGFβ-induced migration and nuclear export of NR4A1. (A) Cells were treated with TGFβ alone or in combination with kinase inhibitors SP600125 (30 μM), SB202190 (30 μM), LY294002 (30 μM) and PD98059 (30 μM), and effects on cell migration were determined. A549 (B), (H460 (C) and H1299 (D) cells were treated with TGFβ alone and in combination with kinase inhibitors, and nuclear and cytosolic extracts were analyzed for NR4A1 expression by western blots. (E) Lung cancer cells were treated with TGFβ and SP600125 alone or in combination, and whole cell lysates were analyzed by western blots. Significant (p
    Figure Legend Snippet: Effects of kinase inhibitors on TGFβ-induced migration and nuclear export of NR4A1. (A) Cells were treated with TGFβ alone or in combination with kinase inhibitors SP600125 (30 μM), SB202190 (30 μM), LY294002 (30 μM) and PD98059 (30 μM), and effects on cell migration were determined. A549 (B), (H460 (C) and H1299 (D) cells were treated with TGFβ alone and in combination with kinase inhibitors, and nuclear and cytosolic extracts were analyzed for NR4A1 expression by western blots. (E) Lung cancer cells were treated with TGFβ and SP600125 alone or in combination, and whole cell lysates were analyzed by western blots. Significant (p

    Techniques Used: Migration, Expressing, Western Blot

    17) Product Images from "Procyanidins from Wild Grape (Vitis amurensis) Seeds Regulate ARE-Mediated Enzyme Expression via Nrf2 Coupled with p38 and PI3K/Akt Pathway in HepG2 Cells"

    Article Title: Procyanidins from Wild Grape (Vitis amurensis) Seeds Regulate ARE-Mediated Enzyme Expression via Nrf2 Coupled with p38 and PI3K/Akt Pathway in HepG2 Cells

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms13010801

    Effects of wild grape seed fractions on the phosphorylations of upstream targets in HepG2 cells. ( A ) Effect of wild grape seeds fractions on phosphorylation of MAPKs. Cells were treated with 25 μg/mL concentrations of wild grape seeds fractions (F1–F6) for 1 h; ( B ) Effect of wild grape seeds fractions on the phosphorylation of Akt. HepG2 cells were treated with vehicle (DMSO, 0.1%) or fractions and then equal amount of proteins from whole cell lysates were analyzed by Western blotting; ( C ) Influence of MAPK inhibitors on procyanidin-induced Nrf2 expression. HepG2 cells were incubated with 50 μM U0126 (MEK1/2 inhibitor), SB202190 (p38 inhibitor), SP600125 (JNK inhibitor) and LY294002 (PI3K inhibitor) for 1 h prior to 25 μg/mL procyanidin fraction treatment for 1 h. The blots shown are representative of three independent experiments with similar results. Values are means ± SD; n = 3, * p
    Figure Legend Snippet: Effects of wild grape seed fractions on the phosphorylations of upstream targets in HepG2 cells. ( A ) Effect of wild grape seeds fractions on phosphorylation of MAPKs. Cells were treated with 25 μg/mL concentrations of wild grape seeds fractions (F1–F6) for 1 h; ( B ) Effect of wild grape seeds fractions on the phosphorylation of Akt. HepG2 cells were treated with vehicle (DMSO, 0.1%) or fractions and then equal amount of proteins from whole cell lysates were analyzed by Western blotting; ( C ) Influence of MAPK inhibitors on procyanidin-induced Nrf2 expression. HepG2 cells were incubated with 50 μM U0126 (MEK1/2 inhibitor), SB202190 (p38 inhibitor), SP600125 (JNK inhibitor) and LY294002 (PI3K inhibitor) for 1 h prior to 25 μg/mL procyanidin fraction treatment for 1 h. The blots shown are representative of three independent experiments with similar results. Values are means ± SD; n = 3, * p

    Techniques Used: Western Blot, Expressing, Incubation

    18) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    19) Product Images from "TKI-addicted ROS1-rearranged cells are destined to survival or death by the intensity of ROS1 kinase activity"

    Article Title: TKI-addicted ROS1-rearranged cells are destined to survival or death by the intensity of ROS1 kinase activity

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-05736-9

    The rescue effect of p38 inhibitor (SB202190) on F2075C-mutated cells obtained by ENU mutagenesis screening or reconstructed F2075C-mutated cells. ( A , B ) Effect of SB202190 on wild-type CD74-ROS1, ENU-screened F2075C-mutated cells ( A ), or reconstructed F2075C cells with or without 1 μg/mL DOX ( B ). Each cell line was treated with the indicated dose ranges of inhibitors for 72 h, then cell viability was measured by the CellTiter-Glo assay. Each value is shown as relative cell growth by normalizing with the values of untreated wells. ( C , D ) Immunoblotting of SB202190-treated wild-type CD74-ROS1 cells or F2075C-mutated cell ( C ), or SB202190- or cabozantinib-treated reconstructed F2075C-mutated cells with or without 1 μg/mL DOX (the cells shown DOX (+) were pretreated with DOX for 24 h.) ( D ). Cell lysates were immunoblotted to detect the indicated proteins. Uncropped blots are presented in Supplementary Fig. S11 .
    Figure Legend Snippet: The rescue effect of p38 inhibitor (SB202190) on F2075C-mutated cells obtained by ENU mutagenesis screening or reconstructed F2075C-mutated cells. ( A , B ) Effect of SB202190 on wild-type CD74-ROS1, ENU-screened F2075C-mutated cells ( A ), or reconstructed F2075C cells with or without 1 μg/mL DOX ( B ). Each cell line was treated with the indicated dose ranges of inhibitors for 72 h, then cell viability was measured by the CellTiter-Glo assay. Each value is shown as relative cell growth by normalizing with the values of untreated wells. ( C , D ) Immunoblotting of SB202190-treated wild-type CD74-ROS1 cells or F2075C-mutated cell ( C ), or SB202190- or cabozantinib-treated reconstructed F2075C-mutated cells with or without 1 μg/mL DOX (the cells shown DOX (+) were pretreated with DOX for 24 h.) ( D ). Cell lysates were immunoblotted to detect the indicated proteins. Uncropped blots are presented in Supplementary Fig. S11 .

    Techniques Used: Mutagenesis, Glo Assay

    20) Product Images from "Activation of c-Jun N-Terminal Kinase (JNK) by widely used specific p38 MAPK inhibitor SB202190 and SB203580: A MLK-3-MKK7-dependent mechanism"

    Article Title: Activation of c-Jun N-Terminal Kinase (JNK) by widely used specific p38 MAPK inhibitor SB202190 and SB203580: A MLK-3-MKK7-dependent mechanism

    Journal: Cellular signalling

    doi: 10.1016/j.cellsig.2007.12.003

    Specific p38 MAPK inhibitor SB202190 induces AP-1 DNA binding
    Figure Legend Snippet: Specific p38 MAPK inhibitor SB202190 induces AP-1 DNA binding

    Techniques Used: Binding Assay

    MLK-3 downregulation by RNA interference decreases the phosphorylation of cJun, ATF-2 and AP-1 DNA binding activated by SB202190 or SB203580
    Figure Legend Snippet: MLK-3 downregulation by RNA interference decreases the phosphorylation of cJun, ATF-2 and AP-1 DNA binding activated by SB202190 or SB203580

    Techniques Used: Binding Assay

    MLK-3-, but not MEKK1-mediated phosphorylation of JNK by SB202190 or SB203580
    Figure Legend Snippet: MLK-3-, but not MEKK1-mediated phosphorylation of JNK by SB202190 or SB203580

    Techniques Used:

    MLK3 is phosphorylated on ser277/281 in response to SB202190 or SB203580 treatment
    Figure Legend Snippet: MLK3 is phosphorylated on ser277/281 in response to SB202190 or SB203580 treatment

    Techniques Used:

    Time course of JNK phosphorylation due to treatment of A549 cells with p38 MAPK inhibitors SB202190 or SB203580
    Figure Legend Snippet: Time course of JNK phosphorylation due to treatment of A549 cells with p38 MAPK inhibitors SB202190 or SB203580

    Techniques Used:

    (A) SB202190 induces phosphorylation of JNK in human microvascular endothelial cells (HMVEC) HMVEC cells were treated with DMSO control or with 10 µM of SB202190 for 0.5, 1, 1.5, 2, 3, 4, or 6 hours, followed by detection of pJNK or JNK as described
    Figure Legend Snippet: (A) SB202190 induces phosphorylation of JNK in human microvascular endothelial cells (HMVEC) HMVEC cells were treated with DMSO control or with 10 µM of SB202190 for 0.5, 1, 1.5, 2, 3, 4, or 6 hours, followed by detection of pJNK or JNK as described

    Techniques Used:

    A. ATF-2 is phosphorylated by the p38 MAPK-specific inhibitor SB202190 A549 cells were treated with indicated concentrations of SB202190 or SP600125 for 16 hours. Anisomycin (1 µg/mL) was used as a positive control for ATF-2 phosphorylation. Cells
    Figure Legend Snippet: A. ATF-2 is phosphorylated by the p38 MAPK-specific inhibitor SB202190 A549 cells were treated with indicated concentrations of SB202190 or SP600125 for 16 hours. Anisomycin (1 µg/mL) was used as a positive control for ATF-2 phosphorylation. Cells

    Techniques Used: Positive Control

    (A) p38 MAPK down-regulation by RNA interference does not decrease JNK phosphorylation induced by SB202190 or SB203580 section. After 48 hours,
    Figure Legend Snippet: (A) p38 MAPK down-regulation by RNA interference does not decrease JNK phosphorylation induced by SB202190 or SB203580 section. After 48 hours,

    Techniques Used:

    Phosphorylation of JNK by specific p38 MAPK inhibitors SB202190 and SB203580: Dose-Response
    Figure Legend Snippet: Phosphorylation of JNK by specific p38 MAPK inhibitors SB202190 and SB203580: Dose-Response

    Techniques Used:

    Activation of MLK3 in response to SB202190 or SB203580
    Figure Legend Snippet: Activation of MLK3 in response to SB202190 or SB203580

    Techniques Used: Activation Assay

    21) Product Images from "Follistatin-Like 1 Promotes Bleomycin-Induced Pulmonary Fibrosis through the Transforming Growth Factor Beta 1/Mitogen-Activated Protein Kinase Signaling Pathway"

    Article Title: Follistatin-Like 1 Promotes Bleomycin-Induced Pulmonary Fibrosis through the Transforming Growth Factor Beta 1/Mitogen-Activated Protein Kinase Signaling Pathway

    Journal: Chinese Medical Journal

    doi: 10.4103/0366-6999.238151

    FSTL1 modulates myofibroblast differentiation by facilitating p38/JNK signaling. (a and b) Primary lung fibroblasts from Fstl1+/− and their WT littermates were treated with 5 ng/ml TGF-β1. (a) Immunofluorescence staining of α-SMA in lung fibroblasts. (b) Protein expression levels of α-SMA and type I collagen. (c-e) MLgs were pretreated with U0126, SB202190, and SP600125. Protein expression levels of α-SMA and type I collagen were detected by Western blotting. n = 4; Bars = 100 μm. * P
    Figure Legend Snippet: FSTL1 modulates myofibroblast differentiation by facilitating p38/JNK signaling. (a and b) Primary lung fibroblasts from Fstl1+/− and their WT littermates were treated with 5 ng/ml TGF-β1. (a) Immunofluorescence staining of α-SMA in lung fibroblasts. (b) Protein expression levels of α-SMA and type I collagen. (c-e) MLgs were pretreated with U0126, SB202190, and SP600125. Protein expression levels of α-SMA and type I collagen were detected by Western blotting. n = 4; Bars = 100 μm. * P

    Techniques Used: Immunofluorescence, Staining, Expressing, Western Blot

    22) Product Images from "Transforming Growth Factor β/NR4A1-Inducible Breast Cancer Cell Migration and Epithelial-to-Mesenchymal Transition Is p38α (Mitogen-Activated Protein Kinase 14) Dependent"

    Article Title: Transforming Growth Factor β/NR4A1-Inducible Breast Cancer Cell Migration and Epithelial-to-Mesenchymal Transition Is p38α (Mitogen-Activated Protein Kinase 14) Dependent

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.00306-17

    Correlation between nuclear export of NR4A1 and TGF-β-induced cell migration. (A to C) MDA-MB-231 cells were treated with DMSO or 5 ng/ml TGF-β and transfected with p38(CA), p38(KD), or p38(DN) (A) or the same p38 constructs with or without TGF-β (B) or transfected with p38(CA) with or without TGF-β, LMB, and CDIM8/CDIM14 (C), and nuclear and cyctosolic extracts were obtained and analyzed by Western blotting. (D and E) MDA-MB-231 cells were transfected with p38(CA), p38(DN), or p38(KC) alone and in combination with TGF-β (5 and 12 h of treatment) (D) or transfected with p38(CA) with or without TGF-β, LMB, CDIM8/CDIM14, or SB202190 (E), and cell migration was determined as outlined in Materials and Methods. The error bars indicate SE.
    Figure Legend Snippet: Correlation between nuclear export of NR4A1 and TGF-β-induced cell migration. (A to C) MDA-MB-231 cells were treated with DMSO or 5 ng/ml TGF-β and transfected with p38(CA), p38(KD), or p38(DN) (A) or the same p38 constructs with or without TGF-β (B) or transfected with p38(CA) with or without TGF-β, LMB, and CDIM8/CDIM14 (C), and nuclear and cyctosolic extracts were obtained and analyzed by Western blotting. (D and E) MDA-MB-231 cells were transfected with p38(CA), p38(DN), or p38(KC) alone and in combination with TGF-β (5 and 12 h of treatment) (D) or transfected with p38(CA) with or without TGF-β, LMB, CDIM8/CDIM14, or SB202190 (E), and cell migration was determined as outlined in Materials and Methods. The error bars indicate SE.

    Techniques Used: Migration, Multiple Displacement Amplification, Transfection, Construct, Western Blot

    23) Product Images from "Inhibition of cancer cell epithelial mesenchymal transition by normal fibroblasts via production of 5-methoxytryptophan"

    Article Title: Inhibition of cancer cell epithelial mesenchymal transition by normal fibroblasts via production of 5-methoxytryptophan

    Journal: Oncotarget

    doi: 10.18632/oncotarget.9111

    Inactivation of TGF-β1-induced p38 MAPK by 5-MTP ( A ) and ( B ) A549 cells were pretreated with 5-MTP at increasing concentrations ( A ) or 10 μM ( B ) or SB202190 (10 μM) for 30 min followed by TGF-β1 for 15 min. Cells were lysed and p-p38 MAPK (p-p38) and total p38 MAPK (p38) were analyzed by Western blotting. Upper panels show representative blots and lower panels the densitometry of p-p38 blots. Error bars denote mean ± SEM ( n = 3). * indicates P
    Figure Legend Snippet: Inactivation of TGF-β1-induced p38 MAPK by 5-MTP ( A ) and ( B ) A549 cells were pretreated with 5-MTP at increasing concentrations ( A ) or 10 μM ( B ) or SB202190 (10 μM) for 30 min followed by TGF-β1 for 15 min. Cells were lysed and p-p38 MAPK (p-p38) and total p38 MAPK (p38) were analyzed by Western blotting. Upper panels show representative blots and lower panels the densitometry of p-p38 blots. Error bars denote mean ± SEM ( n = 3). * indicates P

    Techniques Used: Western Blot

    24) Product Images from "SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43"

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43

    Journal: International Journal of Oncology

    doi: 10.3892/ijo.2017.4171

    SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P
    Figure Legend Snippet: SRC3 expressed in BMSCs promoted tumor growth of multiple myeloma cells by regulating the expression of Cx43. The BMSCs were treated with sh-SRC3 to knockdown the expression of SRC3 and RPMI-8226 cells were either overexpressed with Cx43 or treated with MAPK inhibitor SB202190. The cells were co-injected into nude mice to establish murine multiple myeloma models. Each nude mouse was injected with 100 µ l of cell suspension containing 3×10 6 RPMI-8226 cells and 3×10 5 MSC subcutaneously into the right flank for the following groups. MM+MSC, MM+sh-SRC3-MSC+pcDNA3.1, MM+sh-SRC3-MSC+Cx43, MM+sh-SRC3-MSC+inhibitor. (A) Representative images of tumors from each group. (B) Growth curve of tumors was calculated for each group. (C) Representative images of hematoxylin and eosin staining (x10) of tumors. (D) The proportion of TUNEL positive cells. (E) Representative images of TUNEL staining in tumors. Scale bars, 100 µ m. Data represent mean ± SEM. * P

    Techniques Used: Expressing, Injection, Mouse Assay, Staining, TUNEL Assay

    MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P
    Figure Legend Snippet: MAPK pathway is involved in promoting the proliferation and migration of RPMI-8226 cells regulated by Cx43. The RPMI-8226 cells were transfected with either pcDNA3.1 or pcDNA3.1-Cx43 for 48 h. These cells were treated with 5 µ M MAPK inhibitor SB202190 for 24 h, and then co-cultured with either BMSCs or sh-SRC3-MSC. (A) Western blots analyzed the protein level of Cx43, phosphorylated ERK (pERK), p38 (p-p38) and JNK (p-JNK) in RPMI-8226 cells. (B) Densitometry plot of results from (A). The relative expression levels were normalized to GAPDH. (C) Cell proliferation analysis of RPMI-8226 cells after being co-cultured for 48 h using the CCK-8 assay. (D) Hoechst foci staining for co-cultured RPMI-8226 cells. (E) The cells that stained positive for Hoechst staining were counted. (F and G) Scratch-wound healing assay was used to assess the migration potential of RPMI-8226 cells after being co-cultured for 48 h. The wound closure rate was calculated at 24 h using a phase contrast microscope. (H) Transwell migration assay assessed the change of migration potential of RPMI-8226 cells after being co-cultured for 48 h. Representative images of migrated cells are shown. (I) Relative numbers of migrated cells in the Transwell assay under a phase contrast microscope. Data represent three independent experiments (average and SEM of triplicate samples). * P

    Techniques Used: Migration, Transfection, Cell Culture, Western Blot, Expressing, CCK-8 Assay, Staining, Wound Healing Assay, Microscopy, Transwell Migration Assay, Transwell Assay

    Related Articles

    Cell Counting:

    Article Title: Telocinobufagin and Marinobufagin Produce Different Effects in LLC-PK1 Cells: A Case of Functional Selectivity of Bufadienolides
    Article Snippet: .. Cell Counting Assay In 24-well plates, 1–2 × 104 LLC-PK1 cells/well were treated with 1, 10 or 100 nM CTS for 24, 48, and 72 h. In order to investigate the involvement of intracellular signaling pathways, 100 nM CTS were incubated with or without inhibitors of Src (SU6656, 10 μM; Sigma-Aldrich, St. Louis, MO, USA), ERK1/2-MEK1/2 (U0126, 10 μM; Cell Signaling Technology, Danvers, MA, USA), PI3K (LY294002, 5 μM; Cell Signaling Technology, Danvers, MA, USA), p38 (SB202190, 10 μM; Cell Signaling Technology, Danvers, MA, USA), JNK1/2 (SP600125, 1.5 μM; Cell Signaling Technology, Danvers, MA, USA), or GSK-3β (BIO, 0.5, 1, and 5 μM; Sigma-Aldrich, St. Louis, MO, USA) for 72 h. For MβCD (Sigma-Aldrich, St. Louis, MO, USA) assay, cells were pretreated with 10 mM MβCD for 30 min and then 1 mM MβCD + 100 nM TCB in 2.5% FBS for 72 h. At these time points, two wells from each group were trypsinized and the number of Trypan blue-viable cells was counted in Neubauer chamber (hemocytometer). .. MTT Assay In 96-well plates, 3 × 103 LLC-PK1 cells/well were treated with 100 nM CTS with or without inhibitors of Src (SU6656, 10 μM), ERK1/2-MEK1/2 (U0126, 10 μM), PI3K (LY294002 5 μM), p38 (SB202190, 10 μM), JNK1/2 (SP600125, 1.5 μM), or GSK-3β (BIO, 0.5, 1 and 5 μM) for 72 h. MTT was added directly to culture wells and incubated for 4 h. The absorbance was measured at 570 nm with a 96-well plate reader.

    Incubation:

    Article Title: Telocinobufagin and Marinobufagin Produce Different Effects in LLC-PK1 Cells: A Case of Functional Selectivity of Bufadienolides
    Article Snippet: .. Cell Counting Assay In 24-well plates, 1–2 × 104 LLC-PK1 cells/well were treated with 1, 10 or 100 nM CTS for 24, 48, and 72 h. In order to investigate the involvement of intracellular signaling pathways, 100 nM CTS were incubated with or without inhibitors of Src (SU6656, 10 μM; Sigma-Aldrich, St. Louis, MO, USA), ERK1/2-MEK1/2 (U0126, 10 μM; Cell Signaling Technology, Danvers, MA, USA), PI3K (LY294002, 5 μM; Cell Signaling Technology, Danvers, MA, USA), p38 (SB202190, 10 μM; Cell Signaling Technology, Danvers, MA, USA), JNK1/2 (SP600125, 1.5 μM; Cell Signaling Technology, Danvers, MA, USA), or GSK-3β (BIO, 0.5, 1, and 5 μM; Sigma-Aldrich, St. Louis, MO, USA) for 72 h. For MβCD (Sigma-Aldrich, St. Louis, MO, USA) assay, cells were pretreated with 10 mM MβCD for 30 min and then 1 mM MβCD + 100 nM TCB in 2.5% FBS for 72 h. At these time points, two wells from each group were trypsinized and the number of Trypan blue-viable cells was counted in Neubauer chamber (hemocytometer). .. MTT Assay In 96-well plates, 3 × 103 LLC-PK1 cells/well were treated with 100 nM CTS with or without inhibitors of Src (SU6656, 10 μM), ERK1/2-MEK1/2 (U0126, 10 μM), PI3K (LY294002 5 μM), p38 (SB202190, 10 μM), JNK1/2 (SP600125, 1.5 μM), or GSK-3β (BIO, 0.5, 1 and 5 μM) for 72 h. MTT was added directly to culture wells and incubated for 4 h. The absorbance was measured at 570 nm with a 96-well plate reader.

    Article Title: Protein phosphatase 2A regulates the p38 signaling pathway to affect the migration of astrocytes
    Article Snippet: .. Cells in the SB202190 group were incubated at 37°C for 48 h with cell culture medium containing the p38 signal pathway inhibitor SB202190 (Cell Signaling Technology, Inc.) at a final concentration of 30 µmol/l. .. Cells in the DES + SB202190 group were treated with p38 signal pathway inhibitor SB202190 at a final concentration of 30 µmol/l and 15 nM PP2A activator DES at 37°C for 48 h, while the untreated group received no treatment.

    other:

    Article Title: 4-Hydroxy-2-nonenal induces apoptosis by activating ERK1/2 signaling and depleting intracellular glutathione in intestinal epithelial cells
    Article Snippet: Kinases inhibitors, including ERK1/2 inhibitor U0126, JNK inhibitor SP600125, p38 MAPK inhibitor SB202190, and protein degradation inhibitor MG132 were obtained from Cell Signaling Technology (Beverly, MA).

    Article Title: SRC3 expressed in BMSCs promotes growth and migration of multiple myeloma cells by regulating the expression of Cx43
    Article Snippet: Intratumoral leukocyte populations increased after overexpressing Cx43 and treating with SB202190 in RPMI-8226 cells ( ).

    Cell Culture:

    Article Title: Protein phosphatase 2A regulates the p38 signaling pathway to affect the migration of astrocytes
    Article Snippet: .. Cells in the SB202190 group were incubated at 37°C for 48 h with cell culture medium containing the p38 signal pathway inhibitor SB202190 (Cell Signaling Technology, Inc.) at a final concentration of 30 µmol/l. .. Cells in the DES + SB202190 group were treated with p38 signal pathway inhibitor SB202190 at a final concentration of 30 µmol/l and 15 nM PP2A activator DES at 37°C for 48 h, while the untreated group received no treatment.

    Concentration Assay:

    Article Title: Protein phosphatase 2A regulates the p38 signaling pathway to affect the migration of astrocytes
    Article Snippet: .. Cells in the SB202190 group were incubated at 37°C for 48 h with cell culture medium containing the p38 signal pathway inhibitor SB202190 (Cell Signaling Technology, Inc.) at a final concentration of 30 µmol/l. .. Cells in the DES + SB202190 group were treated with p38 signal pathway inhibitor SB202190 at a final concentration of 30 µmol/l and 15 nM PP2A activator DES at 37°C for 48 h, while the untreated group received no treatment.

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    Effect of <t>p38,</t> JNK1/2 and PI3K inhibition on cell proliferation of LLC-PK1 cells treated with telocinobufagin (TCB). Serum-starved LLC-PK1 cells were treated with 100 nM TCB in 2.5% FBS for 72 h with or without 10 μM SB202180 (p38 inhibitor) ( a ), 1.5 μM SB600125 (JNK1/2 inhibitor) ( b ), or 5 μM LY294002 (PI3K inhibitor) ( c ). Trypan blue-free viable cells were counted in Neubauer chamber. Data are the mean ± SEM of at least three independent experiments in duplicate. *** p
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    Effect of p38, JNK1/2 and PI3K inhibition on cell proliferation of LLC-PK1 cells treated with telocinobufagin (TCB). Serum-starved LLC-PK1 cells were treated with 100 nM TCB in 2.5% FBS for 72 h with or without 10 μM SB202180 (p38 inhibitor) ( a ), 1.5 μM SB600125 (JNK1/2 inhibitor) ( b ), or 5 μM LY294002 (PI3K inhibitor) ( c ). Trypan blue-free viable cells were counted in Neubauer chamber. Data are the mean ± SEM of at least three independent experiments in duplicate. *** p

    Journal: International Journal of Molecular Sciences

    Article Title: Telocinobufagin and Marinobufagin Produce Different Effects in LLC-PK1 Cells: A Case of Functional Selectivity of Bufadienolides

    doi: 10.3390/ijms19092769

    Figure Lengend Snippet: Effect of p38, JNK1/2 and PI3K inhibition on cell proliferation of LLC-PK1 cells treated with telocinobufagin (TCB). Serum-starved LLC-PK1 cells were treated with 100 nM TCB in 2.5% FBS for 72 h with or without 10 μM SB202180 (p38 inhibitor) ( a ), 1.5 μM SB600125 (JNK1/2 inhibitor) ( b ), or 5 μM LY294002 (PI3K inhibitor) ( c ). Trypan blue-free viable cells were counted in Neubauer chamber. Data are the mean ± SEM of at least three independent experiments in duplicate. *** p

    Article Snippet: Cell Counting Assay In 24-well plates, 1–2 × 104 LLC-PK1 cells/well were treated with 1, 10 or 100 nM CTS for 24, 48, and 72 h. In order to investigate the involvement of intracellular signaling pathways, 100 nM CTS were incubated with or without inhibitors of Src (SU6656, 10 μM; Sigma-Aldrich, St. Louis, MO, USA), ERK1/2-MEK1/2 (U0126, 10 μM; Cell Signaling Technology, Danvers, MA, USA), PI3K (LY294002, 5 μM; Cell Signaling Technology, Danvers, MA, USA), p38 (SB202190, 10 μM; Cell Signaling Technology, Danvers, MA, USA), JNK1/2 (SP600125, 1.5 μM; Cell Signaling Technology, Danvers, MA, USA), or GSK-3β (BIO, 0.5, 1, and 5 μM; Sigma-Aldrich, St. Louis, MO, USA) for 72 h. For MβCD (Sigma-Aldrich, St. Louis, MO, USA) assay, cells were pretreated with 10 mM MβCD for 30 min and then 1 mM MβCD + 100 nM TCB in 2.5% FBS for 72 h. At these time points, two wells from each group were trypsinized and the number of Trypan blue-viable cells was counted in Neubauer chamber (hemocytometer).

    Techniques: Inhibition

    Effect of inhibition of the p38 signaling pathway on cell migration and the protein expression of MMPs in astrocytes of the untreated, SB202190 and (DES) + SB202190 groups. (A) Cell migration was determined by a Transwell migration assay. (B) Representative western blot bands for the protein expression of MMP-2 and MMP-9 in the untreated, SB202190 and DES + SB202190 groups. (C) Densitometric analysis was performed to obtain the relative expression level of target proteins with β-actin as the internal reference. SB202190 was employed as an inhibitor of the p38 signaling pathway, while DES was employed as an activator of protein phosphatase 2A. **P

    Journal: Molecular Medicine Reports

    Article Title: Protein phosphatase 2A regulates the p38 signaling pathway to affect the migration of astrocytes

    doi: 10.3892/mmr.2018.9425

    Figure Lengend Snippet: Effect of inhibition of the p38 signaling pathway on cell migration and the protein expression of MMPs in astrocytes of the untreated, SB202190 and (DES) + SB202190 groups. (A) Cell migration was determined by a Transwell migration assay. (B) Representative western blot bands for the protein expression of MMP-2 and MMP-9 in the untreated, SB202190 and DES + SB202190 groups. (C) Densitometric analysis was performed to obtain the relative expression level of target proteins with β-actin as the internal reference. SB202190 was employed as an inhibitor of the p38 signaling pathway, while DES was employed as an activator of protein phosphatase 2A. **P

    Article Snippet: Cells in the SB202190 group were incubated at 37°C for 48 h with cell culture medium containing the p38 signal pathway inhibitor SB202190 (Cell Signaling Technology, Inc.) at a final concentration of 30 µmol/l.

    Techniques: Inhibition, Migration, Expressing, Transwell Migration Assay, Western Blot

    Effect of a p38 signaling pathway inhibitor on p-p38 protein expression i n astrocytes. (A) Representative western blot bands for the protein expression of p-p38 and p38 in untreated astrocytes and astrocytes treated with the p38 signaling pathway inhibitor, SB202190. (B) Densitometric analysis was performed to obtain the relative expression level of p-p38 protein with p38 as the internal reference. **P

    Journal: Molecular Medicine Reports

    Article Title: Protein phosphatase 2A regulates the p38 signaling pathway to affect the migration of astrocytes

    doi: 10.3892/mmr.2018.9425

    Figure Lengend Snippet: Effect of a p38 signaling pathway inhibitor on p-p38 protein expression i n astrocytes. (A) Representative western blot bands for the protein expression of p-p38 and p38 in untreated astrocytes and astrocytes treated with the p38 signaling pathway inhibitor, SB202190. (B) Densitometric analysis was performed to obtain the relative expression level of p-p38 protein with p38 as the internal reference. **P

    Article Snippet: Cells in the SB202190 group were incubated at 37°C for 48 h with cell culture medium containing the p38 signal pathway inhibitor SB202190 (Cell Signaling Technology, Inc.) at a final concentration of 30 µmol/l.

    Techniques: Expressing, Western Blot

    ERK1/2 contributed to cPLA 2 phosphorylation after LPS/IFNγ stimulation. BV-2 cells were starved for 3 h in serum-free DMEM. One hour prior to stimulation, cells were pretreated with indicated concentrations of MAPK inhibitors: U0126 (U) for ERK1/2 inhibition, SB202190 (SB) for p38 MAPK inhibition, and SP600125 (SP) for JNK inhibition. Cells were then stimulated with a , c 200 ng/mL LPS or b , d 20 ng/mL IFNγ. Cells were lysed and proteins were collected and processed 2 h after LPS stimulation or 8 h after IFNγ stimulation for Western blot analyses. a , b Representative blots. Protein expression was quantified with QuantityOne software for three separate experiments for c LPS-stimulated BV-2 cells and d IFNγ-stimulated BV-2 cells. Results were expressed as the mean ± SEM ( n = 3) and significant difference from the respective group was determined by one-way ANOVA followed by Dunnett’s post-tests, * P

    Journal: Journal of Neuroinflammation

    Article Title: Cytosolic phospholipase A2 plays a crucial role in ROS/NO signaling during microglial activation through the lipoxygenase pathway

    doi: 10.1186/s12974-015-0419-0

    Figure Lengend Snippet: ERK1/2 contributed to cPLA 2 phosphorylation after LPS/IFNγ stimulation. BV-2 cells were starved for 3 h in serum-free DMEM. One hour prior to stimulation, cells were pretreated with indicated concentrations of MAPK inhibitors: U0126 (U) for ERK1/2 inhibition, SB202190 (SB) for p38 MAPK inhibition, and SP600125 (SP) for JNK inhibition. Cells were then stimulated with a , c 200 ng/mL LPS or b , d 20 ng/mL IFNγ. Cells were lysed and proteins were collected and processed 2 h after LPS stimulation or 8 h after IFNγ stimulation for Western blot analyses. a , b Representative blots. Protein expression was quantified with QuantityOne software for three separate experiments for c LPS-stimulated BV-2 cells and d IFNγ-stimulated BV-2 cells. Results were expressed as the mean ± SEM ( n = 3) and significant difference from the respective group was determined by one-way ANOVA followed by Dunnett’s post-tests, * P

    Article Snippet: Pharmacological inhibitors used include the following: U0126, SB202190, and SP600125 were from Cell Signaling (Beverly, MA).

    Techniques: Inhibition, Western Blot, Expressing, Software

    Modulating of ERK1/2 activation was responsible for the apoptotic effect induced by 4-HNE. ( A ) Western blot analysis of MAP kinase expression in intestinal epithelial cells. Cells pretreated with NAC (5 mM, 2 h) were exposed to 4-HNE (80 μM for IEC-6 and 40 μM for IPEC-1) for 8 h, the protein levels of ERK1/2, p-ERK1/2, p38 MAPK, p-p38 MAPK, JNK and p-JNK were determined using indicated antibodies. β-actin was used as the loading control. ( B ) Western blot analysis of ERK1/2 activation in a time dependent manner. Cells pretreated with NAC (5 mM, 2 h) were exposed to 4-HNE for different time periods. The protein levels of ERK1/2, and p-ERK1/2 were determined. β-actin was used as the loading control. ( C ) Western blot analysis of ERK1/2 activation in intestinal epithelial cells treated with 4-HNE in the presence or absence of U0126. Cells pretreated with U0126 (10 μM, 1 h) were treated with indicated concentrations of 4-HNE for 2 h. The protein levels of ERK1/2, and p-ERK1/2 were determined. β-actin was used as the loading control. ( D ) Inhibition of ERK1/2 activation blocked 4-HNE-induced cell apoptosis. Cells were treated with 4-HNE (80 μM for IEC-6 and 40 μM for IPEC-1) for 8h after U0126 pretreatment (10 μM, 1 h), and then cell apoptosis was determined by Facs analysis. Values are expressed as the mean ± SEM (n = 3), * p

    Journal: Scientific Reports

    Article Title: 4-Hydroxy-2-nonenal induces apoptosis by activating ERK1/2 signaling and depleting intracellular glutathione in intestinal epithelial cells

    doi: 10.1038/srep32929

    Figure Lengend Snippet: Modulating of ERK1/2 activation was responsible for the apoptotic effect induced by 4-HNE. ( A ) Western blot analysis of MAP kinase expression in intestinal epithelial cells. Cells pretreated with NAC (5 mM, 2 h) were exposed to 4-HNE (80 μM for IEC-6 and 40 μM for IPEC-1) for 8 h, the protein levels of ERK1/2, p-ERK1/2, p38 MAPK, p-p38 MAPK, JNK and p-JNK were determined using indicated antibodies. β-actin was used as the loading control. ( B ) Western blot analysis of ERK1/2 activation in a time dependent manner. Cells pretreated with NAC (5 mM, 2 h) were exposed to 4-HNE for different time periods. The protein levels of ERK1/2, and p-ERK1/2 were determined. β-actin was used as the loading control. ( C ) Western blot analysis of ERK1/2 activation in intestinal epithelial cells treated with 4-HNE in the presence or absence of U0126. Cells pretreated with U0126 (10 μM, 1 h) were treated with indicated concentrations of 4-HNE for 2 h. The protein levels of ERK1/2, and p-ERK1/2 were determined. β-actin was used as the loading control. ( D ) Inhibition of ERK1/2 activation blocked 4-HNE-induced cell apoptosis. Cells were treated with 4-HNE (80 μM for IEC-6 and 40 μM for IPEC-1) for 8h after U0126 pretreatment (10 μM, 1 h), and then cell apoptosis was determined by Facs analysis. Values are expressed as the mean ± SEM (n = 3), * p

    Article Snippet: Kinases inhibitors, including ERK1/2 inhibitor U0126, JNK inhibitor SP600125, p38 MAPK inhibitor SB202190, and protein degradation inhibitor MG132 were obtained from Cell Signaling Technology (Beverly, MA).

    Techniques: Activation Assay, Western Blot, Expressing, Inhibition, FACS