sb202190  (Tocris)

 
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    Name:
    SB 202190
    Description:
    Potent selective inhibitor of p38 MAPK
    Catalog Number:
    1264
    Price:
    None
    Category:
    p38 MAPK Inhibitors p38 MAPK MAPK Family Kinases Enzymes Pharmacology
    Purity:
    ≥99% (HPLC)
    Formula:
    4-[4-(4-Fluorophenyl)-5-(4-pyridinyl)-1H-imidazol-2-yl]phenol
    Buy from Supplier


    Structured Review

    Tocris sb202190
    SB 202190
    Potent selective inhibitor of p38 MAPK
    https://www.bioz.com/result/sb202190/product/Tocris
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sb202190 - by Bioz Stars, 2021-03
    93/100 stars

    Images

    1) Product Images from "The Inflammatory Response to Double Stranded DNA in Endothelial Cells Is Mediated by NF?B and TNF?"

    Article Title: The Inflammatory Response to Double Stranded DNA in Endothelial Cells Is Mediated by NF?B and TNF?

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0019910

    dsDNA activates NFκB and MAPK pathways, which modulate adhesion molecule expression in endothelium. (a) Fluorescence histogram of NFκB reporter clone of endothelial cells treated with Lipofectamine alone (control) or dsDNA (2 µg/ml) for 16 hours. (b) ELISA for NFκB activity in endothelial cells stimulated with a dose of dsDNA (0 to 4 µg/ml) for 6 hours. (c) Phosphorylated protein levels in endothelial cells stimulated with dsDNA (2 µg/ml) for 6 hours. (d) Q-PCR for expression of ICAM-1, VCAM-1, and E-Selectin in RHMECs after stimulation with dsDNA (2 µg/ml) for 4 hours in the presence or absence of PDTC (PD), SP600125 (SP), or SB202190 (SB), which are inhibitors of NFκB, JNK, and p38 MAPK pathways, respectively. (*P
    Figure Legend Snippet: dsDNA activates NFκB and MAPK pathways, which modulate adhesion molecule expression in endothelium. (a) Fluorescence histogram of NFκB reporter clone of endothelial cells treated with Lipofectamine alone (control) or dsDNA (2 µg/ml) for 16 hours. (b) ELISA for NFκB activity in endothelial cells stimulated with a dose of dsDNA (0 to 4 µg/ml) for 6 hours. (c) Phosphorylated protein levels in endothelial cells stimulated with dsDNA (2 µg/ml) for 6 hours. (d) Q-PCR for expression of ICAM-1, VCAM-1, and E-Selectin in RHMECs after stimulation with dsDNA (2 µg/ml) for 4 hours in the presence or absence of PDTC (PD), SP600125 (SP), or SB202190 (SB), which are inhibitors of NFκB, JNK, and p38 MAPK pathways, respectively. (*P

    Techniques Used: Expressing, Fluorescence, Enzyme-linked Immunosorbent Assay, Activity Assay, Polymerase Chain Reaction

    dsDNA mediated TNFα secretion for sustained secondary activation of the endothelium. (a) Q-PCR for expression of TNFα in endothelial cells after stimulation with dsDNA (.5 or 4 µg/ml) or mock transfected with Lipofectamine for 12 hours. (b) ELISA for TNFα in culture supernatant of endothelial cells stimulated with dsDNA (.5 or 4 µg/ml) or mock transfected with Lipofectamine for 24 hours. (c) ELISA for TNFα in supernatants of wildtype MEFs (WT), TBK1/IKKε DKO MEFs (TBK1/IKKε DKO), and IKKα/IKKβ DKO MEFs (IKKα/IKKβ DKO) stimulated with 4 µg/mL of dsDNA for 24 hours. (d) ELISA for TNFα in supernatants of endothelial cells after stimulation with dsDNA (4 µg/ml) for 24 hours in the presence or absence of PDTC (PD), SB202190 (SB) or SP600125 (SP) which are inhibitors of NFκB, p38 MAPK and JNK pathways, respectively. (e) Q-PCR for expression of VCAM1 in endothelial cells stimulated with dsDNA (1 µg/ml) for 4 or 12 hours, in the presence or absence of TNFα neutralizing antibody (+Anti-TNFa) or cycloheximide (+CHX). (*P
    Figure Legend Snippet: dsDNA mediated TNFα secretion for sustained secondary activation of the endothelium. (a) Q-PCR for expression of TNFα in endothelial cells after stimulation with dsDNA (.5 or 4 µg/ml) or mock transfected with Lipofectamine for 12 hours. (b) ELISA for TNFα in culture supernatant of endothelial cells stimulated with dsDNA (.5 or 4 µg/ml) or mock transfected with Lipofectamine for 24 hours. (c) ELISA for TNFα in supernatants of wildtype MEFs (WT), TBK1/IKKε DKO MEFs (TBK1/IKKε DKO), and IKKα/IKKβ DKO MEFs (IKKα/IKKβ DKO) stimulated with 4 µg/mL of dsDNA for 24 hours. (d) ELISA for TNFα in supernatants of endothelial cells after stimulation with dsDNA (4 µg/ml) for 24 hours in the presence or absence of PDTC (PD), SB202190 (SB) or SP600125 (SP) which are inhibitors of NFκB, p38 MAPK and JNK pathways, respectively. (e) Q-PCR for expression of VCAM1 in endothelial cells stimulated with dsDNA (1 µg/ml) for 4 or 12 hours, in the presence or absence of TNFα neutralizing antibody (+Anti-TNFa) or cycloheximide (+CHX). (*P

    Techniques Used: Activation Assay, Polymerase Chain Reaction, Expressing, Transfection, Enzyme-linked Immunosorbent Assay

    2) Product Images from "The VGF-derived peptide TLQP-21 contributes to inflammatory and nerve injury-induced hypersensitivity"

    Article Title: The VGF-derived peptide TLQP-21 contributes to inflammatory and nerve injury-induced hypersensitivity

    Journal: Pain

    doi: 10.1016/j.pain.2014.03.012

    Spinal effects of exogenous TLQP-21 peptide. A , Intrathecal injection of TLQP-21 induced dose-dependent thermal hyperalgesia in the warm water immersion tail withdrawal test. B–D , The p38 MAPK inhibitor SB202190 ( B ), the cyclooxygenase (COX) inhibitor
    Figure Legend Snippet: Spinal effects of exogenous TLQP-21 peptide. A , Intrathecal injection of TLQP-21 induced dose-dependent thermal hyperalgesia in the warm water immersion tail withdrawal test. B–D , The p38 MAPK inhibitor SB202190 ( B ), the cyclooxygenase (COX) inhibitor

    Techniques Used: Injection

    3) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    4) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    5) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    6) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    7) Product Images from ""

    Article Title:

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E06-02-0122

    The JNK signaling pathway is involved in the control of claudin-2, but not ZO-3 expression, independently of cingulin depletion and RhoA activity. (A) Immunoblotting analysis of cell lysates prepared from cingulin KD clone A treated either with solvent (dimethyl sulfoxide) or the MAPK/ERK inhibitor U0126 (15 μM), or the p38 kinase inhibitor SB202190 (20 μM), or the JNK inhibitor SP600125 (30 μM). Note the decrease in claudin-2 protein levels only in lysates from cells treated with the JNK inhibitor SP600125. Images are representative of two independent experiments, and the same results were obtained with cingulin KD clone B (our unpublished data). (B) Immunoblotting analysis of the effect of the JNK inhibitor SP600125 (30 μM) on the expression of cingulin, ZO-3, and claudin-2 in WT cells and control and cingulin KD clones. Note that SP600125 does not affect the protein expression levels of cingulin and ZO-3, but it reduces claudin-2 levels in WT cells and control and cingulin KD clones. Images are representative of two independent experiments. (C) Immunoblotting analysis of active JNK (phospho-JNK) (top) and total JNK (bottom), either in the absence (−) or in the presence (+) of the JNK inhibitor SP600125 (30 μM) in WT MDCK cells. Note that the JNK inhibitor decreases phospho-JNK levels by > 75%. Similar results were obtained for control and cingulin KD clones (our unpublished data). Images are representative of two independent experiments. (D) Immunoblotting analysis of JNK activity in WT cells and control and cingulin KD clones with or without (NT) coexpression of the dominant-negative RhoA mutant RhoAN19. Note that phospho-JNK levels are not affected either by cingulin depletion or by inhibition of RhoA. Images are representative of two independent experiments. (E) Immunoblotting analysis of claudin-2 levels in cingulin KD clones A and B, either untreated, or treated with the JNK inhibitor SP600125 (30 μM), with or without coexpression of RhoAN19. Note that claudin-2 levels in cells where JNK is inhibited are further decreased when RhoA is also inhibited.
    Figure Legend Snippet: The JNK signaling pathway is involved in the control of claudin-2, but not ZO-3 expression, independently of cingulin depletion and RhoA activity. (A) Immunoblotting analysis of cell lysates prepared from cingulin KD clone A treated either with solvent (dimethyl sulfoxide) or the MAPK/ERK inhibitor U0126 (15 μM), or the p38 kinase inhibitor SB202190 (20 μM), or the JNK inhibitor SP600125 (30 μM). Note the decrease in claudin-2 protein levels only in lysates from cells treated with the JNK inhibitor SP600125. Images are representative of two independent experiments, and the same results were obtained with cingulin KD clone B (our unpublished data). (B) Immunoblotting analysis of the effect of the JNK inhibitor SP600125 (30 μM) on the expression of cingulin, ZO-3, and claudin-2 in WT cells and control and cingulin KD clones. Note that SP600125 does not affect the protein expression levels of cingulin and ZO-3, but it reduces claudin-2 levels in WT cells and control and cingulin KD clones. Images are representative of two independent experiments. (C) Immunoblotting analysis of active JNK (phospho-JNK) (top) and total JNK (bottom), either in the absence (−) or in the presence (+) of the JNK inhibitor SP600125 (30 μM) in WT MDCK cells. Note that the JNK inhibitor decreases phospho-JNK levels by > 75%. Similar results were obtained for control and cingulin KD clones (our unpublished data). Images are representative of two independent experiments. (D) Immunoblotting analysis of JNK activity in WT cells and control and cingulin KD clones with or without (NT) coexpression of the dominant-negative RhoA mutant RhoAN19. Note that phospho-JNK levels are not affected either by cingulin depletion or by inhibition of RhoA. Images are representative of two independent experiments. (E) Immunoblotting analysis of claudin-2 levels in cingulin KD clones A and B, either untreated, or treated with the JNK inhibitor SP600125 (30 μM), with or without coexpression of RhoAN19. Note that claudin-2 levels in cells where JNK is inhibited are further decreased when RhoA is also inhibited.

    Techniques Used: Expressing, Activity Assay, Clone Assay, Dominant Negative Mutation, Mutagenesis, Inhibition

    8) Product Images from "Sodium Chloride Drives Autoimmune Disease by the Induction of Pathogenic Th17 Cells"

    Article Title: Sodium Chloride Drives Autoimmune Disease by the Induction of Pathogenic Th17 Cells

    Journal: Nature

    doi: 10.1038/nature11868

    The induction of Th17 cells by sodium chloride depends on p38/MAPK, NFAT5 and SGK1 a , Naive CD4 + cells were stimulated in the presence (NaCl) or absence (none) of additional 40 mM NaCl and were analysed by FACS for phosphorylated p38 (p-p38; n = 5). b, Naïve CD4 cells were differentiated into Th17 cells as indicated in the presence or absence of NaCl and SB202190 (p38i) and analysed by qRT-PCR as depicted in the bar graph (n=7) or by FACS (the left row shows cells differentiated in the absence of TGF-β1). c, Naïve CD4 cells were stimulated for 3h in the presence or absence of NaCl and SB202190 and analysed by qRT-PCR for NFAT5 (n=4). d, Cells were transduced with NFAT5 specific (shNFAT5) or control shRNA (control), stimulated like in b) and analysed by FACS. The bar graphs depict qRT-PCR analyses of NFAT5 , IL-17A and SLC5A3 (n=5). CCR6 was analysed by FACS (black histogram: control, grey histogram: shNFAT5, one representative experiment of four is shown). e, Cells were stimulated like in c), but analysed by qRT-PCR for SGK1 (n=4). f, Cells were transduced with a shRNA specific for SGK1 (shSGK1) or a control shRNA (control) and activated like in b), and analysed by FACS. Expression of SGK1 and IL-17A was determined by qRT-PCR (n=5). CCR6 was analysed by FACS (black histogram: control, grey histogram: shSGK1, one representative experiment of four is shown). g, Cells were cultured like in b), but in the presence or absence of the SGK1 inhibitor GSK650394 (SGK1i) and analysed by FACS. The bar graph shows qRT-PCR for IL-17A under similar conditions (n=5). FACS and qRT-PCR (relative expression) data depicted in bar graphs were normalised to controls.
    Figure Legend Snippet: The induction of Th17 cells by sodium chloride depends on p38/MAPK, NFAT5 and SGK1 a , Naive CD4 + cells were stimulated in the presence (NaCl) or absence (none) of additional 40 mM NaCl and were analysed by FACS for phosphorylated p38 (p-p38; n = 5). b, Naïve CD4 cells were differentiated into Th17 cells as indicated in the presence or absence of NaCl and SB202190 (p38i) and analysed by qRT-PCR as depicted in the bar graph (n=7) or by FACS (the left row shows cells differentiated in the absence of TGF-β1). c, Naïve CD4 cells were stimulated for 3h in the presence or absence of NaCl and SB202190 and analysed by qRT-PCR for NFAT5 (n=4). d, Cells were transduced with NFAT5 specific (shNFAT5) or control shRNA (control), stimulated like in b) and analysed by FACS. The bar graphs depict qRT-PCR analyses of NFAT5 , IL-17A and SLC5A3 (n=5). CCR6 was analysed by FACS (black histogram: control, grey histogram: shNFAT5, one representative experiment of four is shown). e, Cells were stimulated like in c), but analysed by qRT-PCR for SGK1 (n=4). f, Cells were transduced with a shRNA specific for SGK1 (shSGK1) or a control shRNA (control) and activated like in b), and analysed by FACS. Expression of SGK1 and IL-17A was determined by qRT-PCR (n=5). CCR6 was analysed by FACS (black histogram: control, grey histogram: shSGK1, one representative experiment of four is shown). g, Cells were cultured like in b), but in the presence or absence of the SGK1 inhibitor GSK650394 (SGK1i) and analysed by FACS. The bar graph shows qRT-PCR for IL-17A under similar conditions (n=5). FACS and qRT-PCR (relative expression) data depicted in bar graphs were normalised to controls.

    Techniques Used: FACS, Quantitative RT-PCR, Transduction, shRNA, Expressing, Cell Culture

    9) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    10) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    11) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    12) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    13) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    14) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    15) Product Images from "TNF‐α signaling regulates RUNX1 function in endothelial cells, et al. TNF‐α signaling regulates RUNX1 function in endothelial cells"

    Article Title: TNF‐α signaling regulates RUNX1 function in endothelial cells, et al. TNF‐α signaling regulates RUNX1 function in endothelial cells

    Journal: The FASEB Journal

    doi: 10.1096/fj.202001668R

    RUNX1 expression was reduced by blocking the TNF‐α mediated JNK signaling pathway. Treatment of HRMECs with TNF‐α (5 ng/mL) in combination with TNFR1 inhibitor, CAY10500 (1 μM); NF‐κB inhibitors, CAPE (1 μM) and Honokiol (5 μM); dual NF‐κB and JNK inhibitor, Withaferin A (5 μM); JNK inhibitors, SP600125 (1 μM) and TCS JNK 6o (5 μM) and p38/MAPK inhibitors, SB239063 (5 μM) and SB202190 (5 μM). Cells were treated for (A) 48 hours for quantification by qRT‐PCR (n = 6) and (B) 72 hours for Western blot analyses (n = 2). qRT‐PCR data are shown as (log 2 ‐(fold change)), normalized to endogenous HPRT expression and unstimulated control. Western blot analyses are normalized to β‐actin and unstimulated control. Shown are mean values + SEM. Data are analyzed using one‐way ANOVA with Dunnett's post hoc test. * P
    Figure Legend Snippet: RUNX1 expression was reduced by blocking the TNF‐α mediated JNK signaling pathway. Treatment of HRMECs with TNF‐α (5 ng/mL) in combination with TNFR1 inhibitor, CAY10500 (1 μM); NF‐κB inhibitors, CAPE (1 μM) and Honokiol (5 μM); dual NF‐κB and JNK inhibitor, Withaferin A (5 μM); JNK inhibitors, SP600125 (1 μM) and TCS JNK 6o (5 μM) and p38/MAPK inhibitors, SB239063 (5 μM) and SB202190 (5 μM). Cells were treated for (A) 48 hours for quantification by qRT‐PCR (n = 6) and (B) 72 hours for Western blot analyses (n = 2). qRT‐PCR data are shown as (log 2 ‐(fold change)), normalized to endogenous HPRT expression and unstimulated control. Western blot analyses are normalized to β‐actin and unstimulated control. Shown are mean values + SEM. Data are analyzed using one‐way ANOVA with Dunnett's post hoc test. * P

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

    16) Product Images from "Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia"

    Article Title: Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia

    Journal:

    doi: 10.1038/sj.bjp.0706347

    (a) Effect of AG490, SB202190 and LY294002 on the P1GF-induced proliferation of cultured VSMCs. Growth-arrested and hypoxia-treated VSMCs were stimulated with 20 ng ml −1 P1GF in the presence and in the absence (control) of the
    Figure Legend Snippet: (a) Effect of AG490, SB202190 and LY294002 on the P1GF-induced proliferation of cultured VSMCs. Growth-arrested and hypoxia-treated VSMCs were stimulated with 20 ng ml −1 P1GF in the presence and in the absence (control) of the

    Techniques Used: Cell Culture

    Effect of SB202190 (10–1000 n M ) on the contractile response induced by P1GF in preparations exposed to hypoxia. Data are expressed as percent of P1GF-induced contraction (control). Means±s.e.m. of four preparations from four animals
    Figure Legend Snippet: Effect of SB202190 (10–1000 n M ) on the contractile response induced by P1GF in preparations exposed to hypoxia. Data are expressed as percent of P1GF-induced contraction (control). Means±s.e.m. of four preparations from four animals

    Techniques Used:

    17) Product Images from "Trichoplein binds PCM1 and controls endothelial cell function by regulating autophagy"

    Article Title: Trichoplein binds PCM1 and controls endothelial cell function by regulating autophagy

    Journal: EMBO Reports

    doi: 10.15252/embr.201948192

    Identification of the mechanism of p62 accumulation Representative images for p62 of control and TCHP knock‐down HUVECs treated with BAY11‐7082 (300 nM) or TYRPHOSTIN AG1288 (300 nM) or SB202190 (300 nM) or vehicle (DMSO) for 48 h. Scale bars, 50 μm. (B) Expression of IL‐6, IL‐8 and IL‐1β (one‐way ANOVA; IL‐8: ** P = 0.008 vs. control DMSO; # P = 0.0198 (BAY) # P = 0.01 (AG) vs. shTCHP DMSO; IL‐6: ** P = 0.0023 vs. control DMSO; # P = 0.0063 (BAY) # P = 0.0108 (AG) vs. shTCHP DMSO; IL‐1β: ** P = 0.0011 vs. control DMSO; # P = 0.0004 (BAY) # P = 0.0015 (AG) vs. shTCHP DMSO) and (C), migration speed was measured (one‐way ANOVA; ** P = 0.0003 vs. control DMSO; # P = 0.0451 vs. shTCHP DMSO). Western blot analysis for anti‐phosphor‐NF‐κB (S536), total NF‐κB, in TCHP knock‐down and control cells treated with BAY or vehicle. Below panel: quantification (one‐way ANOVA; ** P = 0.0014 vs. control DMSO; # P = 0.0293 vs. shTCHP DMSO). p62 expression in TCHP knock‐down and control cells treated with BAY or vehicle (one‐way ANOVA; ** P = 0.0004 vs. control DMSO; # P = 0.0243 vs. shTCHP DMSO). p62 expression in TCHP knock‐down and control cells treated with siRELA or control (one‐way ANOVA; ** P = 0.0023 vs. control siRNA; # P = 0.0127 vs. shTCHP siRELA). ChIP‐qPCR analysis confirms the of NF‐κB p65 enrichment to IκBα and p62 promoter in TCHP knock‐down cells (unpaired t ‐test; ** P = 0.0057 and ** P = 0.0037 vs. control, respectively). Data information: Statistical analyses were performed on at least three independent experiments. Data are represented as mean ± SD.
    Figure Legend Snippet: Identification of the mechanism of p62 accumulation Representative images for p62 of control and TCHP knock‐down HUVECs treated with BAY11‐7082 (300 nM) or TYRPHOSTIN AG1288 (300 nM) or SB202190 (300 nM) or vehicle (DMSO) for 48 h. Scale bars, 50 μm. (B) Expression of IL‐6, IL‐8 and IL‐1β (one‐way ANOVA; IL‐8: ** P = 0.008 vs. control DMSO; # P = 0.0198 (BAY) # P = 0.01 (AG) vs. shTCHP DMSO; IL‐6: ** P = 0.0023 vs. control DMSO; # P = 0.0063 (BAY) # P = 0.0108 (AG) vs. shTCHP DMSO; IL‐1β: ** P = 0.0011 vs. control DMSO; # P = 0.0004 (BAY) # P = 0.0015 (AG) vs. shTCHP DMSO) and (C), migration speed was measured (one‐way ANOVA; ** P = 0.0003 vs. control DMSO; # P = 0.0451 vs. shTCHP DMSO). Western blot analysis for anti‐phosphor‐NF‐κB (S536), total NF‐κB, in TCHP knock‐down and control cells treated with BAY or vehicle. Below panel: quantification (one‐way ANOVA; ** P = 0.0014 vs. control DMSO; # P = 0.0293 vs. shTCHP DMSO). p62 expression in TCHP knock‐down and control cells treated with BAY or vehicle (one‐way ANOVA; ** P = 0.0004 vs. control DMSO; # P = 0.0243 vs. shTCHP DMSO). p62 expression in TCHP knock‐down and control cells treated with siRELA or control (one‐way ANOVA; ** P = 0.0023 vs. control siRNA; # P = 0.0127 vs. shTCHP siRELA). ChIP‐qPCR analysis confirms the of NF‐κB p65 enrichment to IκBα and p62 promoter in TCHP knock‐down cells (unpaired t ‐test; ** P = 0.0057 and ** P = 0.0037 vs. control, respectively). Data information: Statistical analyses were performed on at least three independent experiments. Data are represented as mean ± SD.

    Techniques Used: Expressing, Migration, Western Blot, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction

    18) Product Images from "COX-2 expression mediated by calcium-TonEBP signaling axis under hyperosmotic conditions serves osmoprotective function in nucleus pulposus cells"

    Article Title: COX-2 expression mediated by calcium-TonEBP signaling axis under hyperosmotic conditions serves osmoprotective function in nucleus pulposus cells

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA117.001167

    Hyperosmotic induction of COX-2 is mediated by p38, but not by ERK or JNK. A and B , phospho-p38 ( p-p38 ) levels significantly increase in response to hyperosmolarity. C and D , hyperosmotic increase of COX-2 mRNA is completely suppressed by p38 inhibitor, SB202190, but unaffected by JNK inhibitor, SP600125, and MEK/ERK inhibitor, PD98059. E , Western blot images showing that p38 inhibition prevents COX-2 induction in response to hyperosmolarity. F , Western blot images showing that ionomycin/PMA (I + P)-mediated COX-2 induction is not affected by p38 inhibition. G , densitometry analyses of Western blots shown in E and F . All the quantitative data are represented as mean ± S.D. from at least three independent experiments (three biological replicates). NS : nonsignificant; *, p
    Figure Legend Snippet: Hyperosmotic induction of COX-2 is mediated by p38, but not by ERK or JNK. A and B , phospho-p38 ( p-p38 ) levels significantly increase in response to hyperosmolarity. C and D , hyperosmotic increase of COX-2 mRNA is completely suppressed by p38 inhibitor, SB202190, but unaffected by JNK inhibitor, SP600125, and MEK/ERK inhibitor, PD98059. E , Western blot images showing that p38 inhibition prevents COX-2 induction in response to hyperosmolarity. F , Western blot images showing that ionomycin/PMA (I + P)-mediated COX-2 induction is not affected by p38 inhibition. G , densitometry analyses of Western blots shown in E and F . All the quantitative data are represented as mean ± S.D. from at least three independent experiments (three biological replicates). NS : nonsignificant; *, p

    Techniques Used: Western Blot, Inhibition

    19) Product Images from "Activation of Ca2+-sensing receptor as a protective pathway to reduce Cadmium-induced cytotoxicity in renal proximal tubular cells"

    Article Title: Activation of Ca2+-sensing receptor as a protective pathway to reduce Cadmium-induced cytotoxicity in renal proximal tubular cells

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-19327-9

    R-467 reduced apoptosis and induced cell proliferation. ( a ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated apoptosis. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of cleaved caspase-3. ( b ) Inhibition of MAPK signaling pathway on Cd induced cytotoxicity. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, the cell viability was evaluated by MTT assay. SB202190, SP600125 significantly inhibited Cd-induced cell death. Co-treatment of R-467 eliminated Cd-induced cytotoxicity, but suppressed by pretreatment of PD98059. Results are presented as mean ± SD (n = 4). *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P
    Figure Legend Snippet: R-467 reduced apoptosis and induced cell proliferation. ( a ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated apoptosis. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of cleaved caspase-3. ( b ) Inhibition of MAPK signaling pathway on Cd induced cytotoxicity. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, the cell viability was evaluated by MTT assay. SB202190, SP600125 significantly inhibited Cd-induced cell death. Co-treatment of R-467 eliminated Cd-induced cytotoxicity, but suppressed by pretreatment of PD98059. Results are presented as mean ± SD (n = 4). *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P

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

    20) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    21) Product Images from "Activation of Ca2+-sensing receptor as a protective pathway to reduce Cadmium-induced cytotoxicity in renal proximal tubular cells"

    Article Title: Activation of Ca2+-sensing receptor as a protective pathway to reduce Cadmium-induced cytotoxicity in renal proximal tubular cells

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-19327-9

    R-467 reduced apoptosis and induced cell proliferation. ( a ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated apoptosis. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of cleaved caspase-3. ( b ) Inhibition of MAPK signaling pathway on Cd induced cytotoxicity. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, the cell viability was evaluated by MTT assay. SB202190, SP600125 significantly inhibited Cd-induced cell death. Co-treatment of R-467 eliminated Cd-induced cytotoxicity, but suppressed by pretreatment of PD98059. Results are presented as mean ± SD (n = 4). *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P
    Figure Legend Snippet: R-467 reduced apoptosis and induced cell proliferation. ( a ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated apoptosis. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of cleaved caspase-3. ( b ) Inhibition of MAPK signaling pathway on Cd induced cytotoxicity. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, the cell viability was evaluated by MTT assay. SB202190, SP600125 significantly inhibited Cd-induced cell death. Co-treatment of R-467 eliminated Cd-induced cytotoxicity, but suppressed by pretreatment of PD98059. Results are presented as mean ± SD (n = 4). *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P

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

    Effects of calcimimetics on Cd-induced ROS generation, autophagic flux inhibition and apoptosis. ( a ) Effect of U73122, 2-APB, BAPTA and Cd increased ROS generation in mRTEC cells. Cells pretreated with U73122 (1 μM), 2-APB (50 μM), and BAPTA (10 μM) for 30 min, followed Cd treatment (5 μM) or Cd (5 μM) + R-467 (1 μM) for 6 h, relative ROS levels in mRTEC cells were determined. Results are presented as mean ± SD (n = 4). ( b , c ) Western blotting shows effects of TCP, CQ and co-treatments of calcimimetics R-467 or S-467 with Cd on Cd-induced autophagy flux inhibition and apoptosis. Cells pretreated with TCP (100 μM) or CQ (20 μM) for 30 min, followed Cd treatment (5 μM) or Cd (5 μM) + R-467 (1 μM) for 24 h, total proteins were extracted for western blotting analysis of expressions of LC3-II and p62, and cleaved caspase-3. ( d ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated cell autophagy. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of LC3-II and p62. *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P
    Figure Legend Snippet: Effects of calcimimetics on Cd-induced ROS generation, autophagic flux inhibition and apoptosis. ( a ) Effect of U73122, 2-APB, BAPTA and Cd increased ROS generation in mRTEC cells. Cells pretreated with U73122 (1 μM), 2-APB (50 μM), and BAPTA (10 μM) for 30 min, followed Cd treatment (5 μM) or Cd (5 μM) + R-467 (1 μM) for 6 h, relative ROS levels in mRTEC cells were determined. Results are presented as mean ± SD (n = 4). ( b , c ) Western blotting shows effects of TCP, CQ and co-treatments of calcimimetics R-467 or S-467 with Cd on Cd-induced autophagy flux inhibition and apoptosis. Cells pretreated with TCP (100 μM) or CQ (20 μM) for 30 min, followed Cd treatment (5 μM) or Cd (5 μM) + R-467 (1 μM) for 24 h, total proteins were extracted for western blotting analysis of expressions of LC3-II and p62, and cleaved caspase-3. ( d ) Inhibition of MAPK signaling pathway on Cd and R-467-regulated cell autophagy. Cells pretreated with SB202190 (10 μM), SP600125 (10 μM) or PD98059 (10 μM), for 30 min, followed by Cd treatment (5 μM) or co-treated with R-467 (1 μM) for 24 h, total proteins were extracted for Western blotting analysis of expression of LC3-II and p62. *Statistical significance between control and treatments or Cd treatment and in presence of inhibitors or calcimimetics, * P

    Techniques Used: Inhibition, Western Blot, Expressing

    22) Product Images from "Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids"

    Article Title: Direct activation of the mitochondrial calcium uniporter by natural plant flavonoids

    Journal: Biochemical Journal

    doi: 10.1042/BJ20040990

    Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.
    Figure Legend Snippet: Inhibition by Ru360 of the mitochondrial Ca 2+ uptake induced by kaempferol and SB202190 MM5 cells expressing mitochondrially targeted mutated aequorin reconstituted with coelenterazine n were permeabilized as described in the Experimental section. Then a Ca 2+ buffer containing 3.5 μM [Ca 2+ ] was perfused either in the absence (Control) or in the presence of 5 μM kaempferol, 10 μM SB202190, 5 μM kaempferol plus 100 nM Ru360 or 10 μM SB202190 plus 100 nM Ru360, as indicated. The experiments shown are representative of 3 similar ones of each type.

    Techniques Used: Inhibition, Expressing

    Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.
    Figure Legend Snippet: Chemical structures of SB202190 and the natural flavonoids used in this study The structure of kaempferol shows the standard letter code used to name flavone rings.

    Techniques Used:

    23) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    24) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    25) Product Images from "Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190"

    Article Title: Separating myoblast differentiation from muscle cell fusion using IGF-I and the p38 MAP kinase inhibitor SB202190

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00184.2015

    IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.
    Figure Legend Snippet: IGF-I promotes muscle differentiation, but not myocyte fusion, in the presence of the p38 inhibitor SB202190. A : experimental plan. Confluent C2 myoblasts were incubated in DM with SB202190 (5 μM) ± R3-IGF-I (1 nM). After 44 h, medium was replaced, and new DM was added ± SB202190 for an additional 30 h. B : immunocytochemistry for troponin-T (red) and myogenin (green). Magnification ×100 (scale bars = 100 μm). C : immunocytochemistry for troponin-T (red) and myogenin (green) and staining for nuclei with Hoechst 33258 (blue). Magnification ×200 (scale bars = 50 μm). D : changes in the extent of myocyte fusion over time during incubation ± SB during live-cell imaging.

    Techniques Used: Incubation, Immunocytochemistry, Staining, Live Cell Imaging

    SB202190
    Figure Legend Snippet: SB202190

    Techniques Used:

    Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.
    Figure Legend Snippet: Muscle and signaling protein expression after removal of the p38 inhibitor SB202190. Protein expression by immunoblotting for MyoD, myogenin, Mef2C, troponin-T, myosin heavy chain (MHC), phosphorylated (p)-p38 and total p38, p-Erk and total Erk, p-Akt (pAkt S308 ) and total Akt, p-mammalian target of rapamycin (mTor) and total mTor, and α-tubulin by immunoblotting during incubation of C2 myoblasts in DM plus SB202190 and R3-IGF-I or after removal of SB202190. Molecular mass markers are indicated at right . Images are representative of ≥3 independent experiments.

    Techniques Used: Expressing, Incubation

    26) Product Images from "Type I and Type III Interferons Display Different Dependency on Mitogen-Activated Protein Kinases to Mount an Antiviral State in the Human Gut"

    Article Title: Type I and Type III Interferons Display Different Dependency on Mitogen-Activated Protein Kinases to Mount an Antiviral State in the Human Gut

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2017.00459

    The antiviral activity of type III interferons (IFNs) strongly dependent on mitogen-activated protein kinases in the contact of primary human intestinal epithelial cells . Human colon organoids were mock incubated (black bar) or pre-incubated with 2 μM Pyridone 6 (pan-JAK inhibitor), 10 μM U0126 (ERK inhibitor), 10 μM M SB202190 (p38 inhibitor) and 100 μM SP600125 (JNK inhibitor). One hour posttreatment, organoids were mock treated (black bar) or co-treated with type I IFN (β) (2,000 RU/mL equivalent 8 ng/mL) or type III IFN (λ1−3) (300 ng/mL) for 2 h. Organoids were then infected with VSV expressing luciferase (multiplicity of infection = 1). Eight hpi, viral replication was assayed by measuring the luciferase activity. Data are normalized to non-IFN-treated sample for each inhibitor (set to 100). The mean value obtained from three independent experiments is plotted. Error bars indicate the SD. **** P
    Figure Legend Snippet: The antiviral activity of type III interferons (IFNs) strongly dependent on mitogen-activated protein kinases in the contact of primary human intestinal epithelial cells . Human colon organoids were mock incubated (black bar) or pre-incubated with 2 μM Pyridone 6 (pan-JAK inhibitor), 10 μM U0126 (ERK inhibitor), 10 μM M SB202190 (p38 inhibitor) and 100 μM SP600125 (JNK inhibitor). One hour posttreatment, organoids were mock treated (black bar) or co-treated with type I IFN (β) (2,000 RU/mL equivalent 8 ng/mL) or type III IFN (λ1−3) (300 ng/mL) for 2 h. Organoids were then infected with VSV expressing luciferase (multiplicity of infection = 1). Eight hpi, viral replication was assayed by measuring the luciferase activity. Data are normalized to non-IFN-treated sample for each inhibitor (set to 100). The mean value obtained from three independent experiments is plotted. Error bars indicate the SD. **** P

    Techniques Used: Activity Assay, Incubation, Infection, Expressing, Luciferase

    Type III interferons (IFNs) require mitogen-activated protein kinases for their antiviral response . (A) T84 cells were mock incubated (black bar) or pre-incubated for 30 min with 2 μM Pyridone 6 (pan-JAK inhibitor), 10 μM U0126 (ERK inhibitor), 10 μM SB202190 (p38 inhibitor), or 100 μM SP600125 (JNK inhibitor). Then, T84 cells were mock treated (black bar) or treated with type I IFN (β) (2,000 RU/mL equivalent 8 ng/mL) or type III IFN (λ1−3) (300 ng/mL) in the presence the inhibitor. Two hours post-IFN treatment cells were infected with a multiplicity of infection of 1 with VSV expressing luciferase (left panel) or mammalian reovirus (right panel). Viral replication was assayed by measuring the luciferase activity or by relative quantification of viral genome using qRT-PCR. Data were normalized to non-IFN-treated sample for each inhibitor (set to 100). (B) Same as (A) , except T84 cells were pre-incubated with increasing concentrations of JAK or MAP kinase inhibitors prior to treatment with IFNs. The mean value obtained from three independent experiments, is plotted. Error bars indicate the SD. **** P
    Figure Legend Snippet: Type III interferons (IFNs) require mitogen-activated protein kinases for their antiviral response . (A) T84 cells were mock incubated (black bar) or pre-incubated for 30 min with 2 μM Pyridone 6 (pan-JAK inhibitor), 10 μM U0126 (ERK inhibitor), 10 μM SB202190 (p38 inhibitor), or 100 μM SP600125 (JNK inhibitor). Then, T84 cells were mock treated (black bar) or treated with type I IFN (β) (2,000 RU/mL equivalent 8 ng/mL) or type III IFN (λ1−3) (300 ng/mL) in the presence the inhibitor. Two hours post-IFN treatment cells were infected with a multiplicity of infection of 1 with VSV expressing luciferase (left panel) or mammalian reovirus (right panel). Viral replication was assayed by measuring the luciferase activity or by relative quantification of viral genome using qRT-PCR. Data were normalized to non-IFN-treated sample for each inhibitor (set to 100). (B) Same as (A) , except T84 cells were pre-incubated with increasing concentrations of JAK or MAP kinase inhibitors prior to treatment with IFNs. The mean value obtained from three independent experiments, is plotted. Error bars indicate the SD. **** P

    Techniques Used: Incubation, Infection, Expressing, Luciferase, Activity Assay, Quantitative RT-PCR

    Related Articles

    other:

    Article Title: Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia
    Article Snippet: To further investigate the intracellular mechanisms activated by P1GF that were possibly responsible for its mitogenic effects, growth-arrested VSMCs previously exposed to hypoxia were stimulated by 20 ng ml−1 P1GF after pretreatment for 1 h with (10–30 μ M ), AG 490 (1–10 μ M ) and SB202190 (1–10 μ M ), able to inhibit PI3K, JAK and p38, respectively.

    Article Title: Ligand-Directed Functional Selectivity at the Mu Opioid Receptor Revealed by Label-Free Integrative Pharmacology On-Target
    Article Snippet: DAMGO, DPDPE, BRL-53527, CTOP, naltrindole hydrochloride, norbinaltorphimine, U0126, SB202190, SP600125, and LY294002 were purchased from Tocris Biosciences (Ellisville, MO).

    Diff-Quik:

    Article Title: Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia
    Article Snippet: Noradrenaline, indomethacin, wortmannin, poly(Glu : Tyr 4 : 1) and cell culture media and reagents were purchased from Sigma Chemical Co. (St Louis, MO, U.S.A.). .. Calf serum was purchased from Hyclone (Logan, UT, U.S.A.); Diff-Quik from Merz+Dade AG (Switzerland); , VEGF-A from Calbiochem-Novabiochem Int. (San Diego, CA, U.S.A.); AG 490, U0126, SB202190 from Tocris Cookson Ltd (Avonmouth, U.K.); anti p-p38 [pTyr1807182 ] was from BioSource Europe SA (Nivelles, Belgium); anti p-Akt [pSer473], anti-p-STAT3 and anti-p-ERK1/2 [Thr202 /Tyr204 ] were from Cell Signaling Technology (Frankfurt, Germany); anti-rabbit IgG peroxidase-linked antibody was from Amersham International Biotech (U.K.); anti-mouse IgG1 peroxidase-linked antibody was from Calbiochem-Novabiochem Int. (San Diego, CA, U.S.A.); Akt1 IP-kinase assay kit was from Upstate (Lake Placid, NY, U.S.A.). .. Acrylamide, TEMED, ammonium persulphate, Coomassie brilliant blue were from Bio-Rad Laboratories (Richmond, CA, U.S.A.).

    IP-Kinase Assay:

    Article Title: Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia
    Article Snippet: Noradrenaline, indomethacin, wortmannin, poly(Glu : Tyr 4 : 1) and cell culture media and reagents were purchased from Sigma Chemical Co. (St Louis, MO, U.S.A.). .. Calf serum was purchased from Hyclone (Logan, UT, U.S.A.); Diff-Quik from Merz+Dade AG (Switzerland); , VEGF-A from Calbiochem-Novabiochem Int. (San Diego, CA, U.S.A.); AG 490, U0126, SB202190 from Tocris Cookson Ltd (Avonmouth, U.K.); anti p-p38 [pTyr1807182 ] was from BioSource Europe SA (Nivelles, Belgium); anti p-Akt [pSer473], anti-p-STAT3 and anti-p-ERK1/2 [Thr202 /Tyr204 ] were from Cell Signaling Technology (Frankfurt, Germany); anti-rabbit IgG peroxidase-linked antibody was from Amersham International Biotech (U.K.); anti-mouse IgG1 peroxidase-linked antibody was from Calbiochem-Novabiochem Int. (San Diego, CA, U.S.A.); Akt1 IP-kinase assay kit was from Upstate (Lake Placid, NY, U.S.A.). .. Acrylamide, TEMED, ammonium persulphate, Coomassie brilliant blue were from Bio-Rad Laboratories (Richmond, CA, U.S.A.).

    Proliferation Assay:

    Article Title: Intracellular pathways triggered by the selective FLT-1-agonist placental growth factor in vascular smooth muscle cells exposed to hypoxia
    Article Snippet: Acrylamide, TEMED, ammonium persulphate, Coomassie brilliant blue were from Bio-Rad Laboratories (Richmond, CA, U.S.A.). .. [ γ 32 P]ATP was from NEN (Boston, MA, U.S.A.)., AG490, U0126 and SB202190 were dissolved in DMSO and further diluted in DMEM, for cell proliferation assay, and in Tyrode solution, for vascular tone experiments. .. It is noteworthy that the amount of DMSO present at the highest inhibitor concentration used (0.001, 0.01 and 0.1% for wortmanin, SB202190 and AG40, , U0126, respectively) did not affect either cell proliferation or vascular tone.

    Protease Inhibitor:

    Article Title: Metabolic Reprogramming Is Required for Myofibroblast Contractility and Differentiation *
    Article Snippet: Our study supports the essential role for the integration of cellular bioenergetics with gene expression to sustain the differentiated phenotype of myofibroblasts. .. Porcine platelet-derived TGF-β1 was purchased from R & D Systems (Minneapolis, MN), protease inhibitor mixture set III was from EMD Chemicals (San Diego, CA), p38 MAPK inhibitor SB202190 was from Tocris Bioscience (Minneapolis, MN), and MitoTracker® was from Life Technologies. .. We purchased antibodies to β-actin (clone AC-15), fibronectin (clone IST-4), and α-tubulin (clone B-5-1-2) from Sigma; α-SMA (clone ASM-1) from American Research Products (Belmont, MA); TFAM, total PGC-1α, hexokinase II (HKII), total MLC20, phospho-MLC20, GAPDH, VDAC, p38 MAPK from Cell Signaling Technology (Boston, MA); TOM20 and lamin A/C from Santa Cruz Biotechnology (Dallas, TX); and phospho-PGC-1α from R & D Systems.

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    Tocris sb202190
    Nuclear p38MAPK localization is necessary for HCF migration. HCFs were seeded on collagen in SSFM at 1×10 5 cells/ml in a 24 well dish. The next day cells were scratch-wounded and incubated in ( A , F , K ) p38MAPK inhibitor, 10 μM <t>SB202190,</t> ( B , G , L ) DMSO, ( C , H , M ) TGFβ1 antibody, ( D , I , N ) Control IgG, or ( E , J , O ) TGFβ RI (ALK5) inhibitor 10 μM SB431542. After 4 h cells were fixed and immunostained for p38MAPK ( A - E ) or SMAD 2/3 ( F - J ). Arrows denote the nuclei of leading edge cells in which p38MAPK and SMAD 2/3 were either localized or excluded (Bar=50 μm) or after 18 h cells were imaged ( K - O ). Bar=200 μm. DMSO is the control for addition of SB202190 or SB431542. Quantification of all data are shown in the bar graphs below the images. Left to right: Exclusion of p38MAPK from the nucleus in leading edge cells, exclusion of SMAD 2/3 from the nucleus in leading edge cells, cell migration into the wound. Nuclear localization was counted using Image J software. Two non-biased people scored cell migration, 0 (less migration) to 5 (most migration). **p-value
    Sb202190, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nuclear p38MAPK localization is necessary for HCF migration. HCFs were seeded on collagen in SSFM at 1×10 5 cells/ml in a 24 well dish. The next day cells were scratch-wounded and incubated in ( A , F , K ) p38MAPK inhibitor, 10 μM SB202190, ( B , G , L ) DMSO, ( C , H , M ) TGFβ1 antibody, ( D , I , N ) Control IgG, or ( E , J , O ) TGFβ RI (ALK5) inhibitor 10 μM SB431542. After 4 h cells were fixed and immunostained for p38MAPK ( A - E ) or SMAD 2/3 ( F - J ). Arrows denote the nuclei of leading edge cells in which p38MAPK and SMAD 2/3 were either localized or excluded (Bar=50 μm) or after 18 h cells were imaged ( K - O ). Bar=200 μm. DMSO is the control for addition of SB202190 or SB431542. Quantification of all data are shown in the bar graphs below the images. Left to right: Exclusion of p38MAPK from the nucleus in leading edge cells, exclusion of SMAD 2/3 from the nucleus in leading edge cells, cell migration into the wound. Nuclear localization was counted using Image J software. Two non-biased people scored cell migration, 0 (less migration) to 5 (most migration). **p-value

    Journal: Molecular Vision

    Article Title: Concentration-dependent effects of transforming growth factor ?1 on corneal wound healing

    doi:

    Figure Lengend Snippet: Nuclear p38MAPK localization is necessary for HCF migration. HCFs were seeded on collagen in SSFM at 1×10 5 cells/ml in a 24 well dish. The next day cells were scratch-wounded and incubated in ( A , F , K ) p38MAPK inhibitor, 10 μM SB202190, ( B , G , L ) DMSO, ( C , H , M ) TGFβ1 antibody, ( D , I , N ) Control IgG, or ( E , J , O ) TGFβ RI (ALK5) inhibitor 10 μM SB431542. After 4 h cells were fixed and immunostained for p38MAPK ( A - E ) or SMAD 2/3 ( F - J ). Arrows denote the nuclei of leading edge cells in which p38MAPK and SMAD 2/3 were either localized or excluded (Bar=50 μm) or after 18 h cells were imaged ( K - O ). Bar=200 μm. DMSO is the control for addition of SB202190 or SB431542. Quantification of all data are shown in the bar graphs below the images. Left to right: Exclusion of p38MAPK from the nucleus in leading edge cells, exclusion of SMAD 2/3 from the nucleus in leading edge cells, cell migration into the wound. Nuclear localization was counted using Image J software. Two non-biased people scored cell migration, 0 (less migration) to 5 (most migration). **p-value

    Article Snippet: TGFβRI inhibitor, SB431542 and p38MAPK inhibitor, SB202190, was from Tocris Bioscience (Ellisville, MO).

    Techniques: Migration, Incubation, Software

    The comparison of the maximum responses of opioid ligands between the buffer- and inhibitor-pretreated HEK-MOR cells. (a) U0126; (b) SB202190; (c) SP100625 and (d) LY294002. The broken circle referred to ICI199441, Leu 5 -enkephalin, DSLET, DAMME, and dynorphin A 1-13 from left to right, respectively.

    Journal: PLoS ONE

    Article Title: Ligand-Directed Functional Selectivity at the Mu Opioid Receptor Revealed by Label-Free Integrative Pharmacology On-Target

    doi: 10.1371/journal.pone.0025643

    Figure Lengend Snippet: The comparison of the maximum responses of opioid ligands between the buffer- and inhibitor-pretreated HEK-MOR cells. (a) U0126; (b) SB202190; (c) SP100625 and (d) LY294002. The broken circle referred to ICI199441, Leu 5 -enkephalin, DSLET, DAMME, and dynorphin A 1-13 from left to right, respectively.

    Article Snippet: DAMGO, DPDPE, BRL-53527, CTOP, naltrindole hydrochloride, norbinaltorphimine, U0126, SB202190, SP600125, and LY294002 were purchased from Tocris Biosciences (Ellisville, MO).

    Techniques:

    The comparison of the real responses (30 min post-stimulation) of opioid ligands between the buffer- and inhibitor-pretreated HEK-MOR cells. (a) U0126; (b) SB202190; (c) SP100625 and (d) LY294002.

    Journal: PLoS ONE

    Article Title: Ligand-Directed Functional Selectivity at the Mu Opioid Receptor Revealed by Label-Free Integrative Pharmacology On-Target

    doi: 10.1371/journal.pone.0025643

    Figure Lengend Snippet: The comparison of the real responses (30 min post-stimulation) of opioid ligands between the buffer- and inhibitor-pretreated HEK-MOR cells. (a) U0126; (b) SB202190; (c) SP100625 and (d) LY294002.

    Article Snippet: DAMGO, DPDPE, BRL-53527, CTOP, naltrindole hydrochloride, norbinaltorphimine, U0126, SB202190, SP600125, and LY294002 were purchased from Tocris Biosciences (Ellisville, MO).

    Techniques:

    Inhibition of p38 MAPK reverses the effects of ACEA on mitochondrial biogenesis in mouse white adipocytes. A : mRNA levels of PGC-1α, NRF-1, and Tfam. B : mtDNA amount. C : Citrate synthase in white adipocytes treated with ACEA for 16 h in the presence or absence of 10 μmol/l SB203580 or SB202190 ( n = 5 experiments; ** P

    Journal: Diabetes

    Article Title: Cannabinoid Receptor Stimulation Impairs Mitochondrial Biogenesis in Mouse White Adipose Tissue, Muscle, and Liver

    doi: 10.2337/db09-1881

    Figure Lengend Snippet: Inhibition of p38 MAPK reverses the effects of ACEA on mitochondrial biogenesis in mouse white adipocytes. A : mRNA levels of PGC-1α, NRF-1, and Tfam. B : mtDNA amount. C : Citrate synthase in white adipocytes treated with ACEA for 16 h in the presence or absence of 10 μmol/l SB203580 or SB202190 ( n = 5 experiments; ** P

    Article Snippet: SB203580 and SB202190 were obtained from Tocris Bioscience (Bristol, U.K.).

    Techniques: Inhibition, Pyrolysis Gas Chromatography

    Loss of p38 MAPK function decreases TGF-β1-induced expression of mitochondrial biogenesis and glycolysis markers. A , IMR-90 cells were transfected with pcDNA3.1 or a vector encoding a p38 MAPK mutant (inactive p38 MAPK). 24 h after transfection,

    Journal: The Journal of Biological Chemistry

    Article Title: Metabolic Reprogramming Is Required for Myofibroblast Contractility and Differentiation *

    doi: 10.1074/jbc.M115.646984

    Figure Lengend Snippet: Loss of p38 MAPK function decreases TGF-β1-induced expression of mitochondrial biogenesis and glycolysis markers. A , IMR-90 cells were transfected with pcDNA3.1 or a vector encoding a p38 MAPK mutant (inactive p38 MAPK). 24 h after transfection,

    Article Snippet: Porcine platelet-derived TGF-β1 was purchased from R & D Systems (Minneapolis, MN), protease inhibitor mixture set III was from EMD Chemicals (San Diego, CA), p38 MAPK inhibitor SB202190 was from Tocris Bioscience (Minneapolis, MN), and MitoTracker® was from Life Technologies.

    Techniques: Expressing, Transfection, Plasmid Preparation, Mutagenesis

    TGF-β1 stimulates metabolic reprogramming via a p38 MAPK pathway. A , IMR-90 cells were treated without or with TGF-β1 (2.5 ng/ml) in the absence or presence of the p38 MAPK inhibitor SB202190 (5 μ m ) for 48 h at 37 °C. SB202190

    Journal: The Journal of Biological Chemistry

    Article Title: Metabolic Reprogramming Is Required for Myofibroblast Contractility and Differentiation *

    doi: 10.1074/jbc.M115.646984

    Figure Lengend Snippet: TGF-β1 stimulates metabolic reprogramming via a p38 MAPK pathway. A , IMR-90 cells were treated without or with TGF-β1 (2.5 ng/ml) in the absence or presence of the p38 MAPK inhibitor SB202190 (5 μ m ) for 48 h at 37 °C. SB202190

    Article Snippet: Porcine platelet-derived TGF-β1 was purchased from R & D Systems (Minneapolis, MN), protease inhibitor mixture set III was from EMD Chemicals (San Diego, CA), p38 MAPK inhibitor SB202190 was from Tocris Bioscience (Minneapolis, MN), and MitoTracker® was from Life Technologies.

    Techniques: