anti phospho p38 mapk t180 y182 rabbit polyclonal  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 mapk t180 y182 rabbit polyclonal
    Anti Phospho P38 Mapk T180 Y182 Rabbit Polyclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk
    Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk
    SMAD3 and <t>p38</t> <t>MAPK</t> inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in <t>phospho-(Thr180/Tyr182)-p38</t> <t>MAPK</t> were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)
    Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho p38 mapk/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho p38 mapk - by Bioz Stars, 2024-02
    86/100 stars

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    1) Product Images from "SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK"

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    Journal: Signal Transduction and Targeted Therapy

    doi: 10.1038/s41392-024-01741-3

    SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)
    Figure Legend Snippet: SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)

    Techniques Used: Expressing, Activity Assay, Activation Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test, Standard Deviation, Binding Assay

    Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain
    Figure Legend Snippet: Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain

    Techniques Used: Binding Assay, Activity Assay, Expressing, Activation Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Inhibition, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Negative Control, Two Tailed Test, Standard Deviation

    Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain
    Figure Legend Snippet: Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain

    Techniques Used: Expressing, Concentration Assay, Activity Assay, Two Tailed Test, Standard Deviation, Binding Assay

    SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain
    Figure Legend Snippet: SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain

    Techniques Used: Protein Binding, Activation Assay, Binding Assay, Infection, Expressing

    pathscan phospho p38 mapk thr180 tyr182 sandwich elisa  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc pathscan phospho p38 mapk thr180 tyr182 sandwich elisa
    SMAD3 and <t>p38</t> <t>MAPK</t> inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases <t>in</t> <t>phospho-(Thr180/Tyr182)-p38</t> MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the <t>p38</t> <t>MAPK</t> inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)
    Pathscan Phospho P38 Mapk Thr180 Tyr182 Sandwich Elisa, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pathscan phospho p38 mapk thr180 tyr182 sandwich elisa/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pathscan phospho p38 mapk thr180 tyr182 sandwich elisa - by Bioz Stars, 2024-02
    86/100 stars

    Images

    1) Product Images from "SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK"

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    Journal: Signal Transduction and Targeted Therapy

    doi: 10.1038/s41392-024-01741-3

    SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)
    Figure Legend Snippet: SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)

    Techniques Used: Expressing, Activity Assay, Activation Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test, Standard Deviation, Binding Assay

    Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain
    Figure Legend Snippet: Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain

    Techniques Used: Binding Assay, Activity Assay, Expressing, Activation Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Inhibition, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Negative Control, Two Tailed Test, Standard Deviation

    Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain
    Figure Legend Snippet: Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain

    Techniques Used: Expressing, Concentration Assay, Activity Assay, Two Tailed Test, Standard Deviation, Binding Assay

    SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain
    Figure Legend Snippet: SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain

    Techniques Used: Protein Binding, Activation Assay, Binding Assay, Infection, Expressing

    anti phospho p38 mapk thr180 tyr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 mapk thr180 tyr182
    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, <t>p38/p-p38,</t> JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    Anti Phospho P38 Mapk Thr180 Tyr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Aggresome formation promotes ASK1/JNK signaling activation and stemness maintenance in ovarian cancer"

    Article Title: Aggresome formation promotes ASK1/JNK signaling activation and stemness maintenance in ovarian cancer

    Journal: Nature Communications

    doi: 10.1038/s41467-024-45698-x

    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, p38/p-p38, JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    Figure Legend Snippet: a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, p38/p-p38, JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.

    Techniques Used: Expressing, Immunoprecipitation, Co-Immunoprecipitation Assay, Mutagenesis

    phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk
    Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 mapk
    Anti Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    k phospho p38 mapk thr180 tyr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc k phospho p38 mapk thr180 tyr182
    K Phospho P38 Mapk Thr180 Tyr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 mapk thr180 tyr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk thr180 tyr182
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    rabbit anti phospho p38 mapk t180 y182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti phospho p38 mapk t180 y182
    (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the <t>p38</t> pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).
    Rabbit Anti Phospho P38 Mapk T180 Y182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling"

    Article Title: Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling

    Journal: bioRxiv

    doi: 10.1101/2024.02.01.578427

    (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the p38 pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).
    Figure Legend Snippet: (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the p38 pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).

    Techniques Used: Transformation Assay, Incubation, Sequencing, Western Blot

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    Cell Signaling Technology Inc anti phospho p38 mapk t180 y182 rabbit polyclonal
    Anti Phospho P38 Mapk T180 Y182 Rabbit Polyclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SMAD3 and <t>p38</t> <t>MAPK</t> inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases <t>in</t> <t>phospho-(Thr180/Tyr182)-p38</t> MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the <t>p38</t> <t>MAPK</t> inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)
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    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, <t>p38/p-p38,</t> JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    Anti Phospho P38 Mapk Thr180 Tyr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, <t>p38/p-p38,</t> JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    Anti Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, <t>p38/p-p38,</t> JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    K Phospho P38 Mapk Thr180 Tyr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, <t>p38/p-p38,</t> JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.
    Phospho P38 Mapk Thr180 Tyr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti phospho p38 mapk t180 y182
    (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the <t>p38</t> pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).
    Rabbit Anti Phospho P38 Mapk T180 Y182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)

    Journal: Signal Transduction and Targeted Therapy

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    doi: 10.1038/s41392-024-01741-3

    Figure Lengend Snippet: SMAD3 and p38 MAPK inhibitors abrogate the effects of SPRBD. a SIS3, a specific inhibitor of phospho-SMAD3, inhibited the SPRBD- and SPRBD + IFN-β- induced increases in expression of CHST15 and CHST11. b Following silencing of ACE2 by siRNA, the SPRBD- and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 MAPK were inhibited. c The SPRBD- and SPRBD + IFN-β- induced increases in phospho-(S423/S425)-SMAD3 were completely inhibited by SIS3 and, to a lesser extent, by SB, the p38 MAPK inhibitor. d The SPRBD and SPRBD + IFN-β- induced increases in phospho-(Thr180/Tyr182)-p38 were unaffected by exposure to SIS3 and were inhibited by SB. e , f Promoter activity of CHST15 and CHST11 was enhanced by exposure to SPRBD and to a greater extent by the combination of IFN-β and SPRBD. Both SIS3 and SB inhibited promoter activation. g Treatment of cells with the specific phospho-p38α/β inhibitor PH797804 or with p38α siRNA completely blocked the SPRBD-induced increase in phospho-p38 MAPK detected by ELISA. In contrast, TAB1 siRNA and control siRNA had no effect. h The SPRBD-induced increases in expression of CHST15 and of CHST11 were inhibited by p38α siRNA and by PH797804, but not by TAB1 siRNA or control siRNA. All p-values were determined by unpaired t test, two-tailed, with unequal variance, and with at least three independent experiments. Error bars represent one standard deviation. *** represents p ≤ 0.001; **** is for p ≤ 0.0001. ACE angiotensin-converting enzyme, CHST carbohydrate sulfotransferase, NSC NSC23766, SB SB203580, si siRNA, SIS3 specific inhibitor of SMAD3, SMAD Mothers against decapentaplegic homolog 3 (DPC3), SPRBD spike protein receptor-binding domain, TAB1 TGF-beta activated kinase (MAP3K7)

    Article Snippet: Phospho-p38 MAPK was measured in cell samples using a Pathscan® Phospho-p38 MAPK Thr180/Tyr182 Sandwich ELISA (Cell Signaling).

    Techniques: Expressing, Activity Assay, Activation Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test, Standard Deviation, Binding Assay

    Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain

    Journal: Signal Transduction and Targeted Therapy

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    doi: 10.1038/s41392-024-01741-3

    Figure Lengend Snippet: Spike protein receptor binding domain inhibits ARSB activity and expression by activation of phospho-p38 MAPK and phospho-(S249/T252)-RB-E2F1 interaction. a ARSB mRNA expression was unaffected by NSC23766, but following exposure to the p38 MAPK inhibitor SB, mRNA expression was restored to baseline control values. b In contrast, to the observed effects of p38α inhibitors on expression of CHST11 and CHST15, p38α siRNA and PH797804 reversed the SPRBD-induced decline in ARSB expression. TAB1 siRNA had no effect. c SIS3 had no impact on the SPRBD- or SPRBD + IFN-β- induced decline in ARSB expression. d ARSB promoter activation was reduced by SPRBD and by SPRBD + IFN-β. These declines were reversed by exposure to SB, but not by SIS3. e Following treatment with SPRBD or SPRBD + IFN-β, C-terminal phospho-(Ser807/811)-Rb declined as shown by ELISA. These declines were reversed by SB, but not by SIS3. f In contrast to the decline in C-terminal Rb phosphorylation, exposure to SPRBD + IFN-β increased N-terminus phospho-(S249/T252)-Rb, as detected by Western blot and shown in detail in Supplementary Fig. . This increase was inhibited by SB, and total Rb was unchanged. g Densitometry confirms the impression of Western blot and shows the ratio of phospho-(S249)-Rb to total Rb following SPRBD + IFN-β has increased to 3.89 times the baseline. h Following exposure to SPRBD and SPRBD + IFN-β, E2F-DNA binding declined significantly, and SB reversed the declines. i %DNA input declined following SPRBD + IFN-β and increased following inhibition of p38-MAPK by SB. j Agarose gel of chromatin immunoprecipitation (ChIP) indicated no effect of the IgG negative control on E2F1 binding to the ARSB promoter at baseline, increased binding following IFN-β, reduced binding following SPRBD + IFN-β, and reversal of this decline following treatment with SB. P values were determined by unpaired t tests, two-tailed with unequal variance, with n of at least 3 independent experiments. Error bars show one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, IFN interferon, ND no difference, NSC = NSC23766, Rb retinoblastoma protein, SB = SB203580, SIS3 specific inhibitor of Smad3, SPRBD spike protein receptor-binding domain

    Article Snippet: Phospho-p38 MAPK was measured in cell samples using a Pathscan® Phospho-p38 MAPK Thr180/Tyr182 Sandwich ELISA (Cell Signaling).

    Techniques: Binding Assay, Activity Assay, Expressing, Activation Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Inhibition, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Negative Control, Two Tailed Test, Standard Deviation

    Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain

    Journal: Signal Transduction and Targeted Therapy

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    doi: 10.1038/s41392-024-01741-3

    Figure Lengend Snippet: Effects of desloratadine, monensin, and carrageenan on expression of CHST15, CHST11, and ARSB. a Exposure to the antihistamine desloratadine at a concentration of 32 µM for 2 h reduced by 62% the SPRBD-induced increase in phospho-(Thr180/Tyr182)-p38 MAPK in the AEC. b Consistent with the decline in phospho-p38 MAPK, desloratadine reduced the SPRBD- and SPRBD + IFN-β- induced increases in CHST15 ( p = 0.04; p ≤ 0.0003 with IFN-β) and CHST11 expression ( p = 0.0008; p ≤ 0.0009 with IFN-β, n = 6). Declines increased with increasing concentrations of desloratadine from 16 µM to 32 µM to 64 µM, without evidence of cytotoxicity. c Fold-change of ARSB mRNA expression increased significantly and progressively with desloratadine 16–64 µM for 2 h ( p = 0.02, p = 1.35 × 10 −6 , p = 4.3 × 10 −8 with IFN-β; n = 6). d Desloratadine 32 µM for 2 h partially reversed the SPRBD- and SPRBD + IFN-β- induced declines in ARSB activity (from 64.7 to 73.4 nmol/mg protein/h and from 41.0 to 61.8 nmol/mg protein/h with IFN-β; n = 3) ( p = 0.036, p = 0.0042, n = 3). e The polyether antibiotic monensin 1.0 µM for 2 h reduced the SPRBD-induced increases in CHST15 mRNA ( p = 0.005; p ≤ 0.0001 with IFN-β) and CHST11 ( p = 0.002, p ≤ 0.0002 with IFN-β; fold-change compared to control; n = 6). f Monensin had no significant impact on the SPRBD-induced decline in ARSB. g Carrageenan-exposed C57BL/6 J mice had marked increase in phospho-p38 MAPK in lung tissue ( p = 6.0 × 10 −6 , n = 6 per group). h mRNA expression of CHST15 and CHST11 was significantly increased in the lung tissue of the carrageenan-exposed mice ( p < 1 × 10 −5 , n = 6). In contrast, ARSB expression declined significantly ( p = 8.4 × 10 −9 , n = 6). i Consistent with the phospho-38 MAPK-Rb-E2F1-mediated mechanism of regulation of ARSB mRNA expression, the DNA-bound E2F was significantly reduced ( p = 1.2 × 10 −6 , n = 6) in the lung tissue of the carrageenan-exposed mice. All p values were determined using unpaired t tests, two-tailed, with unequal variance, and error bars represent one standard deviation. * represents p ≤ 0.05; ** is for p ≤ 0.01, *** for p ≤ 0.001, and **** for p ≤ 0.0001. ARSB arylsulfatase B = N-acetylgalactosamine-4-sulfatase, CHST carbohydrate sulfotransferase, Des Desloratadine, IFN interferon, Mon Monensin, ND no difference, PAPSS 3’-phosphoadenosine 5’-phosphosulfate synthase, sGAG sulfated glycosaminoglycan, SPRBD spike protein receptor-binding domain

    Article Snippet: Phospho-p38 MAPK was measured in cell samples using a Pathscan® Phospho-p38 MAPK Thr180/Tyr182 Sandwich ELISA (Cell Signaling).

    Techniques: Expressing, Concentration Assay, Activity Assay, Two Tailed Test, Standard Deviation, Binding Assay

    SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain

    Journal: Signal Transduction and Targeted Therapy

    Article Title: SARS-CoV-2 spike protein-ACE2 interaction increases carbohydrate sulfotransferases and reduces N-acetylgalactosamine-4-sulfatase by p38 MAPK

    doi: 10.1038/s41392-024-01741-3

    Figure Lengend Snippet: SARS-CoV-2 spike protein binding with ACE2 initiates transcriptional events which modify chondroitin sulfation through activation of phospho-p38 MAPK. This schematic presents the signaling mechanism by which the SARS-CoV-2 spike protein receptor-binding domain (SPRBD) interacts and initiates the transcriptional events which lead to increased chondroitin sulfate in airway epithelial cells and in Covid-19 infected lung. The activation of phospho-p38 MAPK and phospho-SMAD3 lead to increased expression of CHST15 and CHST11. Phospho-p38 MAPK leads to N-terminal phosphorylation of Rb and enhanced Rb binding with E2F1, which reduces ARSB promoter binding with E2F1 and reduces ARSB expression. Additional effects may arise from ACE2-SPRBD binding, due to reduced availability of ACE2 for other biochemical reactions, including the conversion of AngII to Ang1-7. AngII interaction with the angiotensin II receptor type 1 (AT1R) increases phospho-p38 MAPK, and increased availability of AngII may contribute to the observed downstream effects of p38 MAPK on transcription. The altered balance between AngII-induced vasoconstriction and Ang1-7 vasodilatation, following interaction with the G-protein coupled Mas receptor, may have additional pathophysiological consequences. ACE2 angiotensin-converting enzyme 2, AngII angiotensin II, ARSB arylsulfatase B, AT1R angiotensin II receptor type 1, AT2R angiotensin II receptor type 2, CHST carbohydrate sulfotransferase, Mas Ang1-7 receptor, pRb retinoblastoma protein, SMAD Suppressor of Mothers against Decapentaplegic, SPRBD SARS-CoV-2 spike protein receptor binding domain

    Article Snippet: Phospho-p38 MAPK was measured in cell samples using a Pathscan® Phospho-p38 MAPK Thr180/Tyr182 Sandwich ELISA (Cell Signaling).

    Techniques: Protein Binding, Activation Assay, Binding Assay, Infection, Expressing

    a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, p38/p-p38, JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Aggresome formation promotes ASK1/JNK signaling activation and stemness maintenance in ovarian cancer

    doi: 10.1038/s41467-024-45698-x

    Figure Lengend Snippet: a Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis of the differentially expressed genes between sgRNA-OTUD1 and control cells (sgCtrl). The top 9 enriched pathways were listed. The bubble size indicates changed gene numbers and colors represent false discovery rate ( P ‐value). b The specific effect of OTUD1 on the phosphorylation levels of several key components of the MAPK signaling pathway (ERK/p-ERK, p38/p-p38, JNK/p-JNK) were determined. c The expression of CD24 , FOS and several other reported JNK target genes ( IL6 and ATF2 ), as well as a number of CSCs markers such as OCT4, NANOG and NOTCH1 in SKOV3 control or OTUD1 depleted cells, were analyzed by qPCR ( n = 3). d A dox-inducible EGFP-OTUD1 expression system was established to evaluate the effects of OTUD1 on protein levels of JNK signal pathway key components (ASK1/p-ASK1, JNK/p-JNK). Dox doxorubicin. e Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT and HA-ASK1 in 293T cells. f Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 WT or Flag-OTUD1 C320A mutant and HA-ASK1 in 293T cells. C320A, OTUD1-C320A. g Schematic illustration of OTUD1 domain. OTU ovarian tumor protease, UIM ubiquitin-interacting motif, IDR intrinsically disordered protein region. h Co-immunoprecipitation (Co-IP) was performed with Flag-OTUD1 (aa 1–286 or aa 287–481 truncation) and HA-ASK1 in 293T cells. P values are calculated using one-way ANOVA ( c ). Representative of n = 3 independent experiments ( b , d – f , h ). Source data are provided as a Source Data file.

    Article Snippet: Anti-phospho-p44/42 MAPK (Erk1/2) Thr202/Tyr204) (#9101, 1:1000), anti-phospho- p38 MAPK (Thr180/Tyr182) (#9211, 1:1000), anti-SAPK/JNK (Phospho-Thr183/Tyr185) (81E11) (#4668, 1:1000), anti-c-Jun (Phospho-Ser73) (D47G9), (#3270, 1:1000), and anti-c-Jun (#9165, 1:1000) were purchased from Cell Signaling Technology.

    Techniques: Expressing, Immunoprecipitation, Co-Immunoprecipitation Assay, Mutagenesis

    (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the p38 pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).

    Journal: bioRxiv

    Article Title: Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling

    doi: 10.1101/2024.02.01.578427

    Figure Lengend Snippet: (A) Scheme to filter peptides showing up-regulation by inhibitor treatment and summary of the numbers of the up-regulated phosphosites for each inhibitor (B) PCA of the log2-transformed abundance of phosphosites up-regulated by both 8 and 20 min of EGF incubation. (C) STRING-based protein network of proteins showing sanguinarine-dependent up-regulation of its phosphorylation. Proteins with at least one connection with other proteins are included. (D) Illustration of the p38 pathway activated by EGFR. The figure was created using BioRender.com. (E) Sequence motif enrichment analysis of 15 residues surrounding the regulated phosphosites. (F) Heatmap showing the log2-transformed phosphosite abundance changes induced by inhibitor treatment. See also for the heatmap containing all 80 peptides. (G) Western blotting analysis using the cell lysates of Hela cells pre-treated with the inhibitors (500 nM) for 15 min followed by 20 min incubation with EGF (20 nM).

    Article Snippet: Primary antibodies used were rabbit anti-EGFR (ab32198; Abcam), rabbit anti-phospho-EGFR (pY1045) (#2237; Cell Signaling Technology), mouse anti-phospho-EGFR (pY1068) (#2236; Cell Signaling Technology), rabbit anti-Erk1/2 (#4695; Cell Signaling Technology), mouse anti-phospho-Erk1/2 (T202/Y204) (#9106; Cell Signaling Technology), rabbit anti-Akt (#9272; Cell Signaling Technology) rabbit anti-phospho-Akt (S473) (#9271; Cell Signaling Technology), rabbit anti-p38 MAPK (#9212; Cell Signaling Technology), rabbit anti-phospho p38 MAPK (T180/Y182) (#9211; Cell Signaling Technology) and mouse anti-GAPDH (Abcam).

    Techniques: Transformation Assay, Incubation, Sequencing, Western Blot