p p 38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p 38 mapk
    P P 38 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 p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p p38 mapk
    Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, <t>p38</t> <t>MAPK,</t> ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01
    Anti P 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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    1) Product Images from "Chemotherapy-initiated cysteine-rich protein 61 decreases acute B-lymphoblastic leukemia chemosensitivity"

    Article Title: Chemotherapy-initiated cysteine-rich protein 61 decreases acute B-lymphoblastic leukemia chemosensitivity

    Journal: Journal of Cancer Research and Clinical Oncology

    doi: 10.1007/s00432-024-05692-8

    Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, p38 MAPK, ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01
    Figure Legend Snippet: Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, p38 MAPK, ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01

    Techniques Used: Western Blot, Real-time Polymerase Chain Reaction

    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    P 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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    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    P 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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    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total <t>p38</t> proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    P 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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    1) Product Images from "Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions"

    Article Title: Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkae006

    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    Figure Legend Snippet: Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).

    Techniques Used: Activation Assay, Inhibition, CRISPR, Cell Culture, Western Blot, Molecular Weight

    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    Protein expression of markers of the <t>MAPK</t> signaling pathway. Protein expression of <t>p-p38</t> MAPK (A), p-ERK(B), and p-JNK (C) was detected with a high-content imaging analysis system. Top: representative images, bar size: 50 μm. *, P < 0.05; **, P < 0.01.
    P 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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    1) Product Images from "Identification of Active Components for Sports Supplements: Machine Learning-Driven Classification and Cell-Based Validation"

    Article Title: Identification of Active Components for Sports Supplements: Machine Learning-Driven Classification and Cell-Based Validation

    Journal: ACS Omega

    doi: 10.1021/acsomega.3c07395

    Protein expression of markers of the MAPK signaling pathway. Protein expression of p-p38 MAPK (A), p-ERK(B), and p-JNK (C) was detected with a high-content imaging analysis system. Top: representative images, bar size: 50 μm. *, P < 0.05; **, P < 0.01.
    Figure Legend Snippet: Protein expression of markers of the MAPK signaling pathway. Protein expression of p-p38 MAPK (A), p-ERK(B), and p-JNK (C) was detected with a high-content imaging analysis system. Top: representative images, bar size: 50 μm. *, P < 0.05; **, P < 0.01.

    Techniques Used: Expressing, Imaging

    anti p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p p38 mapk
    Anti P 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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    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    P 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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    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    Inhibition of the <t>p38</t> <t>MAPK</t> pathway reverses NE-mediated astrocyte cytotoxic edema: ( A ) The expression of <t>p38</t> <t>MAPK</t> pathway activation marker p-p38 MAPK was detected with Western blot in stressed rat BLA. ( B ) Results are expressed as a grayscale ratio of p-p38 MAPK/β-tubulin ( n = 5 per group). Astrocytes were pre-incubated with 10 μM NE for 1 h, stimulated with 3 µM SB203580 for 1 h, or provided combined treatment. ( C , D ) The protein levels of p-p38 MAPK and β-tubulin were detected with Western blot. Quantification of band intensity was performed for each Western blot ( n = 5 per group). ( E ) Representative immunofluorescence images of AQP4 (red) and GFAP (green) in the cultured astrocytes. Scale bar: 20 µm. ( F ) The mean fluorescence intensity of AQP4 per section was quantified ( n = 5 per group). ( G ) Representative original images of rat astrocytes. Scale bar: 100 µm. ( H ) Changes in area of cultured astrocytes ( n = 30 per group). Data presented as mean ± SEM. ns, no significance. * p < 0.05 and *** p < 0.001 versus control group; # p < 0.05, ## p < 0.01, and ### p < 0.001 versus stress group and NE group. p38 <t>MAPK:</t> <t>p38</t> mitogen-activated protein kinase.
    P 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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    1) Product Images from "Norepinephrine-Activated p38 MAPK Pathway Mediates Stress-Induced Cytotoxic Edema of Basolateral Amygdala Astrocytes"

    Article Title: Norepinephrine-Activated p38 MAPK Pathway Mediates Stress-Induced Cytotoxic Edema of Basolateral Amygdala Astrocytes

    Journal: Brain Sciences

    doi: 10.3390/brainsci14020161

    Inhibition of the p38 MAPK pathway reverses NE-mediated astrocyte cytotoxic edema: ( A ) The expression of p38 MAPK pathway activation marker p-p38 MAPK was detected with Western blot in stressed rat BLA. ( B ) Results are expressed as a grayscale ratio of p-p38 MAPK/β-tubulin ( n = 5 per group). Astrocytes were pre-incubated with 10 μM NE for 1 h, stimulated with 3 µM SB203580 for 1 h, or provided combined treatment. ( C , D ) The protein levels of p-p38 MAPK and β-tubulin were detected with Western blot. Quantification of band intensity was performed for each Western blot ( n = 5 per group). ( E ) Representative immunofluorescence images of AQP4 (red) and GFAP (green) in the cultured astrocytes. Scale bar: 20 µm. ( F ) The mean fluorescence intensity of AQP4 per section was quantified ( n = 5 per group). ( G ) Representative original images of rat astrocytes. Scale bar: 100 µm. ( H ) Changes in area of cultured astrocytes ( n = 30 per group). Data presented as mean ± SEM. ns, no significance. * p < 0.05 and *** p < 0.001 versus control group; # p < 0.05, ## p < 0.01, and ### p < 0.001 versus stress group and NE group. p38 MAPK: p38 mitogen-activated protein kinase.
    Figure Legend Snippet: Inhibition of the p38 MAPK pathway reverses NE-mediated astrocyte cytotoxic edema: ( A ) The expression of p38 MAPK pathway activation marker p-p38 MAPK was detected with Western blot in stressed rat BLA. ( B ) Results are expressed as a grayscale ratio of p-p38 MAPK/β-tubulin ( n = 5 per group). Astrocytes were pre-incubated with 10 μM NE for 1 h, stimulated with 3 µM SB203580 for 1 h, or provided combined treatment. ( C , D ) The protein levels of p-p38 MAPK and β-tubulin were detected with Western blot. Quantification of band intensity was performed for each Western blot ( n = 5 per group). ( E ) Representative immunofluorescence images of AQP4 (red) and GFAP (green) in the cultured astrocytes. Scale bar: 20 µm. ( F ) The mean fluorescence intensity of AQP4 per section was quantified ( n = 5 per group). ( G ) Representative original images of rat astrocytes. Scale bar: 100 µm. ( H ) Changes in area of cultured astrocytes ( n = 30 per group). Data presented as mean ± SEM. ns, no significance. * p < 0.05 and *** p < 0.001 versus control group; # p < 0.05, ## p < 0.01, and ### p < 0.001 versus stress group and NE group. p38 MAPK: p38 mitogen-activated protein kinase.

    Techniques Used: Inhibition, Expressing, Activation Assay, Marker, Western Blot, Incubation, Immunofluorescence, Cell Culture, Fluorescence

    anti p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p p38 mapk
    Anti P 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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    Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, <t>p38</t> <t>MAPK,</t> ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01
    Anti P 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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    Cell Signaling Technology Inc p p38 mapk
    Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, <t>p38</t> <t>MAPK,</t> ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01
    P 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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    Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, p38 MAPK, ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01

    Journal: Journal of Cancer Research and Clinical Oncology

    Article Title: Chemotherapy-initiated cysteine-rich protein 61 decreases acute B-lymphoblastic leukemia chemosensitivity

    doi: 10.1007/s00432-024-05692-8

    Figure Lengend Snippet: Nuclear factor kappa B (NF-κB) signaling pathway involved in daunorubicin (DNR)-induced Cyr61 production in B cell acute lymphoblastic leukemia (B-ALL) cells. a Nalm-6 cells were treated with DNR for 10 min and 30 min, and the PI3K/AKT, p38 MAPK, ERK (p44/p42), and NF-κB pathway phosphorylation detected using western blotting. b Nalm-6 and Reh cells were treated with DNR with or without 40μΜ pyrrolidine dithiocarbamate (PDTC) for 24 h. The Cyr61 mRNA levels were detected using real‐time polymerase chain reaction (PCR). c Nalm-6 and Reh cells were treated with DNR with or without 40 μΜ PDTC for 24 h, and the Cyr61 protein levels detected using western blotting. The band intensity of Cyr61 was quantified by densitometry and normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Data represented the mean ± standard error of the mean (SEM) of at least three independent experiments. * P < 0.05, ** P < 0.01

    Article Snippet: The following antibodies were used: anti-human cyr61 monoclonal antibody (093G9) was kindly provided by Dr. Ningli Li (Shanghai Jiao Tong University School of Medicine, Shanghai, China) (Lin et al. , ; Zhang et al. ; Zhong et al. ), anti‐NF‐κBp65 (4764; Cell Signaling Technology, Danvers, MA, USA), anti-P-NF‐κBp65 (3033; Cell Signaling Technology, Danvers, MA, USA), anti-Bcl-2 (4233; Cell Signaling Technology, Danvers, MA, USA), anti-PI3K/AKT (9272; Cell Signaling Technology, Danvers, MA, USA), anti-p- PI3K/AKT (9271; Cell Signaling Technology, Danvers, MA, USA), anti-p38 MAPK (9212; Cell Signaling Technology, Danvers, MA, USA), anti-p-p38 MAPK (9211; Cell Signaling Technology, Danvers, MA, USA), anti-ERK (p44/42) (9202; Cell Signaling Technology, Danvers, MA, USA), anti-p-ERK (p44/42) (9201; Cell Signaling Technology, Danvers, MA, USA), anti-p-H2A.X (2577; Cell Signaling Technology, Danvers, MA, USA), anti-ATM (2873; Cell Signaling Technology, Danvers, MA, USA), and anti-p-ATM (p44/42) (5883; Cell Signaling Technology, Danvers, MA, USA).

    Techniques: Western Blot, Real-time Polymerase Chain Reaction