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p p53 ser 15  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p53 ser 15
    A , B HUH7 and C , D Hep3B cells were transfected with an empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) for 24 h and then treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. Western blot analysis of γH2AX levels was performed. E Western blot analysis of <t>Ac-p53</t> <t>Lys-382,</t> <t>p-p53</t> <t>Ser-15</t> and p53 levels was performed in HepG2 cells after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. F Densitometric ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. G – I HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing (ATGL-OE) construct and, after 24 h, treated with 50 µM etoposide for 6 h with or without 10 µM C646 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed. H Densitometric analysis ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 6 h. J – L HepG2 cells were treated with 50 µM etoposide for 6 h with or without 1 µM GW7647 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. K Densitometric analysis of ratio between Ac-p53 and p-p53 expression after treatment with 50 µM etoposide for 6 h. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by Student t test and one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.
    P P53 Ser 15, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 491 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 491 article reviews
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    Images

    1) Product Images from "ATGL sensitizes hepatocellular carcinoma cells to genotoxic drugs by modulating p53 acetylation/phosphorylation status"

    Article Title: ATGL sensitizes hepatocellular carcinoma cells to genotoxic drugs by modulating p53 acetylation/phosphorylation status

    Journal: Cell Death Discovery

    doi: 10.1038/s41420-026-03048-4

    A , B HUH7 and C , D Hep3B cells were transfected with an empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) for 24 h and then treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. Western blot analysis of γH2AX levels was performed. E Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed in HepG2 cells after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. F Densitometric ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. G – I HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing (ATGL-OE) construct and, after 24 h, treated with 50 µM etoposide for 6 h with or without 10 µM C646 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed. H Densitometric analysis ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 6 h. J – L HepG2 cells were treated with 50 µM etoposide for 6 h with or without 1 µM GW7647 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. K Densitometric analysis of ratio between Ac-p53 and p-p53 expression after treatment with 50 µM etoposide for 6 h. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by Student t test and one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.
    Figure Legend Snippet: A , B HUH7 and C , D Hep3B cells were transfected with an empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) for 24 h and then treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. Western blot analysis of γH2AX levels was performed. E Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed in HepG2 cells after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. F Densitometric ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. G – I HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing (ATGL-OE) construct and, after 24 h, treated with 50 µM etoposide for 6 h with or without 10 µM C646 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed. H Densitometric analysis ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 6 h. J – L HepG2 cells were treated with 50 µM etoposide for 6 h with or without 1 µM GW7647 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. K Densitometric analysis of ratio between Ac-p53 and p-p53 expression after treatment with 50 µM etoposide for 6 h. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by Student t test and one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.

    Techniques Used: Transfection, Plasmid Preparation, Construct, Western Blot, Expressing

    A – D HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide for 6 h with or without recovery (Rec) with fresh medium for 2 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. E , F HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. The proliferation was assayed via the Trypan blue direct counting procedure. G , H HepG2 cells were treated with 50 µM etoposide for 6 h with or without 25 µM ATGListatin (ATGLi) for 24 h. HepG2 cells were treated with 50 µM etoposide for 6 h. I – K Western blot analysis of p21 and Puma levels was performed. HepG2 cells were treated with 1 µM GW7647 for 24 h. L , M Proliferation was assayed by the Trypan blue direct counting procedure. N – P Western blot analysis of p21 and Puma levels was performed. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.
    Figure Legend Snippet: A – D HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide for 6 h with or without recovery (Rec) with fresh medium for 2 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. E , F HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. The proliferation was assayed via the Trypan blue direct counting procedure. G , H HepG2 cells were treated with 50 µM etoposide for 6 h with or without 25 µM ATGListatin (ATGLi) for 24 h. HepG2 cells were treated with 50 µM etoposide for 6 h. I – K Western blot analysis of p21 and Puma levels was performed. HepG2 cells were treated with 1 µM GW7647 for 24 h. L , M Proliferation was assayed by the Trypan blue direct counting procedure. N – P Western blot analysis of p21 and Puma levels was performed. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.

    Techniques Used: Transfection, Plasmid Preparation, Construct, Western Blot

    A Boxplot showing significantly reduced PNPLA2 expression in primary HCC tissues (primary tumor; n = 371) compared with solid tumor-adjacent non-tumoral liver tissues (solid tissue normal; n = 50) samples based on TCGA data. B Boxplot of Z-score–normalized ATGL expression from TCGA-LIHC RNA-seq data based on TP53 mutation status (wild type n = 263 and mutant n = 111). C Visualization of the PPAR signaling pathway, reporting normalized enrichment score (NES) and adjusted p -value. D Bar plot showing the most significantly enriched transcription factors after a transcription factor enrichment analysis performed using TRRUST transcription factors 2019 database on differentially expressed genes (DEGs) in ATGL-high versus ATGL-low HCC samples. Adjusted p -value was reported. Scatter plot showing the correlation between E PNPLA2 and PPARα ( PPARA ); between F PNPLA2 and EP300 ; between G PPARA and EP300 ; between H PNPLA2 and Puma ( BBC3 ); between I PNPLA2 and p21 ( CDKN1A ) mRNA expression levels in HCC samples from the TCGA-LIHC cohort analyzed using GEPIA. Gene expression values are reported as log2-transformed TPM. Each dot represents an individual tumor sample.
    Figure Legend Snippet: A Boxplot showing significantly reduced PNPLA2 expression in primary HCC tissues (primary tumor; n = 371) compared with solid tumor-adjacent non-tumoral liver tissues (solid tissue normal; n = 50) samples based on TCGA data. B Boxplot of Z-score–normalized ATGL expression from TCGA-LIHC RNA-seq data based on TP53 mutation status (wild type n = 263 and mutant n = 111). C Visualization of the PPAR signaling pathway, reporting normalized enrichment score (NES) and adjusted p -value. D Bar plot showing the most significantly enriched transcription factors after a transcription factor enrichment analysis performed using TRRUST transcription factors 2019 database on differentially expressed genes (DEGs) in ATGL-high versus ATGL-low HCC samples. Adjusted p -value was reported. Scatter plot showing the correlation between E PNPLA2 and PPARα ( PPARA ); between F PNPLA2 and EP300 ; between G PPARA and EP300 ; between H PNPLA2 and Puma ( BBC3 ); between I PNPLA2 and p21 ( CDKN1A ) mRNA expression levels in HCC samples from the TCGA-LIHC cohort analyzed using GEPIA. Gene expression values are reported as log2-transformed TPM. Each dot represents an individual tumor sample.

    Techniques Used: Expressing, RNA Sequencing, Mutagenesis, Gene Expression, Transformation Assay

    Related Articles

    Western Blot:

    Article Title: An African-specific polymorphism in the TP53 gene impairs p53 tumor suppressor function in a mouse model
    Article Snippet: .. Primary antibodies used for Western blotting included p53 (ab6) (Calbiochem, OP43), p53 Ser-46-P (Abcam, ab122898), p53 Ser-15-P (Cell Signaling, 9284), MDM2 (ab1 and ab2) (Calbiochem, OP46T and OP115), p21 (ab6) (Calbiochem, OP79), cleaved lamin A (Cell Signaling, 2035), cleaved caspase-3 (Cell Signaling, 9061), GAPDH (14C10) (Cell Signaling, 2118), GPX4 (Abcam, 125066), and GLS2 (Abcam, ab113509). ..

    Ubiquitin Proteomics:

    Article Title: Identification of TRIML2, a Novel p53 Target, that Enhances p53-SUMOylation and Regulates the Transactivation of Pro-apoptotic Genes
    Article Snippet: Western blot analysis and Immunoprecipitation For western blot analysis, 25-50 μg of protein was resolved over sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using pre-cast NuPAGE® Bis-Tris gels (Life Technologies) and transferred onto PVDF membranes (Bio-Rad). .. Primary antibodies used in this study include p53 (Ab6, Calbiochem, OP43), p53 Ser-15-P (Cell Signaling, 9284), p53 Ser-46-P (Cell Signaling, 2521), TRIML2 (Sigma, HPA043838), TRIML2 (Abcam, ab87292), FLAG-Tag (M2, Sigma, F3165), GAPDH (14C10, Cell Signaling, 2118), Actin (AC-15, Sigma, A5441), p21 (Ab6, Calbiochem, OP79), MDM2 (Ab1-OP46, Ab2-OP115, Calbiochem), Cleaved lamin A (Cell Signaling, 2035), Cleaved caspase 3 (Cell Signaling, 9061), PIDD (Anto-1, Novus Biologicals, NBP1-97595), Caspase 2 (Cell Signaling, 2224), PIG3 (Ab1, Oncogene, PC268), PML (Santa Cruz, sc-5621), PARP (46D11, Cell Signaling, 9532), SUMO2/3 (Cell Signaling, 4971), SUMO1 (Cell Signaling, 4930), Ubiquitin (Cell Signaling, 3933). ..



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    Journal: Cell Death Discovery

    Article Title: ATGL sensitizes hepatocellular carcinoma cells to genotoxic drugs by modulating p53 acetylation/phosphorylation status

    doi: 10.1038/s41420-026-03048-4

    Figure Lengend Snippet: A , B HUH7 and C , D Hep3B cells were transfected with an empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) for 24 h and then treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. Western blot analysis of γH2AX levels was performed. E Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed in HepG2 cells after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. F Densitometric ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 2, 4, 6 and 24 h. G – I HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing (ATGL-OE) construct and, after 24 h, treated with 50 µM etoposide for 6 h with or without 10 µM C646 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15 and p53 levels was performed. H Densitometric analysis ratios of Ac-p53 and p-p53 after treatment with 50 µM etoposide for 6 h. J – L HepG2 cells were treated with 50 µM etoposide for 6 h with or without 1 µM GW7647 for 24 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. K Densitometric analysis of ratio between Ac-p53 and p-p53 expression after treatment with 50 µM etoposide for 6 h. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by Student t test and one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.

    Article Snippet: The following primary antibodies were used: β-Actin (Cell Signaling Technology, cat. number #4970S, diluted 1:1000), γH2AX Ser-139 (Cell Signaling Technology, cat. number #9718, diluted 1:1000), ATGL (Cell Signaling Technology, cat. number 2138S, diluted 1:1000), pATM Ser-1981 (Cell Signaling Technology, cat. number #5883, diluted 1:1000), ATM (Cell Signaling Technology, cat. number #2873, diluted 1:1000), p21 (Cell Signaling Technology, cat. number #2947, diluted 1:1000), PPARα (Santa Cruz Biotechnology, cat. number sc-398394, diluted 1:1000), Puma (Cell Signaling Technology, cat. number #4976, diluted 1:1000), Ac-p53 Lys-382 (Cell Signaling Technology, cat. number #2525S, diluted 1:1000), p-p53 Ser-15 (Cell Signaling Technology, cat. number #9284S, diluted 1:1000), and p53 (Sigma-Aldrich, cat. number #P5813, diluted 1:1000).

    Techniques: Transfection, Plasmid Preparation, Construct, Western Blot, Expressing

    A – D HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide for 6 h with or without recovery (Rec) with fresh medium for 2 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. E , F HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. The proliferation was assayed via the Trypan blue direct counting procedure. G , H HepG2 cells were treated with 50 µM etoposide for 6 h with or without 25 µM ATGListatin (ATGLi) for 24 h. HepG2 cells were treated with 50 µM etoposide for 6 h. I – K Western blot analysis of p21 and Puma levels was performed. HepG2 cells were treated with 1 µM GW7647 for 24 h. L , M Proliferation was assayed by the Trypan blue direct counting procedure. N – P Western blot analysis of p21 and Puma levels was performed. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.

    Journal: Cell Death Discovery

    Article Title: ATGL sensitizes hepatocellular carcinoma cells to genotoxic drugs by modulating p53 acetylation/phosphorylation status

    doi: 10.1038/s41420-026-03048-4

    Figure Lengend Snippet: A – D HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide for 6 h with or without recovery (Rec) with fresh medium for 2 h. Western blot analysis of Ac-p53 Lys-382, p-p53 Ser-15, p53 and γH2AX levels was performed. E , F HepG2 cells were transfected with empty vector (Vehicle) or ATGL-overexpressing construct (ATGL-OE) and, after 24 h, treated with 50 µM etoposide or 2 µM doxorubicin for 6 h. The proliferation was assayed via the Trypan blue direct counting procedure. G , H HepG2 cells were treated with 50 µM etoposide for 6 h with or without 25 µM ATGListatin (ATGLi) for 24 h. HepG2 cells were treated with 50 µM etoposide for 6 h. I – K Western blot analysis of p21 and Puma levels was performed. HepG2 cells were treated with 1 µM GW7647 for 24 h. L , M Proliferation was assayed by the Trypan blue direct counting procedure. N – P Western blot analysis of p21 and Puma levels was performed. The images are representative of three independent experiments that yielded similar results. β-Actin and ATGL were used as loading and transfection controls, respectively. The data are presented as the means ± SDs from three independent experiments. Statistical significance was determined by one-way ANOVA with Tukey’s post hoc test; * p < 0.05, ** p < 0.01, *** p < 0.001 vs CTRL or as indicated by brackets.

    Article Snippet: The following primary antibodies were used: β-Actin (Cell Signaling Technology, cat. number #4970S, diluted 1:1000), γH2AX Ser-139 (Cell Signaling Technology, cat. number #9718, diluted 1:1000), ATGL (Cell Signaling Technology, cat. number 2138S, diluted 1:1000), pATM Ser-1981 (Cell Signaling Technology, cat. number #5883, diluted 1:1000), ATM (Cell Signaling Technology, cat. number #2873, diluted 1:1000), p21 (Cell Signaling Technology, cat. number #2947, diluted 1:1000), PPARα (Santa Cruz Biotechnology, cat. number sc-398394, diluted 1:1000), Puma (Cell Signaling Technology, cat. number #4976, diluted 1:1000), Ac-p53 Lys-382 (Cell Signaling Technology, cat. number #2525S, diluted 1:1000), p-p53 Ser-15 (Cell Signaling Technology, cat. number #9284S, diluted 1:1000), and p53 (Sigma-Aldrich, cat. number #P5813, diluted 1:1000).

    Techniques: Transfection, Plasmid Preparation, Construct, Western Blot

    A Boxplot showing significantly reduced PNPLA2 expression in primary HCC tissues (primary tumor; n = 371) compared with solid tumor-adjacent non-tumoral liver tissues (solid tissue normal; n = 50) samples based on TCGA data. B Boxplot of Z-score–normalized ATGL expression from TCGA-LIHC RNA-seq data based on TP53 mutation status (wild type n = 263 and mutant n = 111). C Visualization of the PPAR signaling pathway, reporting normalized enrichment score (NES) and adjusted p -value. D Bar plot showing the most significantly enriched transcription factors after a transcription factor enrichment analysis performed using TRRUST transcription factors 2019 database on differentially expressed genes (DEGs) in ATGL-high versus ATGL-low HCC samples. Adjusted p -value was reported. Scatter plot showing the correlation between E PNPLA2 and PPARα ( PPARA ); between F PNPLA2 and EP300 ; between G PPARA and EP300 ; between H PNPLA2 and Puma ( BBC3 ); between I PNPLA2 and p21 ( CDKN1A ) mRNA expression levels in HCC samples from the TCGA-LIHC cohort analyzed using GEPIA. Gene expression values are reported as log2-transformed TPM. Each dot represents an individual tumor sample.

    Journal: Cell Death Discovery

    Article Title: ATGL sensitizes hepatocellular carcinoma cells to genotoxic drugs by modulating p53 acetylation/phosphorylation status

    doi: 10.1038/s41420-026-03048-4

    Figure Lengend Snippet: A Boxplot showing significantly reduced PNPLA2 expression in primary HCC tissues (primary tumor; n = 371) compared with solid tumor-adjacent non-tumoral liver tissues (solid tissue normal; n = 50) samples based on TCGA data. B Boxplot of Z-score–normalized ATGL expression from TCGA-LIHC RNA-seq data based on TP53 mutation status (wild type n = 263 and mutant n = 111). C Visualization of the PPAR signaling pathway, reporting normalized enrichment score (NES) and adjusted p -value. D Bar plot showing the most significantly enriched transcription factors after a transcription factor enrichment analysis performed using TRRUST transcription factors 2019 database on differentially expressed genes (DEGs) in ATGL-high versus ATGL-low HCC samples. Adjusted p -value was reported. Scatter plot showing the correlation between E PNPLA2 and PPARα ( PPARA ); between F PNPLA2 and EP300 ; between G PPARA and EP300 ; between H PNPLA2 and Puma ( BBC3 ); between I PNPLA2 and p21 ( CDKN1A ) mRNA expression levels in HCC samples from the TCGA-LIHC cohort analyzed using GEPIA. Gene expression values are reported as log2-transformed TPM. Each dot represents an individual tumor sample.

    Article Snippet: The following primary antibodies were used: β-Actin (Cell Signaling Technology, cat. number #4970S, diluted 1:1000), γH2AX Ser-139 (Cell Signaling Technology, cat. number #9718, diluted 1:1000), ATGL (Cell Signaling Technology, cat. number 2138S, diluted 1:1000), pATM Ser-1981 (Cell Signaling Technology, cat. number #5883, diluted 1:1000), ATM (Cell Signaling Technology, cat. number #2873, diluted 1:1000), p21 (Cell Signaling Technology, cat. number #2947, diluted 1:1000), PPARα (Santa Cruz Biotechnology, cat. number sc-398394, diluted 1:1000), Puma (Cell Signaling Technology, cat. number #4976, diluted 1:1000), Ac-p53 Lys-382 (Cell Signaling Technology, cat. number #2525S, diluted 1:1000), p-p53 Ser-15 (Cell Signaling Technology, cat. number #9284S, diluted 1:1000), and p53 (Sigma-Aldrich, cat. number #P5813, diluted 1:1000).

    Techniques: Expressing, RNA Sequencing, Mutagenesis, Gene Expression, Transformation Assay

    CompC increased the phosphorylation of Cdk1 on Tyr 15 and Wee1 on Ser 642 . ( a ) Renca cells were cultured for one day and then serum-starved by incubation with SFM overnight. The cells were treated with SFM (C) or 10% FBS for the indicated times (8–24 h) in the absence (−) or presence (+) of 10 μM CompC. Cell lysates were analyzed by western blot using antibodies against phosphorylated Cdk1 (P-Tyr 15 -Cdk1), Cdk1, phosphorylated Wee1 (P-Ser 642 -Wee1), Wee1, Myt1, phosphorylated histone H3 (P-Ser 10 -H3), histone H3 (H3), phosphorylated p53 (P-Ser 15 -p53), p53, p21, and β-actin. ( b ) Renca cells treated with vehicle or 25–50 nM Adavo in the absence (−) or presence (+) of 10 μM CompC for 16 h. Cell lysates were analyzed by western blot using antibodies against P-Tyr 15 -Cdk1, Cdk1, P-Ser 10 -H3, H3, P-Ser 15 -p53, p53, and β-actin. The band densities were normalized against β-actin and the fold changes compared to that of control (vehicle/−CompC/−Adavo) are written under each band in ( a , b ). ( c ) The cell viability of 5–10 μM CompC-, 50–100 nM Adavo-, and CompC/Adavo-cotreated cells was measured by MTT assay, and the percentage of cell viability was plotted as the mean ± SD with n = 8. The p -values were determined as *** p < 0.001, compared with vehicle-treated control cells (−CompC/−Adavo) and ### p < 0.001, compared to vehicle- or CompC-treated cells in the absence of Adavo. ( d ) Renca cells were cultured for one day and treated with the vehicle or 5–500 nM Adavo for two days. The cell viability was measured by the MTT assay and the percentage was plotted as the mean ± SD with n = 8. *** p < 0.001, compared with vehicle-treated control cells.

    Journal: International Journal of Molecular Sciences

    Article Title: Compound C Inhibits Renca Renal Epithelial Carcinoma Growth in Syngeneic Mouse Models by Blocking Cell Cycle Progression, Adhesion and Invasion

    doi: 10.3390/ijms23179675

    Figure Lengend Snippet: CompC increased the phosphorylation of Cdk1 on Tyr 15 and Wee1 on Ser 642 . ( a ) Renca cells were cultured for one day and then serum-starved by incubation with SFM overnight. The cells were treated with SFM (C) or 10% FBS for the indicated times (8–24 h) in the absence (−) or presence (+) of 10 μM CompC. Cell lysates were analyzed by western blot using antibodies against phosphorylated Cdk1 (P-Tyr 15 -Cdk1), Cdk1, phosphorylated Wee1 (P-Ser 642 -Wee1), Wee1, Myt1, phosphorylated histone H3 (P-Ser 10 -H3), histone H3 (H3), phosphorylated p53 (P-Ser 15 -p53), p53, p21, and β-actin. ( b ) Renca cells treated with vehicle or 25–50 nM Adavo in the absence (−) or presence (+) of 10 μM CompC for 16 h. Cell lysates were analyzed by western blot using antibodies against P-Tyr 15 -Cdk1, Cdk1, P-Ser 10 -H3, H3, P-Ser 15 -p53, p53, and β-actin. The band densities were normalized against β-actin and the fold changes compared to that of control (vehicle/−CompC/−Adavo) are written under each band in ( a , b ). ( c ) The cell viability of 5–10 μM CompC-, 50–100 nM Adavo-, and CompC/Adavo-cotreated cells was measured by MTT assay, and the percentage of cell viability was plotted as the mean ± SD with n = 8. The p -values were determined as *** p < 0.001, compared with vehicle-treated control cells (−CompC/−Adavo) and ### p < 0.001, compared to vehicle- or CompC-treated cells in the absence of Adavo. ( d ) Renca cells were cultured for one day and treated with the vehicle or 5–500 nM Adavo for two days. The cell viability was measured by the MTT assay and the percentage was plotted as the mean ± SD with n = 8. *** p < 0.001, compared with vehicle-treated control cells.

    Article Snippet: Antibodies against Akt (#9272), phosphorylated Akt on Ser 473 (P-Ser 473 -Akt) (#4051), ERK1/2 (#9102), phosphorylated ERK1/2 on Thr 202 /Tyr 204 (P-ERK1/2) (#4370: rabbit mAb), AMPKα (#2532), phosphorylated AMPKα on Thr 172 (P- Thr 172 -AMPKα) (#2535), PI3K p85 (#4292), phosphorylated PI3K p85 on Tyr 458 and p55 on Tyr 199 (P-PI3K) (#4228), PLCγ1 (#2822), phosphorylated PLCγ1 on Tyr 783 (P-Tyr 783 -PLCγ1) (#2821), Cdk1 (#9112), phosphorylated Cdk1 on Tyr 15 (P-Tyr 15 -Cdk1) (#9111) and on Thr 161 (P-Thr 161 -Cdk1) (#9114), cyclin B1 (#4138), phosphorylated Wee1 on Ser 642 (P-Ser 642 -Wee1) (#4910), Myt1 (#4282), p53 (#9282), P-Ser 15 -p53 (#9284), histone H3 (#9715), and phosphorylated histone H3 on Ser 10 (P-Ser 10 -H3) (#3377) were purchased from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Phospho-proteomics, Cell Culture, Incubation, Western Blot, Control, MTT Assay

    Schematic representation of the effect of CompC on tumor growth in Renca syngeneic mouse model. Arrow (→) and truncated line (┬) indicate activation and inhibition, respectively. Regulatory pathways of cell cycle progression, G2/M cell cycle arrest, adhesion, migration, and invasion diverge into tumor growth in the Renca syngeneic mouse model. The left part of the schematic indicates that CompC suppresses cell cycle progression by inhibiting PDGFR-dependent signaling pathways, including Akt. At the center of the schematic, ROS-dependent ERK1/2 activation also appears to play a role in G2/M cell cycle arrest. The ROS scavenger, N-acetyl cysteine (NAC), interferes with CompC-induced ERK1/2 activation and G2/M cell cycle arrest. ROS may also induce phosphorylation of Wee1 at Ser 642 via ERK1/2 or other signaling pathways. Active Wee1 inactivates Cdk1 by increasing phosphorylation of Cdk1 at Tyr 15 (P-Tyr 15 -Cdk1), which in turn results in the reduction of phosphorylated histone H3 at Ser 10 (P-Ser 10 -H3). CompC-induced inactivation of Cdk1 and reduction of P-Ser 10 -H3 may play a role in G2/M cell cycle arrest. Activation of p53 via ROS production or other signaling pathways also plays a role in G2/M cell cycle arrest. The Wee1 inhibitor Adavosertib (Adavo) prevents the CompC-dependent increase in P-Tyr 15 -Cdk1 and P-Ser 15 -p53 levels and the CompC-dependent decrease in P-Ser 10 -H3 levels, thereby reducing G2/M cell cycle arrest. As shown in the right part of the figure, CompC inhibits Renca cell adhesion, migration, and invasion. Although the molecular mechanism remains to be clarified, CompC-dependent inhibition of adhesion, migration, and invasion may play a role in reducing tumor growth in a Renca syngeneic mouse model.

    Journal: International Journal of Molecular Sciences

    Article Title: Compound C Inhibits Renca Renal Epithelial Carcinoma Growth in Syngeneic Mouse Models by Blocking Cell Cycle Progression, Adhesion and Invasion

    doi: 10.3390/ijms23179675

    Figure Lengend Snippet: Schematic representation of the effect of CompC on tumor growth in Renca syngeneic mouse model. Arrow (→) and truncated line (┬) indicate activation and inhibition, respectively. Regulatory pathways of cell cycle progression, G2/M cell cycle arrest, adhesion, migration, and invasion diverge into tumor growth in the Renca syngeneic mouse model. The left part of the schematic indicates that CompC suppresses cell cycle progression by inhibiting PDGFR-dependent signaling pathways, including Akt. At the center of the schematic, ROS-dependent ERK1/2 activation also appears to play a role in G2/M cell cycle arrest. The ROS scavenger, N-acetyl cysteine (NAC), interferes with CompC-induced ERK1/2 activation and G2/M cell cycle arrest. ROS may also induce phosphorylation of Wee1 at Ser 642 via ERK1/2 or other signaling pathways. Active Wee1 inactivates Cdk1 by increasing phosphorylation of Cdk1 at Tyr 15 (P-Tyr 15 -Cdk1), which in turn results in the reduction of phosphorylated histone H3 at Ser 10 (P-Ser 10 -H3). CompC-induced inactivation of Cdk1 and reduction of P-Ser 10 -H3 may play a role in G2/M cell cycle arrest. Activation of p53 via ROS production or other signaling pathways also plays a role in G2/M cell cycle arrest. The Wee1 inhibitor Adavosertib (Adavo) prevents the CompC-dependent increase in P-Tyr 15 -Cdk1 and P-Ser 15 -p53 levels and the CompC-dependent decrease in P-Ser 10 -H3 levels, thereby reducing G2/M cell cycle arrest. As shown in the right part of the figure, CompC inhibits Renca cell adhesion, migration, and invasion. Although the molecular mechanism remains to be clarified, CompC-dependent inhibition of adhesion, migration, and invasion may play a role in reducing tumor growth in a Renca syngeneic mouse model.

    Article Snippet: Antibodies against Akt (#9272), phosphorylated Akt on Ser 473 (P-Ser 473 -Akt) (#4051), ERK1/2 (#9102), phosphorylated ERK1/2 on Thr 202 /Tyr 204 (P-ERK1/2) (#4370: rabbit mAb), AMPKα (#2532), phosphorylated AMPKα on Thr 172 (P- Thr 172 -AMPKα) (#2535), PI3K p85 (#4292), phosphorylated PI3K p85 on Tyr 458 and p55 on Tyr 199 (P-PI3K) (#4228), PLCγ1 (#2822), phosphorylated PLCγ1 on Tyr 783 (P-Tyr 783 -PLCγ1) (#2821), Cdk1 (#9112), phosphorylated Cdk1 on Tyr 15 (P-Tyr 15 -Cdk1) (#9111) and on Thr 161 (P-Thr 161 -Cdk1) (#9114), cyclin B1 (#4138), phosphorylated Wee1 on Ser 642 (P-Ser 642 -Wee1) (#4910), Myt1 (#4282), p53 (#9282), P-Ser 15 -p53 (#9284), histone H3 (#9715), and phosphorylated histone H3 on Ser 10 (P-Ser 10 -H3) (#3377) were purchased from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Activation Assay, Inhibition, Migration, Protein-Protein interactions, Phospho-proteomics