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The <t>E2F1–WDHD1</t> axis promotes malignant phenotypes in pancreatic cancer by upregulating cyclin D1. ( A , B ) Expression of cell cycle-related proteins after knocking down WDHD1. β-actin served as a loading control; Representative images were selected from three independent experiments. ( C ) Expression of CDK4 and cyclin D proteins after overexpression of WDHD1. β-actin served as a loading control. Representative images were selected from three independent experiments. ( D ) RNA expression levels of E2F1 in various pancreatic cancer cell lines show elevated expression compared to normal pancreatic cell lines ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test), ns, non-significant. ( E , F ) Overexpression of E2F1 can increase the expression of WDHD1 at both the RNA and protein levels ( n = 4 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, *** p < 0.001 (Student’s t -test). β-actin served as a loading control. Representative images were selected from three independent experiments. ( G ) The impact of WDHD1 knockdown after overexpression of E2F1 on cyclin D1, cyclin D3, and CDK4 at protein level. β-actin served as a loading control. Representative images were selected from three independent experiments. ( H ) E2F1 activates the WDHD1 promoter. E2F1 overexpression significantly increased the activity of a luciferase reporter driven by the full-length WDHD1 promoter relative to the vector control, consistent with direct transcriptional activation of WDHD1 by E2F1 ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: *** p < 0.001 (Student’s t -test). ( I ) ChIP–qPCR shows enrichment of the WDHD1 promoter <t>in</t> <t>anti-E2F1</t> immunoprecipitates relative to IgG control ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: **** p < 0.0001 (Student’s t -test). The unedited blots can be found in .
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(A, B) Kaplan–Meier plot showing that overexpression of <t>E2F1</t> is associated with shorter overall survival (A) and progression-free interval (B) in endometrial cancer cohort. (C, D) Kaplan–Meier plot showing that co-overexpression of LARP1 and E2F1 is associated with shorter overall survival (C) and progression-free interval (D) in endometrial cancer cohort. (E) Spearman correlation analysis shows a correlation between LARP1 and E2F1 in endometrial cancer patients.
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Image Search Results


The E2F1–WDHD1 axis promotes malignant phenotypes in pancreatic cancer by upregulating cyclin D1. ( A , B ) Expression of cell cycle-related proteins after knocking down WDHD1. β-actin served as a loading control; Representative images were selected from three independent experiments. ( C ) Expression of CDK4 and cyclin D proteins after overexpression of WDHD1. β-actin served as a loading control. Representative images were selected from three independent experiments. ( D ) RNA expression levels of E2F1 in various pancreatic cancer cell lines show elevated expression compared to normal pancreatic cell lines ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test), ns, non-significant. ( E , F ) Overexpression of E2F1 can increase the expression of WDHD1 at both the RNA and protein levels ( n = 4 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, *** p < 0.001 (Student’s t -test). β-actin served as a loading control. Representative images were selected from three independent experiments. ( G ) The impact of WDHD1 knockdown after overexpression of E2F1 on cyclin D1, cyclin D3, and CDK4 at protein level. β-actin served as a loading control. Representative images were selected from three independent experiments. ( H ) E2F1 activates the WDHD1 promoter. E2F1 overexpression significantly increased the activity of a luciferase reporter driven by the full-length WDHD1 promoter relative to the vector control, consistent with direct transcriptional activation of WDHD1 by E2F1 ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: *** p < 0.001 (Student’s t -test). ( I ) ChIP–qPCR shows enrichment of the WDHD1 promoter in anti-E2F1 immunoprecipitates relative to IgG control ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: **** p < 0.0001 (Student’s t -test). The unedited blots can be found in .

Journal: Current Oncology

Article Title: E2F1-Driven WDHD1 Transcription Enhances Cell-Cycle Progression and Promotes Pancreatic Cancer Progression

doi: 10.3390/curroncol33040186

Figure Lengend Snippet: The E2F1–WDHD1 axis promotes malignant phenotypes in pancreatic cancer by upregulating cyclin D1. ( A , B ) Expression of cell cycle-related proteins after knocking down WDHD1. β-actin served as a loading control; Representative images were selected from three independent experiments. ( C ) Expression of CDK4 and cyclin D proteins after overexpression of WDHD1. β-actin served as a loading control. Representative images were selected from three independent experiments. ( D ) RNA expression levels of E2F1 in various pancreatic cancer cell lines show elevated expression compared to normal pancreatic cell lines ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test), ns, non-significant. ( E , F ) Overexpression of E2F1 can increase the expression of WDHD1 at both the RNA and protein levels ( n = 4 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, *** p < 0.001 (Student’s t -test). β-actin served as a loading control. Representative images were selected from three independent experiments. ( G ) The impact of WDHD1 knockdown after overexpression of E2F1 on cyclin D1, cyclin D3, and CDK4 at protein level. β-actin served as a loading control. Representative images were selected from three independent experiments. ( H ) E2F1 activates the WDHD1 promoter. E2F1 overexpression significantly increased the activity of a luciferase reporter driven by the full-length WDHD1 promoter relative to the vector control, consistent with direct transcriptional activation of WDHD1 by E2F1 ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: *** p < 0.001 (Student’s t -test). ( I ) ChIP–qPCR shows enrichment of the WDHD1 promoter in anti-E2F1 immunoprecipitates relative to IgG control ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: **** p < 0.0001 (Student’s t -test). The unedited blots can be found in .

Article Snippet: The antibodies utilized in this study included anti-WDHD1 (abclonal, A15396, 1:1000), anti-E2F1 (abclonal, A19579, 1:1000), anti-CDK4 (abclonal, A0366, 1:1000), anti-CDK6 (abclonal, A1545, 1:1000), anti-cyclin D1 (abclonal, A1301, 1:1000), and anti-cyclin D3 (abclonal, A3589, 1:1000). β-actin (ZSGB-BIO, TA-09, 1:1000) was used as the sample loading control.

Techniques: Expressing, Control, Over Expression, RNA Expression, Knockdown, Activity Assay, Luciferase, Plasmid Preparation, Activation Assay, ChIP-qPCR

(A, B) Kaplan–Meier plot showing that overexpression of E2F1 is associated with shorter overall survival (A) and progression-free interval (B) in endometrial cancer cohort. (C, D) Kaplan–Meier plot showing that co-overexpression of LARP1 and E2F1 is associated with shorter overall survival (C) and progression-free interval (D) in endometrial cancer cohort. (E) Spearman correlation analysis shows a correlation between LARP1 and E2F1 in endometrial cancer patients.

Journal: bioRxiv

Article Title: “Targeting LARP1 Enhances Carboplatin Sensitivity and Suppresses Tumor Growth in Endometrial Cancer”

doi: 10.64898/2026.03.22.713473

Figure Lengend Snippet: (A, B) Kaplan–Meier plot showing that overexpression of E2F1 is associated with shorter overall survival (A) and progression-free interval (B) in endometrial cancer cohort. (C, D) Kaplan–Meier plot showing that co-overexpression of LARP1 and E2F1 is associated with shorter overall survival (C) and progression-free interval (D) in endometrial cancer cohort. (E) Spearman correlation analysis shows a correlation between LARP1 and E2F1 in endometrial cancer patients.

Article Snippet: Cells were then incubated overnight at 4 °C with the following primary antibodies: LARP1 (Cat. No. sc-515873; 1:200 dilution; Santa Cruz Biotechnology, Dallas, TX, USA) and E2F1 (Cat. No. 3742S; 1:400 dilution; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Over Expression

(A, B) Immunoblot analysis showing the protein expression of LARP1 and E2F1 after transfecting ISHI (A) and HEC-1A (B) cells with control or LARP1 siRNA. β-actin was used as a loading control. (C) Images representing immunofluorescence staining of LARP1 (green) and E2F1 (red) in HEC-1A cells after transfection with control or LARP1 siRNA. DAPI was used as a counter stain. Scale bar = 50 µm.

Journal: bioRxiv

Article Title: “Targeting LARP1 Enhances Carboplatin Sensitivity and Suppresses Tumor Growth in Endometrial Cancer”

doi: 10.64898/2026.03.22.713473

Figure Lengend Snippet: (A, B) Immunoblot analysis showing the protein expression of LARP1 and E2F1 after transfecting ISHI (A) and HEC-1A (B) cells with control or LARP1 siRNA. β-actin was used as a loading control. (C) Images representing immunofluorescence staining of LARP1 (green) and E2F1 (red) in HEC-1A cells after transfection with control or LARP1 siRNA. DAPI was used as a counter stain. Scale bar = 50 µm.

Article Snippet: Cells were then incubated overnight at 4 °C with the following primary antibodies: LARP1 (Cat. No. sc-515873; 1:200 dilution; Santa Cruz Biotechnology, Dallas, TX, USA) and E2F1 (Cat. No. 3742S; 1:400 dilution; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Western Blot, Expressing, Control, Immunofluorescence, Staining, Transfection