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ATCC pl45
Pl45, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 173 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 173 article reviews

pl45 - by Bioz Stars, 2026-03

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JUP is highly expressed in PDAC and precancerous lesions. A The expression of JUP in normal and PDAC tissues were detected by IHC and IFS. Compared with normal tissues, JUP was highly expressed in PDAC tissues (n=25). B IFS of JUP in mouse pancreatic tissue samples ( n =6). Orange, JUP; green, CK-19; purple, Amylase; blue, DAPI. JUP co-localized mainly with CK-19, and increased in ADM, PanIN and PDAC. C Quantitative and statistical analyses of IHC and IFS results in human pancreatic tissues. D Quantitative and statistical analyses of relative expression levels of JUP, CK-19 and Amylase in mouse pancreatic tissues. All data were expressed as mean ± SD. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group. Scale bars, 100 μm

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: JUP is highly expressed in PDAC and precancerous lesions. A The expression of JUP in normal and PDAC tissues were detected by IHC and IFS. Compared with normal tissues, JUP was highly expressed in PDAC tissues (n=25). B IFS of JUP in mouse pancreatic tissue samples ( n =6). Orange, JUP; green, CK-19; purple, Amylase; blue, DAPI. JUP co-localized mainly with CK-19, and increased in ADM, PanIN and PDAC. C Quantitative and statistical analyses of IHC and IFS results in human pancreatic tissues. D Quantitative and statistical analyses of relative expression levels of JUP, CK-19 and Amylase in mouse pancreatic tissues. All data were expressed as mean ± SD. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group. Scale bars, 100 μm

Article Snippet: HPNE and HPDE human normal ductal epithelial cell lines, AsPC-1, BxPC-3, CaPan-2, CFPAC-1, HPAC, HPAF-II, MIA PaCa-2, PANC-1 and PL45 human PDAC cell lines, and Panc02 murine PDAC cell line were originally purchased from the American Type Culture Collection (ATCC, Virgin Islands, USA).

Techniques: Expressing, Control

JUP is essential for the growth of PDAC cells. Proliferative capacity of AsPC-1, PL45 and Panc02 cells with JUP knockdown or overexpression. A , CCK-8 assay: JUP knockdown suppressed PDAC cell proliferation ( A 1), overexpression of JUP promoted PDAC cell proliferation ( A 2). B , Clonogenic assay: siJUP suppressed the colony formation ( B 1). pJUP promoted the colony formation. ( B 2). C , EdU assay: JUP silence suppressed EdU incorporation ( C 1), JUP overexpression enhanced EdU incorporation ( C 2). All data were expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: JUP is essential for the growth of PDAC cells. Proliferative capacity of AsPC-1, PL45 and Panc02 cells with JUP knockdown or overexpression. A , CCK-8 assay: JUP knockdown suppressed PDAC cell proliferation ( A 1), overexpression of JUP promoted PDAC cell proliferation ( A 2). B , Clonogenic assay: siJUP suppressed the colony formation ( B 1). pJUP promoted the colony formation. ( B 2). C , EdU assay: JUP silence suppressed EdU incorporation ( C 1), JUP overexpression enhanced EdU incorporation ( C 2). All data were expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Techniques: Knockdown, Over Expression, CCK-8 Assay, Clonogenic Assay, EdU Assay, Control

JUP enhances the migration and invasion of PDAC cells. Scratch and transwell assays of PDAC cells with JUP knockdown ( A ) or overexpression ( B ). Silencing JUP attenuated the invasion and migration ability of PDAC cells, whereas overexpression of JUP enhanced the invasion and migration ability of PDAC cells. ( C , D ) Representative HE staining and CA199 staining of liver tissues. JUP promoted the formation of liver metastasis in mice. All data are expressed as mean ± SD, n = 4. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: JUP enhances the migration and invasion of PDAC cells. Scratch and transwell assays of PDAC cells with JUP knockdown ( A ) or overexpression ( B ). Silencing JUP attenuated the invasion and migration ability of PDAC cells, whereas overexpression of JUP enhanced the invasion and migration ability of PDAC cells. ( C , D ) Representative HE staining and CA199 staining of liver tissues. JUP promoted the formation of liver metastasis in mice. All data are expressed as mean ± SD, n = 4. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Techniques: Migration, Knockdown, Over Expression, Staining, Control

FOXM1 transcriptionally regulates JUP in PDAC. A , IHC: Levels of JUP and FOXM1 protein expression in PDAC ( A1 ). Linear regression analysis: the correlation of FOXM1 and JUP ( n = 16) ( A2 ). Correlation analysis of FOXM1 and JUP expression in PDAC ( http://gepia.cancer-pku.cn/ ) ( n = 329) ( A3 ). B-C , Expression of FOXM1 was altered by transfection with siRNA or expression vectors. The impact of FOXM1 on JUP expression in PDAC cells by WB ( B ) and RT-qPCR ( C ) analyses. Note that FOXM1 inhibited the expression of JUP mRNA and protein in AsPC-1 and PL45, while the overexpression of FOXM1 increased the JUP mRNA and protein in AsPC-1 and PL45. FOXM1 regulated the expression of both JUP protein and mRNA. D , Direct binding of JUP to FOXM1 promoter. Sequences and positions of putative FOXM1-binding elements on JUP promoter (#1 and #2) ( D1 ). Normal IgG was used as a control, and 1.5% of the total cell lysates was subjected to PCR before immunoprecipitation. The ChIP assay to test the direct binding of FOXM1 on the genomic locus of JUP promoter regions ( D2 ). Quantitative analysis of ChIP results ( D3 ). All data are expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: FOXM1 transcriptionally regulates JUP in PDAC. A , IHC: Levels of JUP and FOXM1 protein expression in PDAC ( A1 ). Linear regression analysis: the correlation of FOXM1 and JUP ( n = 16) ( A2 ). Correlation analysis of FOXM1 and JUP expression in PDAC ( http://gepia.cancer-pku.cn/ ) ( n = 329) ( A3 ). B-C , Expression of FOXM1 was altered by transfection with siRNA or expression vectors. The impact of FOXM1 on JUP expression in PDAC cells by WB ( B ) and RT-qPCR ( C ) analyses. Note that FOXM1 inhibited the expression of JUP mRNA and protein in AsPC-1 and PL45, while the overexpression of FOXM1 increased the JUP mRNA and protein in AsPC-1 and PL45. FOXM1 regulated the expression of both JUP protein and mRNA. D , Direct binding of JUP to FOXM1 promoter. Sequences and positions of putative FOXM1-binding elements on JUP promoter (#1 and #2) ( D1 ). Normal IgG was used as a control, and 1.5% of the total cell lysates was subjected to PCR before immunoprecipitation. The ChIP assay to test the direct binding of FOXM1 on the genomic locus of JUP promoter regions ( D2 ). Quantitative analysis of ChIP results ( D3 ). All data are expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Techniques: Expressing, Transfection, Quantitative RT-PCR, Over Expression, Binding Assay, Control, Immunoprecipitation

FOXM1-mediated cancer cell proliferation requires JUP expression. A - C , FOXM1-silenced and JUP-overexpressing PDAC cells were established. The protein levels of FOXM1 and JUP were determined by Western blot ( A1 ) and the mRNA levels by RT-qPCR ( A2 ); cell viability by CCK-8 ( B ), and colony formation assay and the number of clones by ImageJ software. Note that JUP mediated FOXM1-induced PDAC cell proliferation and colony formation ( C ). D , PDAC cells were injected subcutaneously into mice. Tumor sizes were measured weekly ( D1 ). The mice were sacrificed and the tumors were removed and weighed ( D2 , D3 ). All data were expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: FOXM1-mediated cancer cell proliferation requires JUP expression. A - C , FOXM1-silenced and JUP-overexpressing PDAC cells were established. The protein levels of FOXM1 and JUP were determined by Western blot ( A1 ) and the mRNA levels by RT-qPCR ( A2 ); cell viability by CCK-8 ( B ), and colony formation assay and the number of clones by ImageJ software. Note that JUP mediated FOXM1-induced PDAC cell proliferation and colony formation ( C ). D , PDAC cells were injected subcutaneously into mice. Tumor sizes were measured weekly ( D1 ). The mice were sacrificed and the tumors were removed and weighed ( D2 , D3 ). All data were expressed as mean ± SD, n = 3. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Techniques: Expressing, Western Blot, Quantitative RT-PCR, CCK-8 Assay, Colony Assay, Clone Assay, Software, Injection, Control

FOXM1-mediated therapeutic resistance requires JUP expression. AsPC-1, PL45 and Panc02 cells were either transfection with siRNA (NC or siJUP) or expression vectors (p3.1 or pJUP) to alter the expression levels of JUP. A , The cells were then treated in vitro with different concentrations of GEM and OXA for 48 h and cell viability was determined by CCK8 assay. Note that increased expression of JUP significantly enhanced PDAC cells resistance to both GEM and OXA, whereas reduced expression of JUP did the opposite. B , GEM/OXA in vivo treatment model scheme. C , D , The cells with altered expression of JUP were subcutaneously injected into groups of mice, which then received treatment of drugs ( C , GEM; D , OXA) for indicated times. The tumor growth curves ( C1 , D1 ), subcutaneous tumors from mice ( C2 , D2 ) and tumor weights ( C3 , D3 ) were shown. Note that increased JUP expression significantly reduced the therapeutic efficacy of both GEM and OXA. All data were expressed as mean ± SD, n = 5. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Journal: Cell Communication and Signaling : CCS

Article Title: Transcriptional deregulation by FOXM1–JUP signaling confers dual oncogenic drivers for pancreatic tumorigenesis and therapeutic resistance

doi: 10.1186/s12964-025-02512-5

Figure Lengend Snippet: FOXM1-mediated therapeutic resistance requires JUP expression. AsPC-1, PL45 and Panc02 cells were either transfection with siRNA (NC or siJUP) or expression vectors (p3.1 or pJUP) to alter the expression levels of JUP. A , The cells were then treated in vitro with different concentrations of GEM and OXA for 48 h and cell viability was determined by CCK8 assay. Note that increased expression of JUP significantly enhanced PDAC cells resistance to both GEM and OXA, whereas reduced expression of JUP did the opposite. B , GEM/OXA in vivo treatment model scheme. C , D , The cells with altered expression of JUP were subcutaneously injected into groups of mice, which then received treatment of drugs ( C , GEM; D , OXA) for indicated times. The tumor growth curves ( C1 , D1 ), subcutaneous tumors from mice ( C2 , D2 ) and tumor weights ( C3 , D3 ) were shown. Note that increased JUP expression significantly reduced the therapeutic efficacy of both GEM and OXA. All data were expressed as mean ± SD, n = 5. Statistical analysis: student t-test or ANOVA, * P < 0.05, ** P < 0.01 and *** P < 0.001 vs. control group

Techniques: Expressing, Transfection, In Vitro, CCK-8 Assay, In Vivo, Injection, Drug discovery, Control

Menin suppressed the glycolysis of PDAC in vitro (A) Gene set enrichment analysis (GSEA) based on the TCGA database to explore the relationship between Menin expression and glycolysis pathway. (B–D) RT-qPCR and western blot were utilized for detecting the glycolysis-associated protein GLUT1 and LDHA in Menin-modulated PL45 and Bx-PC3 cells. (E–G) Relative ATP, extracellular lactatequantification, and total glucose consumption of Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. (H) Glucose stress test via measuring the extracellular acidification rate (ECAR) in Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. 2-DG: 2-deoxyglucose. (I) Real-time analysis of oxygen consumption rate (OCR) in Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. FCCP: carbonyl cyanide p-(trifluoromethoxy) phenylhydrazone. ∗∗∗ p < 0.001 when comparing Menin-OE plasmid transfected cells to control vector-transfected cells. Error bars represent mean ± SD. Each experiment was conducted in biological triplicates for each condition.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin suppressed the glycolysis of PDAC in vitro (A) Gene set enrichment analysis (GSEA) based on the TCGA database to explore the relationship between Menin expression and glycolysis pathway. (B–D) RT-qPCR and western blot were utilized for detecting the glycolysis-associated protein GLUT1 and LDHA in Menin-modulated PL45 and Bx-PC3 cells. (E–G) Relative ATP, extracellular lactatequantification, and total glucose consumption of Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. (H) Glucose stress test via measuring the extracellular acidification rate (ECAR) in Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. 2-DG: 2-deoxyglucose. (I) Real-time analysis of oxygen consumption rate (OCR) in Menin-overexpression and control vector-transfected PL45 and Bx-PC3 cells. FCCP: carbonyl cyanide p-(trifluoromethoxy) phenylhydrazone. ∗∗∗ p < 0.001 when comparing Menin-OE plasmid transfected cells to control vector-transfected cells. Error bars represent mean ± SD. Each experiment was conducted in biological triplicates for each condition.

Article Snippet: The pancreatic ductal adenocarcinoma (PDAC) cell lines PL45 and Bx-PC3 were obtained from iCell Bioscience Inc. (Shanghai, China) and the American Type Culture Collection (ATCC; Manassas, VA, USA), respectively.

Techniques: In Vitro, Expressing, Quantitative RT-PCR, Western Blot, Over Expression, Control, Plasmid Preparation, Transfection

Menin regulates proliferation, colony formation and migration via glycolysis (A) CCK-8 assays show the 5-day proliferation curves of PL45 and BxPC-3 cells stably over-expressing Menin or a negative-control vector (NC) cultured with or without the glycolysis activator EMP; values are mean ± SD. (B) Representative crystal-violet–stained colonies formed by PL45 and BxPC-3 cells. (C) Quantification of colony numbers from (B); data are mean ± SD. (D) Representative crystal-violet–stained Transwell images of migrated PL45 and BxPC-3 cells obtained under the indicated conditions; scale bars, 100 μm. (E) Quantification of relative cell migration (fold change) from (D); values are mean ± SD. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin regulates proliferation, colony formation and migration via glycolysis (A) CCK-8 assays show the 5-day proliferation curves of PL45 and BxPC-3 cells stably over-expressing Menin or a negative-control vector (NC) cultured with or without the glycolysis activator EMP; values are mean ± SD. (B) Representative crystal-violet–stained colonies formed by PL45 and BxPC-3 cells. (C) Quantification of colony numbers from (B); data are mean ± SD. (D) Representative crystal-violet–stained Transwell images of migrated PL45 and BxPC-3 cells obtained under the indicated conditions; scale bars, 100 μm. (E) Quantification of relative cell migration (fold change) from (D); values are mean ± SD. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001.

Techniques: Migration, CCK-8 Assay, Stable Transfection, Expressing, Negative Control, Plasmid Preparation, Cell Culture, Staining

Menin regulates glycolysis via affecting HKDC1 gene expression (A) Volcano plot illustrating upregulated and downregulated genes in Menin-overexpressing (Menin-OE) PL45 cells in comparison to the vector control group. (B) Heatmap representation of differentially expressed genes from the RNA-seq analysis. (C and D) Measurement of HKDC1 expression after Menin-overexpression in PL45 and BxPC-3 cells detected by RT-qPCR and western blot. (E and F) Expression levels (both mRNA and protein) of GLUT1 and LDHA in PL45 and BxPC-3 cells following HKDC1 silencing, as observed through RT-qPCR and western blot. (G–I) ATP, lactate secretion, and glucose consumption levels in HKDC1-silenced versus control PL45 and Bx-PC3 cell. ∗∗∗ p < 0.001. Error bars represent mean ± SD. Each experiment was conducted in biological triplicates for each condition.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin regulates glycolysis via affecting HKDC1 gene expression (A) Volcano plot illustrating upregulated and downregulated genes in Menin-overexpressing (Menin-OE) PL45 cells in comparison to the vector control group. (B) Heatmap representation of differentially expressed genes from the RNA-seq analysis. (C and D) Measurement of HKDC1 expression after Menin-overexpression in PL45 and BxPC-3 cells detected by RT-qPCR and western blot. (E and F) Expression levels (both mRNA and protein) of GLUT1 and LDHA in PL45 and BxPC-3 cells following HKDC1 silencing, as observed through RT-qPCR and western blot. (G–I) ATP, lactate secretion, and glucose consumption levels in HKDC1-silenced versus control PL45 and Bx-PC3 cell. ∗∗∗ p < 0.001. Error bars represent mean ± SD. Each experiment was conducted in biological triplicates for each condition.

Techniques: Gene Expression, Comparison, Plasmid Preparation, Control, RNA Sequencing, Expressing, Over Expression, Quantitative RT-PCR, Western Blot

HKDC1 knock-down rescues Menin-suppressed glycolysis and the associated oncogenic phenotypes (A) Western-blot analysis of GLUT1 and LDHA protein levels in PL45 and BxPC-3 cells stably expressing a negative control (NC), Menin over-expression (Menin-OE), HKDC1 short hairpin RNA (shHKDC1), or Menin-OE + shHKDC1; GAPDH is the loading control. (B–D) Quantification of relative cellular ATP levels (B), lactate production (C), and glucose consumption (D) under the indicated conditions. (E) Five-day CCK-8 proliferation curves of PL45 and BxPC-3 cells in the same groups. (F) Representative crystal-violet-stained colonies produced by PL45 and BxPC-3 cells. (G) Quantification of colony numbers from (F). (H) Representative crystal-violet-stained Transwell micrographs of migrated PL45 and BxPC-3 cells; scale bars, 100 μm. (I) Quantification of relative cell migration (fold change) from (H). All quantitative data are mean ± SD. ∗∗ p < 0.01 and ∗∗∗ p < 0.001 versus the Menin-OE group.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: HKDC1 knock-down rescues Menin-suppressed glycolysis and the associated oncogenic phenotypes (A) Western-blot analysis of GLUT1 and LDHA protein levels in PL45 and BxPC-3 cells stably expressing a negative control (NC), Menin over-expression (Menin-OE), HKDC1 short hairpin RNA (shHKDC1), or Menin-OE + shHKDC1; GAPDH is the loading control. (B–D) Quantification of relative cellular ATP levels (B), lactate production (C), and glucose consumption (D) under the indicated conditions. (E) Five-day CCK-8 proliferation curves of PL45 and BxPC-3 cells in the same groups. (F) Representative crystal-violet-stained colonies produced by PL45 and BxPC-3 cells. (G) Quantification of colony numbers from (F). (H) Representative crystal-violet-stained Transwell micrographs of migrated PL45 and BxPC-3 cells; scale bars, 100 μm. (I) Quantification of relative cell migration (fold change) from (H). All quantitative data are mean ± SD. ∗∗ p < 0.01 and ∗∗∗ p < 0.001 versus the Menin-OE group.

Techniques: Knockdown, Western Blot, Stable Transfection, Expressing, Negative Control, Over Expression, shRNA, Control, CCK-8 Assay, Staining, Produced, Migration

Menin binds transcription factor YBX1 to regulate glycolysis (A) Immunostaining of PL45 cell protein samples following immunoprecipitation with IgG and anti-Menin antibody. (B) Analysis of peptide segments from mass spectrometry to identify proteins interacting with Menin. (C) Venn diagram highlighting the overlap between proteins associated with Menin and potential transcription factors of HKDC1. (D) Co-immunoprecipitation confirmed the direct combination between Menin and YBX1 in PL45 and Bx-PC3 cells. (E) Predicted interaction of Menin and YBX1. F, GST pull-down assays demonstrating direct in vitro interaction between Menin and YBX1. Purified GST-Menin (but not GST alone) pulled down HIS-YBX1. (F) Further mapping using GST-tagged Menin truncation mutants revealed that the interaction with HA-YBX1 is mediated primarily through the central and C-terminal regions of Menin (amino acids 211–610), as fragments containing these regions, but not the N-terminal (1-210 aa) fragment, showed binding. Blots were probed with indicated antibodies (anti-HIS, anti-GST, anti-HA). (G–I) Glycolysis indicators (ATP, lactate, and glucose consumption) influenced by Menin was restored by YBX1 knocking down in both PL45 and BxPC-3 cell lines,∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 when comparing Menin-OE plasmid transfected cells to control vector-transfected cells. Error bars represent mean ± SD.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin binds transcription factor YBX1 to regulate glycolysis (A) Immunostaining of PL45 cell protein samples following immunoprecipitation with IgG and anti-Menin antibody. (B) Analysis of peptide segments from mass spectrometry to identify proteins interacting with Menin. (C) Venn diagram highlighting the overlap between proteins associated with Menin and potential transcription factors of HKDC1. (D) Co-immunoprecipitation confirmed the direct combination between Menin and YBX1 in PL45 and Bx-PC3 cells. (E) Predicted interaction of Menin and YBX1. F, GST pull-down assays demonstrating direct in vitro interaction between Menin and YBX1. Purified GST-Menin (but not GST alone) pulled down HIS-YBX1. (F) Further mapping using GST-tagged Menin truncation mutants revealed that the interaction with HA-YBX1 is mediated primarily through the central and C-terminal regions of Menin (amino acids 211–610), as fragments containing these regions, but not the N-terminal (1-210 aa) fragment, showed binding. Blots were probed with indicated antibodies (anti-HIS, anti-GST, anti-HA). (G–I) Glycolysis indicators (ATP, lactate, and glucose consumption) influenced by Menin was restored by YBX1 knocking down in both PL45 and BxPC-3 cell lines,∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 when comparing Menin-OE plasmid transfected cells to control vector-transfected cells. Error bars represent mean ± SD.

Techniques: Immunostaining, Immunoprecipitation, Mass Spectrometry, In Vitro, Purification, Binding Assay, Plasmid Preparation, Transfection, Control

$Menin induces nuclear localization of YBX1 and activates HKDC1 transcription (A) Immunoblotting of cytoplasmic and nuclear fractions shows that Menin over-expression (Menin-OE) markedly increases nuclear YBX1 in PL45 and BxPC-3 cells compared with the negative control (NC); GAPDH and Histone H3 serve as cytoplasmic and nuclear loading controls, respectively. (B) Immunofluorescence imaging confirms the enhanced nuclear accumulation of YBX1 (red) following Menin-OE, with nuclei counter-stained by DAPI (blue); scale bars, 200 μm. (C) Cycloheximide (CHX) chase assays (0–8 h) reveal that Menin-OE does not affect YBX1 protein stability in either cell line (LaminB1 loading control). (D) FLAG immunoprecipitation of nuclear extracts demonstrates a physical association between Flag-tagged Menin and endogenous YBX1 in PL45 and BxPC-3 cells, with LaminB1 as the input control. (E) Schematic of HKDC1-promoter luciferase reporters containing a wild-type (WT) or mutated (Mut) YBX1-binding motif. (F) Dual-luciferase assays in HEK-293 cells show that YBX1 activates the WT reporter but not the Mut reporter. (G) In PL45 and BxPC-3 cells, Menin-OE and YBX1 co-expression synergistically enhance WT-reporter activity, whereas mutation of the YBX1 site abolishes this effect. (H) ChIP-qPCR confirms increased recruitment of YBX1 to the HKDC1 promoter upon Menin-OE. (I) YBX1 over-expression alone serves as a positive control. (J) Combined Menin-OE and YBX1-OE further augment YBX1 binding relative to vector or IgG controls. Quantitative data are presented as mean ± SD ( n = 3); ∗∗∗ p < 0.001 versus the indicated control.$

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin induces nuclear localization of YBX1 and activates HKDC1 transcription (A) Immunoblotting of cytoplasmic and nuclear fractions shows that Menin over-expression (Menin-OE) markedly increases nuclear YBX1 in PL45 and BxPC-3 cells compared with the negative control (NC); GAPDH and Histone H3 serve as cytoplasmic and nuclear loading controls, respectively. (B) Immunofluorescence imaging confirms the enhanced nuclear accumulation of YBX1 (red) following Menin-OE, with nuclei counter-stained by DAPI (blue); scale bars, 200 μm. (C) Cycloheximide (CHX) chase assays (0–8 h) reveal that Menin-OE does not affect YBX1 protein stability in either cell line (LaminB1 loading control). (D) FLAG immunoprecipitation of nuclear extracts demonstrates a physical association between Flag-tagged Menin and endogenous YBX1 in PL45 and BxPC-3 cells, with LaminB1 as the input control. (E) Schematic of HKDC1-promoter luciferase reporters containing a wild-type (WT) or mutated (Mut) YBX1-binding motif. (F) Dual-luciferase assays in HEK-293 cells show that YBX1 activates the WT reporter but not the Mut reporter. (G) In PL45 and BxPC-3 cells, Menin-OE and YBX1 co-expression synergistically enhance WT-reporter activity, whereas mutation of the YBX1 site abolishes this effect. (H) ChIP-qPCR confirms increased recruitment of YBX1 to the HKDC1 promoter upon Menin-OE. (I) YBX1 over-expression alone serves as a positive control. (J) Combined Menin-OE and YBX1-OE further augment YBX1 binding relative to vector or IgG controls. Quantitative data are presented as mean ± SD ( n = 3); ∗∗∗ p < 0.001 versus the indicated control.

Techniques: Western Blot, Over Expression, Negative Control, Immunofluorescence, Imaging, Staining, Control, Immunoprecipitation, Luciferase, Binding Assay, Expressing, Activity Assay, Mutagenesis, ChIP-qPCR, Positive Control, Plasmid Preparation

Menin over-expression suppresses tumor growth and attenuates glycolytic activity in a PL45 xenograft model (A) Representative photographs of nude mice bearing PL45 xenografts and the corresponding tumors immediately after excision (scale bars, 1 cm). (B) Tumor-volume growth curves (mean ± SD, n = 5) recorded every three days from implantation to day 24; ∗∗∗ p < 0.001 versus NC at the endpoint. (C) Final tumor weights at sacrifice (mean ± SD, n = 5). (D) Intratumoral concentrations of glucose, ATP, and lactate measured in freshly isolated tumors; Menin-OE significantly lowers glycolytic read-outs relative to NC (mean ± SD, n = 5). (E) Immunoblotting of xenograft lysates shows increased Menin and decreased HKDC1, GLUT1, and LDHA in the Menin-OE group; GAPDH serves as the loading control. (F) Immunohistochemical staining of xenograft sections for Menin, HKDC1, GLUT1, and LDHA at 200 × (left; scale bars, 100 μm) and 400 × (right; scale bars, 50 μm) magnification. At least one micrograph in each magnification group carries the indicated scale bar. Data are expressed as mean ± SD.∗ p < 0.05; ∗∗ p < 0.01; and ∗∗∗ p < 0.001 versus NC. All in vivo experiments were performed with five biological replicates per condition.

Journal: iScience

Article Title: Menin regulates YBX1 nucleus translocation to boost the HKDC1 transcription and affects pancreatic cancer glycolysis

doi: 10.1016/j.isci.2025.113245

Figure Lengend Snippet: Menin over-expression suppresses tumor growth and attenuates glycolytic activity in a PL45 xenograft model (A) Representative photographs of nude mice bearing PL45 xenografts and the corresponding tumors immediately after excision (scale bars, 1 cm). (B) Tumor-volume growth curves (mean ± SD, n = 5) recorded every three days from implantation to day 24; ∗∗∗ p < 0.001 versus NC at the endpoint. (C) Final tumor weights at sacrifice (mean ± SD, n = 5). (D) Intratumoral concentrations of glucose, ATP, and lactate measured in freshly isolated tumors; Menin-OE significantly lowers glycolytic read-outs relative to NC (mean ± SD, n = 5). (E) Immunoblotting of xenograft lysates shows increased Menin and decreased HKDC1, GLUT1, and LDHA in the Menin-OE group; GAPDH serves as the loading control. (F) Immunohistochemical staining of xenograft sections for Menin, HKDC1, GLUT1, and LDHA at 200 × (left; scale bars, 100 μm) and 400 × (right; scale bars, 50 μm) magnification. At least one micrograph in each magnification group carries the indicated scale bar. Data are expressed as mean ± SD.∗ p < 0.05; ∗∗ p < 0.01; and ∗∗∗ p < 0.001 versus NC. All in vivo experiments were performed with five biological replicates per condition.

Techniques: Over Expression, Activity Assay, Isolation, Western Blot, Control, Immunohistochemical staining, Staining, In Vivo

(A) Immunohistochemistry images for GPX4 and ROS (8-OHdG) staining in four PDAC cell lines (PL45, BxPC-3, PANC-1, and Panc04.03). (B) Semi-quantitative analysis of staining expressed as percentage of positive cells, intensity (0–3), and H-Score. (C) Chemical structure of RSL3. (D) Cell viability curves in response to RSL3 treatment (μM) in four cell lines. (E) Calculated IC₅₀ values for RSL3. (F) Cell viability curves in response to FOLFIRINOX treatment in logarithmic scale. (G) Individual IC₅₀ values for each FOLFIRINOX component (5-FU, leucovorin, irinotecan, and oxaliplatin) in mg/mL. Data represents the mean of three biological replicates.

Journal: bioRxiv

Article Title: FOLFIRINOX Combined with GPX4 Inhibition Induces Ferroptosis and Defines Redox-Based Therapeutic Subgroups in Pancreatic Cancer

doi: 10.1101/2025.09.12.675778

Figure Lengend Snippet: (A) Immunohistochemistry images for GPX4 and ROS (8-OHdG) staining in four PDAC cell lines (PL45, BxPC-3, PANC-1, and Panc04.03). (B) Semi-quantitative analysis of staining expressed as percentage of positive cells, intensity (0–3), and H-Score. (C) Chemical structure of RSL3. (D) Cell viability curves in response to RSL3 treatment (μM) in four cell lines. (E) Calculated IC₅₀ values for RSL3. (F) Cell viability curves in response to FOLFIRINOX treatment in logarithmic scale. (G) Individual IC₅₀ values for each FOLFIRINOX component (5-FU, leucovorin, irinotecan, and oxaliplatin) in mg/mL. Data represents the mean of three biological replicates.

Article Snippet: Human pancreatic cancer cell lines PL45, PANC-1, BxPC-3, and Panc04.03 were obtained from ATCC and cultured in DMEM or RPMI-1640 medium supplemented with 10% FBS and 1% P/S under standard conditions (37 °C, in a humidified atmosphere containing 5% CO2).

Techniques: Immunohistochemistry, Staining

This figure shows dose-response curves for four pancreatic cancer cell lines (PL45, Panc04.03, BxPC-3, and PANC-1) treated with FOLFIRINOX (A-D) or RSL3 (E-H). Cell viability (%) is shown in y-axis while drug concentration is shown in x-axis. For FOLFIRINOX, the X-axis is log-transformed concentration; for RSL3, it is linear in μM. Each panel includes the best-fit equation and R² value. White boxes: RSL3-sensitive PDAC-derived cell lines; black boxes: RSL3-resistant PDAC-derived cell lines.

Journal: bioRxiv

Article Title: FOLFIRINOX Combined with GPX4 Inhibition Induces Ferroptosis and Defines Redox-Based Therapeutic Subgroups in Pancreatic Cancer

doi: 10.1101/2025.09.12.675778

Figure Lengend Snippet: This figure shows dose-response curves for four pancreatic cancer cell lines (PL45, Panc04.03, BxPC-3, and PANC-1) treated with FOLFIRINOX (A-D) or RSL3 (E-H). Cell viability (%) is shown in y-axis while drug concentration is shown in x-axis. For FOLFIRINOX, the X-axis is log-transformed concentration; for RSL3, it is linear in μM. Each panel includes the best-fit equation and R² value. White boxes: RSL3-sensitive PDAC-derived cell lines; black boxes: RSL3-resistant PDAC-derived cell lines.

Techniques: Concentration Assay, Transformation Assay, Derivative Assay

Quantification of ferroptosis in PL45 (control mean ± 95% CI = 1.00 [0.45–1.55], FOLFIRINOX mean ± 95% CI = 1.67 [1.34–1.99]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.66 [2.22–3.11]) (A), Panc04.03 (control mean ± 95% CI = 1.00 [0.52–1.48], FOLFIRINOX mean ± 95% CI = 1.01 [0.53–1.50]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.48 [2.20–2.77])(B), BxPC-3 (control mean ± 95% CI = 1.00 [0.87–1.12], FOLFIRINOX mean ± 95% CI = 1.54 [1.27–1.81]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.48 [1.21–1.75]) (C), and PANC-1 (control mean ± 95% CI = 1.21 [0.80–1.63], FOLFIRINOX mean ± 95% CI = 1.74 [1.13–2.34]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.72 [1.46–1.97]) (D). Bar graphs show fold change in the ferroptosis ratio. Quantification of apoptosis in PL45 (control mean ± 95% CI = 1.00 [0.59–1.41], FOLFIRINOX mean ± 95% CI = 1.56 [0.81–2.31], FOLFIRINOX + RSL3 mean ± 95% CI = 2.94 [2.69–3.20]) (E), Panc04.03 (control mean ± 95% CI = 1.00 [0.66–1.34], FOLFIRINOX mean ± 95% CI = 2.51 [1.71–3.31], FOLFIRINOX + RSL3 mean ± 95% CI = 5.76 [3.02–8.50]) (F), BxPC-3 (control mean ± 95% CI = 1.00 [0.68–1.32], FOLFIRINOX mean ± 95% CI = 1.17 [0.95–1.38], FOLFIRINOX + RSL3 mean ± 95% CI = 0.82 [0.60–1.04]) (G), and PANC-1 (control mean ± 95% CI = 1.00 [0.55–1.28], FOLFIRINOX mean ± 95% CI = 1.75 [0.67–2.63], FOLFIRINOX + RSL3 mean ± 95% CI = 1.72 [0.24–2.54]) (H). Dot plots show Annexin V (x-axis) and propidium iodide (y-axis). Bar graphs show fold change in the apoptosis ratio (both early and late apoptosis). Quantification of intracellular ROS levels in PL45 (control mean ± 95% CI = 1.000 [0.914–1.086]; NAC mean ± 95% CI = 0.8460 [0.573–1.119]; FOLFIRINOX mean ± 95% CI = 0.8468 [0.625–1.069]; FOLFIRINOX + RSL3 mean ± 95% CI = 31.367 [1.132–1.601]; FOLFIRINOX + RSL3 + NAC mean ± 95% CI = 0.4424 [0.292– 0.593]) (I); Panc04.03 (control mean ± 95% CI = 1.011[0.750–1.272]; NAC mean ± 95% CI = 0.96 [0.80–1.11]; FOLFIRINOX mean ± 95% CI = 0.96 [0.67–1.25]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.694 [2.328–3.061]; FOLFIRINOX +RSL3 + NAC mean ± 95% CI = 0.7553 [0.327–1.183]) (J); BxPC-3 (control mean ± 95% CI = 1.000 [0.643–1.357]; FOLFIRINOX mean ± 95% CI = 1.172 [1.084–1.267]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.237 [1.170–1.305]) (K); and PANC-1 (control mean ± 95% CI = 1.013 [0.948–1.078]; FOLFIRINOX mean ± 95% CI = 0.6980 [0.768–1.185]; FOLFIRINOX + RSL3 mean ± 95% CI = 0.8678 [1.045–2.251]) (L). Bar graphs show fold change of intracellular ROS levels. Western blot quantification of GPX4 expression levels (PL45 control (mean ± 95 % CI: 0.9206 [0.1519 – 1.689]); PL45 FOLFIRINOX (mean ± 95 % CI: 2.373 [0.8821 – 3.863]); PL45 FOLFIRINOX + RSL3 (mean ± 95 % CI: 1.071 [–0.1754 – 2.318]); PL45 FOLFIRINOX + RSL3 + NAC (mean ± 95 % CI: 1.598 [0.5043 – 2.692]); Panc04.03 control (mean ± 95 % CI: 0.7333 [0.2162 – 1.250]); Panc04.03 FOLFIRINOX (mean ± 95 % CI: 1.500 [–0.01104 – 3.011]); Panc04.03 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.7667 [–0.6015 – 2.135]); Panc04.03 FOLFIRINOX + RSL3 + NAC (mean ± 95 % CI: 1.200 [0.5428 – 1.857]); BxPC-3 control (mean ± 95 % CI: 1.160 [0.4648 – 1.855]); BxPC-3 FOLFIRINOX (mean ± 95 % CI: 1.163 [0.9971 – 1.323]); BxPC-3 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.2615 [0.01392 – 0.5090]), PANC1 control (mean ± 95 % CI: 0.7926 [0.5111 – 1.074]); PANC1 FOLFIRINOX (mean ± 95 % CI: 0.6218 [0.4785 – 0.7650]); PANC1 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.1323 [0.06885 – 0.1957])); and SOD2 expression levels (PL45 control (mean ± 95% CI: 0.9972 [0.290– 1.704]); PL45 FOLFIRINOX (mean ± 95% CI: 1.409 [0.7315–2.086]); PL45 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.624 [0.9175–2.330]); PL45 FOLFIRINOX + RSL3 + NAC (mean ± 95% CI: 1.458 [0.9079–2.008]); (Panc04.03 control (mean ± 95% CI: 0.55 [0.3194–1.419]); Panc04.03 FOLFIRINOX (mean ± 95% CI: 1.0 [0.1043–1.896]); Panc04.03 FOLFIRINOX + RSL3 (mean ± 95% CI: 0.8 [0.0957–1.696]); Panc04.03 FOLFIRINOX + RSL3 + NAC (mean ± 95% CI: 0.9 [0.1548–1.645]); BxPC-3 control (mean ± 95% CI: 0.861 [0.5527–1.169]); BxPC-3 FOLFIRINOX (mean ± 95% CI: 1.436 [0.7947–2.078]); BxPC-3 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.873 [0.6964–4.443]); PANC1 control (mean ± 95% CI: 0.6098 [0.3236–0.896]); PANC1 FOLFIRINOX (mean ± 95% CI: 1.004 [0.6345–1.374]); PANC1 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.101 [0.6139–1.588]), including representative bands and histograms normalized to actin expression for PL45 (M), Panc04.03 (N), BxPC-3 (O), and PANC-1 (P). Abbreviations: Control (C), N-acetyl-cysteine (NAC), FOLFIRINOX (F), FOLFIRINOX + RSL3 (F+R), and FOLFIRINOX + RSL3 + N-acetyl-cysteine (F+R+NAC). White boxes: RSL3-sensitive PDAC-derived cell lines; black boxes: RSL3-resistant PDAC-derived cell lines. Statistical significance was considered at p < 0.05 (n.s. = not significant).

Journal: bioRxiv

Article Title: FOLFIRINOX Combined with GPX4 Inhibition Induces Ferroptosis and Defines Redox-Based Therapeutic Subgroups in Pancreatic Cancer

doi: 10.1101/2025.09.12.675778

Figure Lengend Snippet: Quantification of ferroptosis in PL45 (control mean ± 95% CI = 1.00 [0.45–1.55], FOLFIRINOX mean ± 95% CI = 1.67 [1.34–1.99]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.66 [2.22–3.11]) (A), Panc04.03 (control mean ± 95% CI = 1.00 [0.52–1.48], FOLFIRINOX mean ± 95% CI = 1.01 [0.53–1.50]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.48 [2.20–2.77])(B), BxPC-3 (control mean ± 95% CI = 1.00 [0.87–1.12], FOLFIRINOX mean ± 95% CI = 1.54 [1.27–1.81]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.48 [1.21–1.75]) (C), and PANC-1 (control mean ± 95% CI = 1.21 [0.80–1.63], FOLFIRINOX mean ± 95% CI = 1.74 [1.13–2.34]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.72 [1.46–1.97]) (D). Bar graphs show fold change in the ferroptosis ratio. Quantification of apoptosis in PL45 (control mean ± 95% CI = 1.00 [0.59–1.41], FOLFIRINOX mean ± 95% CI = 1.56 [0.81–2.31], FOLFIRINOX + RSL3 mean ± 95% CI = 2.94 [2.69–3.20]) (E), Panc04.03 (control mean ± 95% CI = 1.00 [0.66–1.34], FOLFIRINOX mean ± 95% CI = 2.51 [1.71–3.31], FOLFIRINOX + RSL3 mean ± 95% CI = 5.76 [3.02–8.50]) (F), BxPC-3 (control mean ± 95% CI = 1.00 [0.68–1.32], FOLFIRINOX mean ± 95% CI = 1.17 [0.95–1.38], FOLFIRINOX + RSL3 mean ± 95% CI = 0.82 [0.60–1.04]) (G), and PANC-1 (control mean ± 95% CI = 1.00 [0.55–1.28], FOLFIRINOX mean ± 95% CI = 1.75 [0.67–2.63], FOLFIRINOX + RSL3 mean ± 95% CI = 1.72 [0.24–2.54]) (H). Dot plots show Annexin V (x-axis) and propidium iodide (y-axis). Bar graphs show fold change in the apoptosis ratio (both early and late apoptosis). Quantification of intracellular ROS levels in PL45 (control mean ± 95% CI = 1.000 [0.914–1.086]; NAC mean ± 95% CI = 0.8460 [0.573–1.119]; FOLFIRINOX mean ± 95% CI = 0.8468 [0.625–1.069]; FOLFIRINOX + RSL3 mean ± 95% CI = 31.367 [1.132–1.601]; FOLFIRINOX + RSL3 + NAC mean ± 95% CI = 0.4424 [0.292– 0.593]) (I); Panc04.03 (control mean ± 95% CI = 1.011[0.750–1.272]; NAC mean ± 95% CI = 0.96 [0.80–1.11]; FOLFIRINOX mean ± 95% CI = 0.96 [0.67–1.25]; FOLFIRINOX + RSL3 mean ± 95% CI = 2.694 [2.328–3.061]; FOLFIRINOX +RSL3 + NAC mean ± 95% CI = 0.7553 [0.327–1.183]) (J); BxPC-3 (control mean ± 95% CI = 1.000 [0.643–1.357]; FOLFIRINOX mean ± 95% CI = 1.172 [1.084–1.267]; FOLFIRINOX + RSL3 mean ± 95% CI = 1.237 [1.170–1.305]) (K); and PANC-1 (control mean ± 95% CI = 1.013 [0.948–1.078]; FOLFIRINOX mean ± 95% CI = 0.6980 [0.768–1.185]; FOLFIRINOX + RSL3 mean ± 95% CI = 0.8678 [1.045–2.251]) (L). Bar graphs show fold change of intracellular ROS levels. Western blot quantification of GPX4 expression levels (PL45 control (mean ± 95 % CI: 0.9206 [0.1519 – 1.689]); PL45 FOLFIRINOX (mean ± 95 % CI: 2.373 [0.8821 – 3.863]); PL45 FOLFIRINOX + RSL3 (mean ± 95 % CI: 1.071 [–0.1754 – 2.318]); PL45 FOLFIRINOX + RSL3 + NAC (mean ± 95 % CI: 1.598 [0.5043 – 2.692]); Panc04.03 control (mean ± 95 % CI: 0.7333 [0.2162 – 1.250]); Panc04.03 FOLFIRINOX (mean ± 95 % CI: 1.500 [–0.01104 – 3.011]); Panc04.03 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.7667 [–0.6015 – 2.135]); Panc04.03 FOLFIRINOX + RSL3 + NAC (mean ± 95 % CI: 1.200 [0.5428 – 1.857]); BxPC-3 control (mean ± 95 % CI: 1.160 [0.4648 – 1.855]); BxPC-3 FOLFIRINOX (mean ± 95 % CI: 1.163 [0.9971 – 1.323]); BxPC-3 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.2615 [0.01392 – 0.5090]), PANC1 control (mean ± 95 % CI: 0.7926 [0.5111 – 1.074]); PANC1 FOLFIRINOX (mean ± 95 % CI: 0.6218 [0.4785 – 0.7650]); PANC1 FOLFIRINOX + RSL3 (mean ± 95 % CI: 0.1323 [0.06885 – 0.1957])); and SOD2 expression levels (PL45 control (mean ± 95% CI: 0.9972 [0.290– 1.704]); PL45 FOLFIRINOX (mean ± 95% CI: 1.409 [0.7315–2.086]); PL45 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.624 [0.9175–2.330]); PL45 FOLFIRINOX + RSL3 + NAC (mean ± 95% CI: 1.458 [0.9079–2.008]); (Panc04.03 control (mean ± 95% CI: 0.55 [0.3194–1.419]); Panc04.03 FOLFIRINOX (mean ± 95% CI: 1.0 [0.1043–1.896]); Panc04.03 FOLFIRINOX + RSL3 (mean ± 95% CI: 0.8 [0.0957–1.696]); Panc04.03 FOLFIRINOX + RSL3 + NAC (mean ± 95% CI: 0.9 [0.1548–1.645]); BxPC-3 control (mean ± 95% CI: 0.861 [0.5527–1.169]); BxPC-3 FOLFIRINOX (mean ± 95% CI: 1.436 [0.7947–2.078]); BxPC-3 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.873 [0.6964–4.443]); PANC1 control (mean ± 95% CI: 0.6098 [0.3236–0.896]); PANC1 FOLFIRINOX (mean ± 95% CI: 1.004 [0.6345–1.374]); PANC1 FOLFIRINOX + RSL3 (mean ± 95% CI: 1.101 [0.6139–1.588]), including representative bands and histograms normalized to actin expression for PL45 (M), Panc04.03 (N), BxPC-3 (O), and PANC-1 (P). Abbreviations: Control (C), N-acetyl-cysteine (NAC), FOLFIRINOX (F), FOLFIRINOX + RSL3 (F+R), and FOLFIRINOX + RSL3 + N-acetyl-cysteine (F+R+NAC). White boxes: RSL3-sensitive PDAC-derived cell lines; black boxes: RSL3-resistant PDAC-derived cell lines. Statistical significance was considered at p < 0.05 (n.s. = not significant).

Techniques: Control, Western Blot, Expressing, Derivative Assay

(A) Tumor growth kinetics (left) and final tumor volume analysis (right) of PL45 xenografts treated with control (blue), FOLFIRINOX (orange), or FOLFIRINOX + RSL3 (green). Arrows indicate the final day of chemotherapy administration. (B) Representative photographs of mice bearing PL45 tumors (left) and excised tumors per treatment group (right). (C) Tumor growth kinetics (left) and final tumor volumes (right) of PANC-1 xenografts under identical treatment conditions. (D) Representative photographs of mice bearing PANC-1 tumors (left) and excised tumors (right). The ruler is marked in centimeters (cm). (E–F) Comparative efficacy of FOLFIRINOX monotherapy and FOLFIRINOX + RSL3 combination in PL45 and PANC-1 models, respectively. (G–H) Body weight monitoring over time for PL45 and PANC-1 xenografts, respectively. Red arrows denote FOLFIRINOX dosing days. (I) Immunohistochemical staining of xenografts for intracellular ROS, GPX4, and SOD2 expression. Scale bar represents 100 µm.

Journal: bioRxiv

Article Title: FOLFIRINOX Combined with GPX4 Inhibition Induces Ferroptosis and Defines Redox-Based Therapeutic Subgroups in Pancreatic Cancer

doi: 10.1101/2025.09.12.675778

Figure Lengend Snippet: (A) Tumor growth kinetics (left) and final tumor volume analysis (right) of PL45 xenografts treated with control (blue), FOLFIRINOX (orange), or FOLFIRINOX + RSL3 (green). Arrows indicate the final day of chemotherapy administration. (B) Representative photographs of mice bearing PL45 tumors (left) and excised tumors per treatment group (right). (C) Tumor growth kinetics (left) and final tumor volumes (right) of PANC-1 xenografts under identical treatment conditions. (D) Representative photographs of mice bearing PANC-1 tumors (left) and excised tumors (right). The ruler is marked in centimeters (cm). (E–F) Comparative efficacy of FOLFIRINOX monotherapy and FOLFIRINOX + RSL3 combination in PL45 and PANC-1 models, respectively. (G–H) Body weight monitoring over time for PL45 and PANC-1 xenografts, respectively. Red arrows denote FOLFIRINOX dosing days. (I) Immunohistochemical staining of xenografts for intracellular ROS, GPX4, and SOD2 expression. Scale bar represents 100 µm.

Techniques: Control, Immunohistochemical staining, Staining, Expressing

TWIST1 contributed to proliferation in PDAC cells. A . TWIST1, PKM2 and HK2 protein were significantly expressed in PL45, MIA-PACA-1, CFPAL-1 and PANC-1 cells. B . Knockdown of TWIST1 in TWISCFPAL-1 cell line. C . over-expression of TWIST1 in PANC-1 cell line. D . Red fluorescence represented EDU positive, which could be used as a representative of cell proliferation activity. Blue represented the nucleus. The magnification was 200 times. Cell proliferation was reduced by treatment with shRNA against TWIST1 and was promoted by over-expression of TWIST1. E . Clone formation number: knockdown TWIST1 inhibited cell cloning, while over-expression played a role in promoting cell cloning

Journal: Cancer Cell International

Article Title: TWIST1 regulates HK2 ubiquitination degradation to promote pancreatic cancer invasion and metastasis

doi: 10.1186/s12935-024-03583-z

Figure Lengend Snippet: TWIST1 contributed to proliferation in PDAC cells. A . TWIST1, PKM2 and HK2 protein were significantly expressed in PL45, MIA-PACA-1, CFPAL-1 and PANC-1 cells. B . Knockdown of TWIST1 in TWISCFPAL-1 cell line. C . over-expression of TWIST1 in PANC-1 cell line. D . Red fluorescence represented EDU positive, which could be used as a representative of cell proliferation activity. Blue represented the nucleus. The magnification was 200 times. Cell proliferation was reduced by treatment with shRNA against TWIST1 and was promoted by over-expression of TWIST1. E . Clone formation number: knockdown TWIST1 inhibited cell cloning, while over-expression played a role in promoting cell cloning

Article Snippet: PDAC cell lines (PL45, MIA-PACA-1, CFPAC-1, and PANC-1) were purchased from ATCC.

Techniques: Knockdown, Over Expression, Fluorescence, Activity Assay, shRNA, Cloning

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