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human colorectal cancer cell lines sw480  (ATCC)


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    ATCC human colorectal cancer cell lines sw480
    ACLY activity regulates MDR1 expression in colorectal cancer. (A) Transcript levels of ACLY and MDR1 (ABCB1) in colorectal cancer (red) and normal colon tissues (grey) analyzed using GEPIA (TCGA/GTEx datasets). (B) Immunoblot analysis of MDR1 in <t>SW480</t> and DLD1 cells treated with the ACLY inhibitor BMS-303141 (20 or 50 μM, 48 h). (C) Immunoblot analysis of ACLY and MDR1 in SW480 and DLD1 cells transduced with empty vector (pLV) or ACLY-overexpressing vector (pLV[Exp]-hACLY). (D) Immunoblot analysis of ACLY and MDR1 in control and ACLY-overexpressing cells treated with BMS-303141 (50 μM, 48 h). (E) Relative ABCB1 mRNA levels in control and ACLY-overexpressing cells, and in cells treated with BMS-303141. (F) Relative ACLY mRNA levels under the same conditions. Data are presented as mean ± SD (n = 3 unless otherwise indicated). Statistical significance was determined using unpaired two-tailed t-tests or one-way ANOVA with Tukey’s post hoc test. *P < 0.05; **P < 0.01; ***P < 0.001.
    Human Colorectal Cancer Cell Lines Sw480, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 7327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+cancer+cell+lines/SW480/pmc13142016-33-0-14
    Average 99 stars, based on 7327 article reviews
    human colorectal cancer cell lines sw480 - by Bioz Stars, 2026-09
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    1) Product Images from "Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability"

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    Journal: Neoplasia (New York, N.Y.)

    doi: 10.1016/j.neo.2026.101314

    ACLY activity regulates MDR1 expression in colorectal cancer. (A) Transcript levels of ACLY and MDR1 (ABCB1) in colorectal cancer (red) and normal colon tissues (grey) analyzed using GEPIA (TCGA/GTEx datasets). (B) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (20 or 50 μM, 48 h). (C) Immunoblot analysis of ACLY and MDR1 in SW480 and DLD1 cells transduced with empty vector (pLV) or ACLY-overexpressing vector (pLV[Exp]-hACLY). (D) Immunoblot analysis of ACLY and MDR1 in control and ACLY-overexpressing cells treated with BMS-303141 (50 μM, 48 h). (E) Relative ABCB1 mRNA levels in control and ACLY-overexpressing cells, and in cells treated with BMS-303141. (F) Relative ACLY mRNA levels under the same conditions. Data are presented as mean ± SD (n = 3 unless otherwise indicated). Statistical significance was determined using unpaired two-tailed t-tests or one-way ANOVA with Tukey’s post hoc test. *P < 0.05; **P < 0.01; ***P < 0.001.
    Figure Legend Snippet: ACLY activity regulates MDR1 expression in colorectal cancer. (A) Transcript levels of ACLY and MDR1 (ABCB1) in colorectal cancer (red) and normal colon tissues (grey) analyzed using GEPIA (TCGA/GTEx datasets). (B) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (20 or 50 μM, 48 h). (C) Immunoblot analysis of ACLY and MDR1 in SW480 and DLD1 cells transduced with empty vector (pLV) or ACLY-overexpressing vector (pLV[Exp]-hACLY). (D) Immunoblot analysis of ACLY and MDR1 in control and ACLY-overexpressing cells treated with BMS-303141 (50 μM, 48 h). (E) Relative ABCB1 mRNA levels in control and ACLY-overexpressing cells, and in cells treated with BMS-303141. (F) Relative ACLY mRNA levels under the same conditions. Data are presented as mean ± SD (n = 3 unless otherwise indicated). Statistical significance was determined using unpaired two-tailed t-tests or one-way ANOVA with Tukey’s post hoc test. *P < 0.05; **P < 0.01; ***P < 0.001.

    Techniques Used: Activity Assay, Expressing, Western Blot, Transduction, Plasmid Preparation, Control, Two Tailed Test

    ACLY activity modulates histone acetylation and MDR1 expression. (A) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the histone deacetylase inhibitor vorinostat (VOR; 0.5 μM for SW480 and 3.5 μM for DLD1) or DMSO for 24 h. Representative blots and densitometric quantification relative to control are shown. (B) Immunoblot analysis of acetylated histone H3 (H3K9ac) and histone H4 (H4K16ac) in SW480 wild-type (WT) and ACLY-overexpressing (OE) cells treated with vehicle or the ACLY inhibitor BMS-303141 (50 μM, 48 h). (C) Immunoblot analysis of H3K9ac and H4K16ac in DLD1 cells under the same conditions. β-actin was used as a loading control. Data are presented as mean ± SD (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.
    Figure Legend Snippet: ACLY activity modulates histone acetylation and MDR1 expression. (A) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the histone deacetylase inhibitor vorinostat (VOR; 0.5 μM for SW480 and 3.5 μM for DLD1) or DMSO for 24 h. Representative blots and densitometric quantification relative to control are shown. (B) Immunoblot analysis of acetylated histone H3 (H3K9ac) and histone H4 (H4K16ac) in SW480 wild-type (WT) and ACLY-overexpressing (OE) cells treated with vehicle or the ACLY inhibitor BMS-303141 (50 μM, 48 h). (C) Immunoblot analysis of H3K9ac and H4K16ac in DLD1 cells under the same conditions. β-actin was used as a loading control. Data are presented as mean ± SD (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Techniques Used: Activity Assay, Expressing, Western Blot, Histone Deacetylase Assay, Control, Two Tailed Test

    ACLY expression is associated with resistance-related transcriptional programs in colorectal cancer. (A) Correlation analysis between ACLY expression and a gene set associated with lipid metabolism (ACLY, ACSS2, ACSS1, FASN, SREBP1) and drug transport pathways (ABCB1, ABCC2, ABCG5, EpCAM, CD24) in colorectal cancer samples using GEPIA2 (TCGA dataset). (B) Schematic representation of a proposed model linking ACLY-dependent acetyl-CoA production to histone acetylation and transcriptional regulation in CRC cells. (C) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells overexpressing ACLY compared with empty vector controls. (D) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (50 μM) compared with vehicle-treated controls. Gene expression levels were determined by qPCR and normalized to ACTB. Data are presented as mean ± SEM (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.
    Figure Legend Snippet: ACLY expression is associated with resistance-related transcriptional programs in colorectal cancer. (A) Correlation analysis between ACLY expression and a gene set associated with lipid metabolism (ACLY, ACSS2, ACSS1, FASN, SREBP1) and drug transport pathways (ABCB1, ABCC2, ABCG5, EpCAM, CD24) in colorectal cancer samples using GEPIA2 (TCGA dataset). (B) Schematic representation of a proposed model linking ACLY-dependent acetyl-CoA production to histone acetylation and transcriptional regulation in CRC cells. (C) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells overexpressing ACLY compared with empty vector controls. (D) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (50 μM) compared with vehicle-treated controls. Gene expression levels were determined by qPCR and normalized to ACTB. Data are presented as mean ± SEM (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Techniques Used: Expressing, Drug Transport Assay, Plasmid Preparation, Gene Expression, Two Tailed Test

    Vitamin C induces coordinated changes in metabolic and chromatin-associated pathways in colorectal cancer cells. (A) Gene Ontology (GO) enrichment analysis of proteins differentially expressed following vitamin C treatment (5 mM, 4 h). (B) Volcano plot showing significantly upregulated and downregulated proteins (log₂ fold change > 1, p < 0.05). (C) KEGG pathway enrichment analysis highlighting pathways related to chromatin organization, DNA replication, nucleotide metabolism, and cell cycle regulation. (D) GO Cellular Component analysis showing enrichment of chromatin-associated complexes, including transcription regulator complexes, histone acetyltransferase-containing complexes, and Polycomb group (PcG) assemblies. (E) Heatmap representation of differentially expressed chromatin-associated proteins in control and vitamin C-treated cells. Proteomic analysis was performed in SW480 and DLD1 cells using label-free LC–MS/MS (diaPASEF). Data represent combined analysis of both cell lines.
    Figure Legend Snippet: Vitamin C induces coordinated changes in metabolic and chromatin-associated pathways in colorectal cancer cells. (A) Gene Ontology (GO) enrichment analysis of proteins differentially expressed following vitamin C treatment (5 mM, 4 h). (B) Volcano plot showing significantly upregulated and downregulated proteins (log₂ fold change > 1, p < 0.05). (C) KEGG pathway enrichment analysis highlighting pathways related to chromatin organization, DNA replication, nucleotide metabolism, and cell cycle regulation. (D) GO Cellular Component analysis showing enrichment of chromatin-associated complexes, including transcription regulator complexes, histone acetyltransferase-containing complexes, and Polycomb group (PcG) assemblies. (E) Heatmap representation of differentially expressed chromatin-associated proteins in control and vitamin C-treated cells. Proteomic analysis was performed in SW480 and DLD1 cells using label-free LC–MS/MS (diaPASEF). Data represent combined analysis of both cell lines.

    Techniques Used: Control, Liquid Chromatography with Mass Spectroscopy, Data-independent acquisition

    Metabolic and epigenetic consequences of vitamin C treatment in colorectal cancer cells. (A) Quantification of ¹³C-glucose-derived citrate in SW480 and DLD1 cells treated with vitamin C (5 mM) for 4 h (n = 3). (B) Immunoblot analysis of total ACLY and phosphorylated ACLY at Ser455 following vitamin C treatment (5 mM) (n = 3). (C) Immunoblot analysis and quantification of acetylated histone H4 (AcH4K16) and histone H3 (AcH3K9) in SW480 and DLD1 cells after vitamin C exposure (n = 3). (D) MDR1 (ABCB1) protein levels in SW480 and DLD1 cells treated with vitamin C (5 mM), quantified relative to vehicle control (n = 3). (E) Relative ACLY and ABCB1 mRNA expression determined by qPCR after 6 h of vitamin C treatment (5 mM) in SW480 and DLD1 cells (n = 3). Data are presented as mean ± SEM. Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.
    Figure Legend Snippet: Metabolic and epigenetic consequences of vitamin C treatment in colorectal cancer cells. (A) Quantification of ¹³C-glucose-derived citrate in SW480 and DLD1 cells treated with vitamin C (5 mM) for 4 h (n = 3). (B) Immunoblot analysis of total ACLY and phosphorylated ACLY at Ser455 following vitamin C treatment (5 mM) (n = 3). (C) Immunoblot analysis and quantification of acetylated histone H4 (AcH4K16) and histone H3 (AcH3K9) in SW480 and DLD1 cells after vitamin C exposure (n = 3). (D) MDR1 (ABCB1) protein levels in SW480 and DLD1 cells treated with vitamin C (5 mM), quantified relative to vehicle control (n = 3). (E) Relative ACLY and ABCB1 mRNA expression determined by qPCR after 6 h of vitamin C treatment (5 mM) in SW480 and DLD1 cells (n = 3). Data are presented as mean ± SEM. Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Techniques Used: Derivative Assay, Western Blot, Control, Expressing, Two Tailed Test

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    ACLY activity regulates MDR1 expression in colorectal cancer. (A) Transcript levels of ACLY and MDR1 (ABCB1) in colorectal cancer (red) and normal colon tissues (grey) analyzed using GEPIA (TCGA/GTEx datasets). (B) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (20 or 50 μM, 48 h). (C) Immunoblot analysis of ACLY and MDR1 in SW480 and DLD1 cells transduced with empty vector (pLV) or ACLY-overexpressing vector (pLV[Exp]-hACLY). (D) Immunoblot analysis of ACLY and MDR1 in control and ACLY-overexpressing cells treated with BMS-303141 (50 μM, 48 h). (E) Relative ABCB1 mRNA levels in control and ACLY-overexpressing cells, and in cells treated with BMS-303141. (F) Relative ACLY mRNA levels under the same conditions. Data are presented as mean ± SD (n = 3 unless otherwise indicated). Statistical significance was determined using unpaired two-tailed t-tests or one-way ANOVA with Tukey’s post hoc test. *P < 0.05; **P < 0.01; ***P < 0.001.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    doi: 10.1016/j.neo.2026.101314

    Figure Lengend Snippet: ACLY activity regulates MDR1 expression in colorectal cancer. (A) Transcript levels of ACLY and MDR1 (ABCB1) in colorectal cancer (red) and normal colon tissues (grey) analyzed using GEPIA (TCGA/GTEx datasets). (B) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (20 or 50 μM, 48 h). (C) Immunoblot analysis of ACLY and MDR1 in SW480 and DLD1 cells transduced with empty vector (pLV) or ACLY-overexpressing vector (pLV[Exp]-hACLY). (D) Immunoblot analysis of ACLY and MDR1 in control and ACLY-overexpressing cells treated with BMS-303141 (50 μM, 48 h). (E) Relative ABCB1 mRNA levels in control and ACLY-overexpressing cells, and in cells treated with BMS-303141. (F) Relative ACLY mRNA levels under the same conditions. Data are presented as mean ± SD (n = 3 unless otherwise indicated). Statistical significance was determined using unpaired two-tailed t-tests or one-way ANOVA with Tukey’s post hoc test. *P < 0.05; **P < 0.01; ***P < 0.001.

    Article Snippet: Human colorectal cancer cell lines SW480 (KRASG12V) and DLD1 (KRASG13D) were obtained from the American Type Culture Collection (ATCC) and authenticated by short tandem repeat profiling.

    Techniques: Activity Assay, Expressing, Western Blot, Transduction, Plasmid Preparation, Control, Two Tailed Test

    ACLY activity modulates histone acetylation and MDR1 expression. (A) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the histone deacetylase inhibitor vorinostat (VOR; 0.5 μM for SW480 and 3.5 μM for DLD1) or DMSO for 24 h. Representative blots and densitometric quantification relative to control are shown. (B) Immunoblot analysis of acetylated histone H3 (H3K9ac) and histone H4 (H4K16ac) in SW480 wild-type (WT) and ACLY-overexpressing (OE) cells treated with vehicle or the ACLY inhibitor BMS-303141 (50 μM, 48 h). (C) Immunoblot analysis of H3K9ac and H4K16ac in DLD1 cells under the same conditions. β-actin was used as a loading control. Data are presented as mean ± SD (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    doi: 10.1016/j.neo.2026.101314

    Figure Lengend Snippet: ACLY activity modulates histone acetylation and MDR1 expression. (A) Immunoblot analysis of MDR1 in SW480 and DLD1 cells treated with the histone deacetylase inhibitor vorinostat (VOR; 0.5 μM for SW480 and 3.5 μM for DLD1) or DMSO for 24 h. Representative blots and densitometric quantification relative to control are shown. (B) Immunoblot analysis of acetylated histone H3 (H3K9ac) and histone H4 (H4K16ac) in SW480 wild-type (WT) and ACLY-overexpressing (OE) cells treated with vehicle or the ACLY inhibitor BMS-303141 (50 μM, 48 h). (C) Immunoblot analysis of H3K9ac and H4K16ac in DLD1 cells under the same conditions. β-actin was used as a loading control. Data are presented as mean ± SD (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Article Snippet: Human colorectal cancer cell lines SW480 (KRASG12V) and DLD1 (KRASG13D) were obtained from the American Type Culture Collection (ATCC) and authenticated by short tandem repeat profiling.

    Techniques: Activity Assay, Expressing, Western Blot, Histone Deacetylase Assay, Control, Two Tailed Test

    ACLY expression is associated with resistance-related transcriptional programs in colorectal cancer. (A) Correlation analysis between ACLY expression and a gene set associated with lipid metabolism (ACLY, ACSS2, ACSS1, FASN, SREBP1) and drug transport pathways (ABCB1, ABCC2, ABCG5, EpCAM, CD24) in colorectal cancer samples using GEPIA2 (TCGA dataset). (B) Schematic representation of a proposed model linking ACLY-dependent acetyl-CoA production to histone acetylation and transcriptional regulation in CRC cells. (C) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells overexpressing ACLY compared with empty vector controls. (D) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (50 μM) compared with vehicle-treated controls. Gene expression levels were determined by qPCR and normalized to ACTB. Data are presented as mean ± SEM (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    doi: 10.1016/j.neo.2026.101314

    Figure Lengend Snippet: ACLY expression is associated with resistance-related transcriptional programs in colorectal cancer. (A) Correlation analysis between ACLY expression and a gene set associated with lipid metabolism (ACLY, ACSS2, ACSS1, FASN, SREBP1) and drug transport pathways (ABCB1, ABCC2, ABCG5, EpCAM, CD24) in colorectal cancer samples using GEPIA2 (TCGA dataset). (B) Schematic representation of a proposed model linking ACLY-dependent acetyl-CoA production to histone acetylation and transcriptional regulation in CRC cells. (C) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells overexpressing ACLY compared with empty vector controls. (D) Relative mRNA expression of EpCAM, ABCC2, and CD24 in SW480 and DLD1 cells treated with the ACLY inhibitor BMS-303141 (50 μM) compared with vehicle-treated controls. Gene expression levels were determined by qPCR and normalized to ACTB. Data are presented as mean ± SEM (n = 3). Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Article Snippet: Human colorectal cancer cell lines SW480 (KRASG12V) and DLD1 (KRASG13D) were obtained from the American Type Culture Collection (ATCC) and authenticated by short tandem repeat profiling.

    Techniques: Expressing, Drug Transport Assay, Plasmid Preparation, Gene Expression, Two Tailed Test

    Vitamin C induces coordinated changes in metabolic and chromatin-associated pathways in colorectal cancer cells. (A) Gene Ontology (GO) enrichment analysis of proteins differentially expressed following vitamin C treatment (5 mM, 4 h). (B) Volcano plot showing significantly upregulated and downregulated proteins (log₂ fold change > 1, p < 0.05). (C) KEGG pathway enrichment analysis highlighting pathways related to chromatin organization, DNA replication, nucleotide metabolism, and cell cycle regulation. (D) GO Cellular Component analysis showing enrichment of chromatin-associated complexes, including transcription regulator complexes, histone acetyltransferase-containing complexes, and Polycomb group (PcG) assemblies. (E) Heatmap representation of differentially expressed chromatin-associated proteins in control and vitamin C-treated cells. Proteomic analysis was performed in SW480 and DLD1 cells using label-free LC–MS/MS (diaPASEF). Data represent combined analysis of both cell lines.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    doi: 10.1016/j.neo.2026.101314

    Figure Lengend Snippet: Vitamin C induces coordinated changes in metabolic and chromatin-associated pathways in colorectal cancer cells. (A) Gene Ontology (GO) enrichment analysis of proteins differentially expressed following vitamin C treatment (5 mM, 4 h). (B) Volcano plot showing significantly upregulated and downregulated proteins (log₂ fold change > 1, p < 0.05). (C) KEGG pathway enrichment analysis highlighting pathways related to chromatin organization, DNA replication, nucleotide metabolism, and cell cycle regulation. (D) GO Cellular Component analysis showing enrichment of chromatin-associated complexes, including transcription regulator complexes, histone acetyltransferase-containing complexes, and Polycomb group (PcG) assemblies. (E) Heatmap representation of differentially expressed chromatin-associated proteins in control and vitamin C-treated cells. Proteomic analysis was performed in SW480 and DLD1 cells using label-free LC–MS/MS (diaPASEF). Data represent combined analysis of both cell lines.

    Article Snippet: Human colorectal cancer cell lines SW480 (KRASG12V) and DLD1 (KRASG13D) were obtained from the American Type Culture Collection (ATCC) and authenticated by short tandem repeat profiling.

    Techniques: Control, Liquid Chromatography with Mass Spectroscopy, Data-independent acquisition

    Metabolic and epigenetic consequences of vitamin C treatment in colorectal cancer cells. (A) Quantification of ¹³C-glucose-derived citrate in SW480 and DLD1 cells treated with vitamin C (5 mM) for 4 h (n = 3). (B) Immunoblot analysis of total ACLY and phosphorylated ACLY at Ser455 following vitamin C treatment (5 mM) (n = 3). (C) Immunoblot analysis and quantification of acetylated histone H4 (AcH4K16) and histone H3 (AcH3K9) in SW480 and DLD1 cells after vitamin C exposure (n = 3). (D) MDR1 (ABCB1) protein levels in SW480 and DLD1 cells treated with vitamin C (5 mM), quantified relative to vehicle control (n = 3). (E) Relative ACLY and ABCB1 mRNA expression determined by qPCR after 6 h of vitamin C treatment (5 mM) in SW480 and DLD1 cells (n = 3). Data are presented as mean ± SEM. Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Metabolic regulation of histone acetylation by ACLY supports MDR1 expression in colorectal cancer and highlights a targetable vulnerability

    doi: 10.1016/j.neo.2026.101314

    Figure Lengend Snippet: Metabolic and epigenetic consequences of vitamin C treatment in colorectal cancer cells. (A) Quantification of ¹³C-glucose-derived citrate in SW480 and DLD1 cells treated with vitamin C (5 mM) for 4 h (n = 3). (B) Immunoblot analysis of total ACLY and phosphorylated ACLY at Ser455 following vitamin C treatment (5 mM) (n = 3). (C) Immunoblot analysis and quantification of acetylated histone H4 (AcH4K16) and histone H3 (AcH3K9) in SW480 and DLD1 cells after vitamin C exposure (n = 3). (D) MDR1 (ABCB1) protein levels in SW480 and DLD1 cells treated with vitamin C (5 mM), quantified relative to vehicle control (n = 3). (E) Relative ACLY and ABCB1 mRNA expression determined by qPCR after 6 h of vitamin C treatment (5 mM) in SW480 and DLD1 cells (n = 3). Data are presented as mean ± SEM. Statistical significance was determined using unpaired two-tailed t-tests. *P < 0.05; **P < 0.01; ***P < 0.001.

    Article Snippet: Human colorectal cancer cell lines SW480 (KRASG12V) and DLD1 (KRASG13D) were obtained from the American Type Culture Collection (ATCC) and authenticated by short tandem repeat profiling.

    Techniques: Derivative Assay, Western Blot, Control, Expressing, Two Tailed Test

    Specific IFN-γ and TNF-α release of T lymphocytes transduced with TIM-3-silenced HER2-specific chimeric antigen receptor (CAR) or HER2-specific CAR. (A, B) TIM-3-silenced CAR-T cells and control T cells were co-incubated with Galectin-9 + or Galectin-9 – SKOV3 tumor cells (E:T ratio 5:1 or 10:1). At 20 h after coculture, a specific enzyme-linked immunosorbent assay was used to analyze the supernatant for IFN-γ cytokine-release. Results were presented as mean ± standard deviation. (C, D) The detection of TNF-α in the same culture supernatant. Results were presented as mean ± standard deviation. ∗ P < 0.05 and ∗∗ P < 0.01.

    Journal: Genes & Diseases

    Article Title: Blockade of co-inhibitory receptor immune checkpoint protein TIM3/CD366 augments the anti-cancer activity of CAR-T therapy in solid tumors: An ovarian cancer example

    doi: 10.1016/j.gendis.2025.101978

    Figure Lengend Snippet: Specific IFN-γ and TNF-α release of T lymphocytes transduced with TIM-3-silenced HER2-specific chimeric antigen receptor (CAR) or HER2-specific CAR. (A, B) TIM-3-silenced CAR-T cells and control T cells were co-incubated with Galectin-9 + or Galectin-9 – SKOV3 tumor cells (E:T ratio 5:1 or 10:1). At 20 h after coculture, a specific enzyme-linked immunosorbent assay was used to analyze the supernatant for IFN-γ cytokine-release. Results were presented as mean ± standard deviation. (C, D) The detection of TNF-α in the same culture supernatant. Results were presented as mean ± standard deviation. ∗ P < 0.05 and ∗∗ P < 0.01.

    Article Snippet: Human cervical cancer cell line HeLa, lentivirus packaging cell line HEK 293TD, and human ovarian cancer cell line SKOV3 were purchased from American Type Culture Collection (Manassas, Virginia, USA) and cultured in Dulbecco's modified Eagle's medium (Invitrogen, Grand Island, New York) supplemented with 10% heat-inactivated fetal bovine serum.

    Techniques: Transduction, Control, Incubation, Enzyme-linked Immunosorbent Assay, Standard Deviation

    TIM-3 silencing augmented the anti-tumor activity of chimeric antigen receptor-T (CAR-T) cells in vivo . 2 × 10 6 SKOV3 tumor cells expressing luciferase were intraperitoneally inoculated in a xenograft mouse model, and 7 days after inoculation, the 2 × 10 6 HER2-specific CAR-T kdTim-3 cells or CAR-T cells, or untreated T cells were intraperitoneally administered. (A, B) Tumor growth was monitored using an in vivo imaging system. (C) Survival curve of 80-day post-treatment. ∗ P < 0.05 and ∗∗ P < 0.01.

    Journal: Genes & Diseases

    Article Title: Blockade of co-inhibitory receptor immune checkpoint protein TIM3/CD366 augments the anti-cancer activity of CAR-T therapy in solid tumors: An ovarian cancer example

    doi: 10.1016/j.gendis.2025.101978

    Figure Lengend Snippet: TIM-3 silencing augmented the anti-tumor activity of chimeric antigen receptor-T (CAR-T) cells in vivo . 2 × 10 6 SKOV3 tumor cells expressing luciferase were intraperitoneally inoculated in a xenograft mouse model, and 7 days after inoculation, the 2 × 10 6 HER2-specific CAR-T kdTim-3 cells or CAR-T cells, or untreated T cells were intraperitoneally administered. (A, B) Tumor growth was monitored using an in vivo imaging system. (C) Survival curve of 80-day post-treatment. ∗ P < 0.05 and ∗∗ P < 0.01.

    Article Snippet: Human cervical cancer cell line HeLa, lentivirus packaging cell line HEK 293TD, and human ovarian cancer cell line SKOV3 were purchased from American Type Culture Collection (Manassas, Virginia, USA) and cultured in Dulbecco's modified Eagle's medium (Invitrogen, Grand Island, New York) supplemented with 10% heat-inactivated fetal bovine serum.

    Techniques: Activity Assay, In Vivo, Expressing, Luciferase, In Vivo Imaging

    Efficiency of XBP1 gene silencing in MCF7 and MDA-MB-231 cells. XBP1 expression was evaluated in MCF7 and MDA-MB-231 cells at the mRNA and protein levels by qPCR and western blot analysis, respectively. Protein expression was assessed following shRNA-2-mediated silencing. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis of qPCR data was performed using one-way ANOVA, whereas western blot data were analyzed using Student’s t-test. ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Efficiency of XBP1 gene silencing in MCF7 and MDA-MB-231 cells. XBP1 expression was evaluated in MCF7 and MDA-MB-231 cells at the mRNA and protein levels by qPCR and western blot analysis, respectively. Protein expression was assessed following shRNA-2-mediated silencing. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis of qPCR data was performed using one-way ANOVA, whereas western blot data were analyzed using Student’s t-test. ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Expressing, Western Blot, shRNA

    Representative microscopic images of transduced cells. Upper panels: MCF7; lower panels: MDA-MB-231. ( A ) Brightfield and ( B ) TurboGFP fluorescence images demonstrating transduction in the indicated cell lines. Images are representative of three independent experiments with similar results and were captured at 10X magnification, scale bars: 200 μm

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Representative microscopic images of transduced cells. Upper panels: MCF7; lower panels: MDA-MB-231. ( A ) Brightfield and ( B ) TurboGFP fluorescence images demonstrating transduction in the indicated cell lines. Images are representative of three independent experiments with similar results and were captured at 10X magnification, scale bars: 200 μm

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Fluorescence, Transduction

    Que-induced cytotoxicity and the combined effects of Que and XBP1 silencing on breast cancer cells viability. ( A , B ) Cell viability of MCF7 and MDA-MB-231 cells after treatment with increasing concentrations of Que (0–200 µM) for 24, 48, and 72 h. ( C ) Cell viability of MCF7 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups at 24, 48, and 72 h, using Que at its IC 50 concentration (154.262 µM). ( D ) Cell viability of MDA-MB-231 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups at 24, 48, and 72 h, using Que at its IC 50 concentration (192.103 µM). Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis of cell viability was performed using one-way ANOVA followed by Tukey’s post-hoc test. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Que-induced cytotoxicity and the combined effects of Que and XBP1 silencing on breast cancer cells viability. ( A , B ) Cell viability of MCF7 and MDA-MB-231 cells after treatment with increasing concentrations of Que (0–200 µM) for 24, 48, and 72 h. ( C ) Cell viability of MCF7 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups at 24, 48, and 72 h, using Que at its IC 50 concentration (154.262 µM). ( D ) Cell viability of MDA-MB-231 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups at 24, 48, and 72 h, using Que at its IC 50 concentration (192.103 µM). Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis of cell viability was performed using one-way ANOVA followed by Tukey’s post-hoc test. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001; **** p ≤ 0.0001

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Control, Concentration Assay

    Colony formation capacity of MCF7 and MDA-MB-231 cells following Que treatment and XBP1 silencing. Representative colony images and quantitative colony counts are shown for MCF7 and MDA-MB-231 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups. Que was used at the IC 50 concentration determined for each cell line. Colonies were counted manually. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Colony formation capacity of MCF7 and MDA-MB-231 cells following Que treatment and XBP1 silencing. Representative colony images and quantitative colony counts are shown for MCF7 and MDA-MB-231 cells in the Control, Que, XBP1(-), and XBP1(-) + Que groups. Que was used at the IC 50 concentration determined for each cell line. Colonies were counted manually. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Control, Concentration Assay

    Effects of Que, XBP1 silencing, and their combination on expression levels of apoptosis-associated genes in MCF7 and MDA-MB-231 breast cancer cell lines. ( A ) Relative mRNA expression levels of BAX, BCL2, CASP3, CASP7, CASP8, CASP9, CYCS, and FADD were analyzed using qPCR in the Control, Que, XBP1(-), and XBP1(-) + Que groups. ( B ) Protein level expressions of CASP3, CASP8, and CASP9 were evaluated by western blot analysis in the same treatment groups. Bar graphs in panel B represent densitometric quantification of western blot bands performed using ImageJ and normalized to GAPDH. Que was applied at the IC 50 concentration determined for each cell line. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Effects of Que, XBP1 silencing, and their combination on expression levels of apoptosis-associated genes in MCF7 and MDA-MB-231 breast cancer cell lines. ( A ) Relative mRNA expression levels of BAX, BCL2, CASP3, CASP7, CASP8, CASP9, CYCS, and FADD were analyzed using qPCR in the Control, Que, XBP1(-), and XBP1(-) + Que groups. ( B ) Protein level expressions of CASP3, CASP8, and CASP9 were evaluated by western blot analysis in the same treatment groups. Bar graphs in panel B represent densitometric quantification of western blot bands performed using ImageJ and normalized to GAPDH. Que was applied at the IC 50 concentration determined for each cell line. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Expressing, Control, Western Blot, Concentration Assay

    Effects of Que, XBP1 silencing, and their combination on EMT- and metastasis-associated genes in MCF7 and MDA-MB-231 breast cancer cell lines. ( A ) Relative mRNA expression levels of EMT/metastasis-associated markers were analyzed by qPCR in the Control, Que, XBP1(-), and XBP1(-) + Que groups. ( B ) Protein level expressions of CDH1 and CDH2 were evaluated by western blot analysis in the same treatment groups. Bar graphs in panel B represent densitometric quantification of western blot bands performed using ImageJ and normalized to GAPDH. Que was applied at the IC 50 concentration determined for each cell line. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Effects of Que, XBP1 silencing, and their combination on EMT- and metastasis-associated genes in MCF7 and MDA-MB-231 breast cancer cell lines. ( A ) Relative mRNA expression levels of EMT/metastasis-associated markers were analyzed by qPCR in the Control, Que, XBP1(-), and XBP1(-) + Que groups. ( B ) Protein level expressions of CDH1 and CDH2 were evaluated by western blot analysis in the same treatment groups. Bar graphs in panel B represent densitometric quantification of western blot bands performed using ImageJ and normalized to GAPDH. Que was applied at the IC 50 concentration determined for each cell line. Data are presented as mean ± SEM from three independent experiments ( n = 3). Statistical analysis was performed using one-way ANOVA. * p ≤ 0.05; ** p ≤ 0.01; *** p ≤ 0.001

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: Expressing, Control, Western Blot, Concentration Assay

    Proposed mechanistic overview of the combined treatment with Que and XBP1 silencing in MCF7 and MDA-MB-231 breast cancer cells. The schematic summarizes the treatment-associated reduction in cell viability, suppression of colony formation, modulation of apoptosis-associated markers, and EMT-related molecular changes observed in the present study. The relationships shown are presented as a conceptual summary of the current findings

    Journal: 3 Biotech

    Article Title: XBP1 gene silencing augments quercetin-induced apoptosis and anti-metastatic activity in breast cancer cell lines

    doi: 10.1007/s13205-026-04923-8

    Figure Lengend Snippet: Proposed mechanistic overview of the combined treatment with Que and XBP1 silencing in MCF7 and MDA-MB-231 breast cancer cells. The schematic summarizes the treatment-associated reduction in cell viability, suppression of colony formation, modulation of apoptosis-associated markers, and EMT-related molecular changes observed in the present study. The relationships shown are presented as a conceptual summary of the current findings

    Article Snippet: Human breast cancer cell lines MCF7 (ATCC ® HTB-22TM) and MDA-MB-231 (ATCC ® HTB-26TM) were purchased from the American Type Culture Collection (ATCC, USA).

    Techniques: