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human colon cancer caco 2 cell line  (ATCC)


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    ATCC human colon cancer caco 2 cell line
    The cytotoxic effect of Myr-B peptide against human colon <t>cancer</t> <t>Caco-2</t> cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.
    Human Colon Cancer Caco 2 Cell Line, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 14954 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+colon+cancer+cell+lines+caco+2/pmc13163312-219-1-7?v=ATCC
    Average 99 stars, based on 14954 article reviews
    human colon cancer caco 2 cell line - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights"

    Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms27093918

    The cytotoxic effect of Myr-B peptide against human colon cancer Caco-2 cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.
    Figure Legend Snippet: The cytotoxic effect of Myr-B peptide against human colon cancer Caco-2 cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.

    Techniques Used: MTT Assay, Incubation, Negative Control, Positive Control

    Evaluation of Myr-B peptide-induced death of human cervical cancer HeLa ( a ) and colon cancer Caco-2 ( b ) cells. Cell membrane integrity was assessed through lactate dehydrogenase (LDH) release from untreated HeLa or Caco-2 cells (negative control) after 3 h exposure of HeLa and Caco-2 cells to their respective IC 50 doses of Myr-B peptide (38 μM and 50 μM, respectively) and from HeLa or Caco-2 cells treated with a lysis solution to release all LDH (positive control). The exposure to Pep-B was carried out under the same conditions as the corresponding treatment with the Myr-B peptide for each cancer cell line. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; *** p -value < 0.001; **** p -value < 0.0001.
    Figure Legend Snippet: Evaluation of Myr-B peptide-induced death of human cervical cancer HeLa ( a ) and colon cancer Caco-2 ( b ) cells. Cell membrane integrity was assessed through lactate dehydrogenase (LDH) release from untreated HeLa or Caco-2 cells (negative control) after 3 h exposure of HeLa and Caco-2 cells to their respective IC 50 doses of Myr-B peptide (38 μM and 50 μM, respectively) and from HeLa or Caco-2 cells treated with a lysis solution to release all LDH (positive control). The exposure to Pep-B was carried out under the same conditions as the corresponding treatment with the Myr-B peptide for each cancer cell line. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; *** p -value < 0.001; **** p -value < 0.0001.

    Techniques Used: Membrane, Negative Control, Lysis, Positive Control

    SEM analysis of Myr-B peptide-induced effects on human colon cancer Caco-2 cells. SEM micrographs (acquired and processed using JEOL inTouchScope Interface software) of untreated Caco-2 cells (negative control) ( a , b ), Caco-2 cells after 3 h exposure to 50 μM Myr-B ( c , d ) and 50 μM Pep-B ( e , f ) and Caco-2 cells treated with 2% NaN 3 (positive control) ( g , h ). Magnification and scale bars = ( a – d ) 1500× and 10 μm, respectively; ( e – h ) 10,000× and 1 μm, respectively.
    Figure Legend Snippet: SEM analysis of Myr-B peptide-induced effects on human colon cancer Caco-2 cells. SEM micrographs (acquired and processed using JEOL inTouchScope Interface software) of untreated Caco-2 cells (negative control) ( a , b ), Caco-2 cells after 3 h exposure to 50 μM Myr-B ( c , d ) and 50 μM Pep-B ( e , f ) and Caco-2 cells treated with 2% NaN 3 (positive control) ( g , h ). Magnification and scale bars = ( a – d ) 1500× and 10 μm, respectively; ( e – h ) 10,000× and 1 μm, respectively.

    Techniques Used: Software, Negative Control, Positive Control



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    ATCC human colon cancer caco 2 cell line
    The cytotoxic effect of Myr-B peptide against human colon <t>cancer</t> <t>Caco-2</t> cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.
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    ATCC human colon cancer epithelial cell line caco2
    Zinc as an Active Principle of ZPT. (A) Chemical structures of dipyrithione and sodium pyrithione are shown. The activities of varying concentrations of ZPT, ZnSO 4 , dipyrithione and sodium pyrithione to inhibit the hydrolysis of Compound 1 by purified PLCε were measured as described in Methods. ( B ) The activities of varying concentrations of ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε, PLCβ4, PLCδ1 or PLCγ1 were measured as described in Methods. (C) The activities of 5 µM ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε were measured in the presence of varying concentrations of sodium pyrithione. ( D ) <t>Caco2</t> cells were treated with 5 µM ZnSO 4 in the presence or absence of 5 µM sodium pyrithione or with 5 µM ZPT for 30 min. Intracellular Zn 2+ concentrations of the treated cells were measured by using Zinquin ethyl ester as described in Methods. The values obtained are expressed as fold changes over the average value of untreated cells. All the experiments described above were performed three times in duplicates.
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    ATCC human colon cancer caco 2 cell line atcc ref htb 37
    Zinc as an Active Principle of ZPT. (A) Chemical structures of dipyrithione and sodium pyrithione are shown. The activities of varying concentrations of ZPT, ZnSO 4 , dipyrithione and sodium pyrithione to inhibit the hydrolysis of Compound 1 by purified PLCε were measured as described in Methods. ( B ) The activities of varying concentrations of ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε, PLCβ4, PLCδ1 or PLCγ1 were measured as described in Methods. (C) The activities of 5 µM ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε were measured in the presence of varying concentrations of sodium pyrithione. ( D ) <t>Caco2</t> cells were treated with 5 µM ZnSO 4 in the presence or absence of 5 µM sodium pyrithione or with 5 µM ZPT for 30 min. Intracellular Zn 2+ concentrations of the treated cells were measured by using Zinquin ethyl ester as described in Methods. The values obtained are expressed as fold changes over the average value of untreated cells. All the experiments described above were performed three times in duplicates.
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    Image Search Results


    The cytotoxic effect of Myr-B peptide against human colon cancer Caco-2 cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.

    Journal: International Journal of Molecular Sciences

    Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

    doi: 10.3390/ijms27093918

    Figure Lengend Snippet: The cytotoxic effect of Myr-B peptide against human colon cancer Caco-2 cells. Cell viability was assessed using the MTT assay for the Caco-2 cell line after 3 h and 24 h of incubation with N-myristoylated Myr-B peptide ( a ) and corresponding non-myristoylated Pep-B peptide ( b ). Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated Caco-2 cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: ** adjusted p -value < 0.01; **** p -value < 0.0001.

    Article Snippet: The human colon cancer Caco-2 cell line (ATCC HTB-37) was cultured in DMEM supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, 1% Non-Essential Amino Acids and 1% sodium pyruvate and maintained at 37 °C in a humidified incubator with 5% CO 2 [ ].

    Techniques: MTT Assay, Incubation, Negative Control, Positive Control

    Evaluation of Myr-B peptide-induced death of human cervical cancer HeLa ( a ) and colon cancer Caco-2 ( b ) cells. Cell membrane integrity was assessed through lactate dehydrogenase (LDH) release from untreated HeLa or Caco-2 cells (negative control) after 3 h exposure of HeLa and Caco-2 cells to their respective IC 50 doses of Myr-B peptide (38 μM and 50 μM, respectively) and from HeLa or Caco-2 cells treated with a lysis solution to release all LDH (positive control). The exposure to Pep-B was carried out under the same conditions as the corresponding treatment with the Myr-B peptide for each cancer cell line. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; *** p -value < 0.001; **** p -value < 0.0001.

    Journal: International Journal of Molecular Sciences

    Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

    doi: 10.3390/ijms27093918

    Figure Lengend Snippet: Evaluation of Myr-B peptide-induced death of human cervical cancer HeLa ( a ) and colon cancer Caco-2 ( b ) cells. Cell membrane integrity was assessed through lactate dehydrogenase (LDH) release from untreated HeLa or Caco-2 cells (negative control) after 3 h exposure of HeLa and Caco-2 cells to their respective IC 50 doses of Myr-B peptide (38 μM and 50 μM, respectively) and from HeLa or Caco-2 cells treated with a lysis solution to release all LDH (positive control). The exposure to Pep-B was carried out under the same conditions as the corresponding treatment with the Myr-B peptide for each cancer cell line. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; *** p -value < 0.001; **** p -value < 0.0001.

    Article Snippet: The human colon cancer Caco-2 cell line (ATCC HTB-37) was cultured in DMEM supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, 1% Non-Essential Amino Acids and 1% sodium pyruvate and maintained at 37 °C in a humidified incubator with 5% CO 2 [ ].

    Techniques: Membrane, Negative Control, Lysis, Positive Control

    SEM analysis of Myr-B peptide-induced effects on human colon cancer Caco-2 cells. SEM micrographs (acquired and processed using JEOL inTouchScope Interface software) of untreated Caco-2 cells (negative control) ( a , b ), Caco-2 cells after 3 h exposure to 50 μM Myr-B ( c , d ) and 50 μM Pep-B ( e , f ) and Caco-2 cells treated with 2% NaN 3 (positive control) ( g , h ). Magnification and scale bars = ( a – d ) 1500× and 10 μm, respectively; ( e – h ) 10,000× and 1 μm, respectively.

    Journal: International Journal of Molecular Sciences

    Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

    doi: 10.3390/ijms27093918

    Figure Lengend Snippet: SEM analysis of Myr-B peptide-induced effects on human colon cancer Caco-2 cells. SEM micrographs (acquired and processed using JEOL inTouchScope Interface software) of untreated Caco-2 cells (negative control) ( a , b ), Caco-2 cells after 3 h exposure to 50 μM Myr-B ( c , d ) and 50 μM Pep-B ( e , f ) and Caco-2 cells treated with 2% NaN 3 (positive control) ( g , h ). Magnification and scale bars = ( a – d ) 1500× and 10 μm, respectively; ( e – h ) 10,000× and 1 μm, respectively.

    Article Snippet: The human colon cancer Caco-2 cell line (ATCC HTB-37) was cultured in DMEM supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, 1% Non-Essential Amino Acids and 1% sodium pyruvate and maintained at 37 °C in a humidified incubator with 5% CO 2 [ ].

    Techniques: Software, Negative Control, Positive Control

    TRV130 represses proliferation of colon cancer cells. ( A ) Caco-2 and HCT116 cells were treated with TRV130 at varying concentrations (2.5, 5, 10, 20, 40, 80, and 160 µM) for 24 h, and cell viability was measured by MTT assay. (B-C) Caco-2 and HCT116 cells were treated with different concentrations of TRV130 (10, 20, and 40 µM). ( B ) EdU incorporation assay was used to evaluate cell proliferation in Caco-2 and HCT116 cells (Scale bar = 100 μm). ( C ) Colony formation assay was performed to assess the clonogenic potential of Caco-2 and HCT116 cells. * P < 0.05, *** P < 0.001, ns, not significant

    Journal: Hereditas

    Article Title: TRV130 inhibits colon cancer progression via suppressing the Hedgehog signaling pathway: in vitro and in vivo evidence

    doi: 10.1186/s41065-026-00633-6

    Figure Lengend Snippet: TRV130 represses proliferation of colon cancer cells. ( A ) Caco-2 and HCT116 cells were treated with TRV130 at varying concentrations (2.5, 5, 10, 20, 40, 80, and 160 µM) for 24 h, and cell viability was measured by MTT assay. (B-C) Caco-2 and HCT116 cells were treated with different concentrations of TRV130 (10, 20, and 40 µM). ( B ) EdU incorporation assay was used to evaluate cell proliferation in Caco-2 and HCT116 cells (Scale bar = 100 μm). ( C ) Colony formation assay was performed to assess the clonogenic potential of Caco-2 and HCT116 cells. * P < 0.05, *** P < 0.001, ns, not significant

    Article Snippet: The human colon cancer cell lines Caco-2 and HCT116 were obtained from Wuhan Procell (Wuhan, China).

    Techniques: MTT Assay, Colony Assay

    TRV130 induces apoptosis in colon cancer cells in a concentration-dependent manner. ( A ) Apoptosis of Caco-2 and HCT116 colon cancer cells treated with TRV130 (10, 20, and 40 µM) was analyzed by Annexin V-FITC/PI flow cytometry, and the apoptosis rate was quantified.( B ) TUNEL staining was used to detect apoptotic cells in Caco-2 and HCT116 colon cancer cells after TRV130 treatment (10, 20, and 40 µM) (Scale bar = 100 μm). * P < 0.05, ** P < 0.01, *** P < 0.001

    Journal: Hereditas

    Article Title: TRV130 inhibits colon cancer progression via suppressing the Hedgehog signaling pathway: in vitro and in vivo evidence

    doi: 10.1186/s41065-026-00633-6

    Figure Lengend Snippet: TRV130 induces apoptosis in colon cancer cells in a concentration-dependent manner. ( A ) Apoptosis of Caco-2 and HCT116 colon cancer cells treated with TRV130 (10, 20, and 40 µM) was analyzed by Annexin V-FITC/PI flow cytometry, and the apoptosis rate was quantified.( B ) TUNEL staining was used to detect apoptotic cells in Caco-2 and HCT116 colon cancer cells after TRV130 treatment (10, 20, and 40 µM) (Scale bar = 100 μm). * P < 0.05, ** P < 0.01, *** P < 0.001

    Article Snippet: The human colon cancer cell lines Caco-2 and HCT116 were obtained from Wuhan Procell (Wuhan, China).

    Techniques: Concentration Assay, Flow Cytometry, TUNEL Assay, Staining

    TRV130 suppresses migration and invasion of colon cancer cells. Caco-2 and HCT116 cells were treated with 10, 20, and 40 µM TRV130. ( A - B ) Transwell assays were performed to assess the migratory and invasive capacity of Caco-2 and HCT116 cells (Scale bar = 50 μm). ( C ) Wound healing assays were used to detect the migratory potential of Caco-2 and HCT116 cells; representative images at 0 h and 24 h were captured, and the wound closure percentage was quantified (Scale bar = 100 μm). * P < 0.05, ** P < 0.01, *** P < 0.001, ns, not significant

    Journal: Hereditas

    Article Title: TRV130 inhibits colon cancer progression via suppressing the Hedgehog signaling pathway: in vitro and in vivo evidence

    doi: 10.1186/s41065-026-00633-6

    Figure Lengend Snippet: TRV130 suppresses migration and invasion of colon cancer cells. Caco-2 and HCT116 cells were treated with 10, 20, and 40 µM TRV130. ( A - B ) Transwell assays were performed to assess the migratory and invasive capacity of Caco-2 and HCT116 cells (Scale bar = 50 μm). ( C ) Wound healing assays were used to detect the migratory potential of Caco-2 and HCT116 cells; representative images at 0 h and 24 h were captured, and the wound closure percentage was quantified (Scale bar = 100 μm). * P < 0.05, ** P < 0.01, *** P < 0.001, ns, not significant

    Article Snippet: The human colon cancer cell lines Caco-2 and HCT116 were obtained from Wuhan Procell (Wuhan, China).

    Techniques: Migration

    TRV130 modulates expression of cell proliferation- and apoptosis-related proteins in colon cancer cells. Caco-2 and HCT116 cells were treated with TRV130 (10, 20, and 40 µM). ( A ) Western blot analysis of Cyclin D1, Bcl-2, total-caspase 3, and C-caspase 3 expression levels in Caco-2 cells. ( B ) Western blot analysis of Cyclin D1, Bcl-2, total-caspase 3, and C-caspase 3 levels in HCT116 cells. * P < 0.05, ** P < 0.01, *** P < 0.001

    Journal: Hereditas

    Article Title: TRV130 inhibits colon cancer progression via suppressing the Hedgehog signaling pathway: in vitro and in vivo evidence

    doi: 10.1186/s41065-026-00633-6

    Figure Lengend Snippet: TRV130 modulates expression of cell proliferation- and apoptosis-related proteins in colon cancer cells. Caco-2 and HCT116 cells were treated with TRV130 (10, 20, and 40 µM). ( A ) Western blot analysis of Cyclin D1, Bcl-2, total-caspase 3, and C-caspase 3 expression levels in Caco-2 cells. ( B ) Western blot analysis of Cyclin D1, Bcl-2, total-caspase 3, and C-caspase 3 levels in HCT116 cells. * P < 0.05, ** P < 0.01, *** P < 0.001

    Article Snippet: The human colon cancer cell lines Caco-2 and HCT116 were obtained from Wuhan Procell (Wuhan, China).

    Techniques: Expressing, Western Blot

    TRV130 inhibits the Hh signaling pathway in colon cancer cells. Caco-2 cells and HCT116 cells were treated TRV130 (10, 20, and 40 µM) or Cyc (5 µM) ( A - B ) Western blot analysis of GLI1 and PTCH1 (key Hh pathway proteins) expression levels in Caco-2 and HCT116 cells. * P < 0.05, ** P < 0.01, *** P < 0.001

    Journal: Hereditas

    Article Title: TRV130 inhibits colon cancer progression via suppressing the Hedgehog signaling pathway: in vitro and in vivo evidence

    doi: 10.1186/s41065-026-00633-6

    Figure Lengend Snippet: TRV130 inhibits the Hh signaling pathway in colon cancer cells. Caco-2 cells and HCT116 cells were treated TRV130 (10, 20, and 40 µM) or Cyc (5 µM) ( A - B ) Western blot analysis of GLI1 and PTCH1 (key Hh pathway proteins) expression levels in Caco-2 and HCT116 cells. * P < 0.05, ** P < 0.01, *** P < 0.001

    Article Snippet: The human colon cancer cell lines Caco-2 and HCT116 were obtained from Wuhan Procell (Wuhan, China).

    Techniques: Western Blot, Expressing

    Zinc as an Active Principle of ZPT. (A) Chemical structures of dipyrithione and sodium pyrithione are shown. The activities of varying concentrations of ZPT, ZnSO 4 , dipyrithione and sodium pyrithione to inhibit the hydrolysis of Compound 1 by purified PLCε were measured as described in Methods. ( B ) The activities of varying concentrations of ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε, PLCβ4, PLCδ1 or PLCγ1 were measured as described in Methods. (C) The activities of 5 µM ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε were measured in the presence of varying concentrations of sodium pyrithione. ( D ) Caco2 cells were treated with 5 µM ZnSO 4 in the presence or absence of 5 µM sodium pyrithione or with 5 µM ZPT for 30 min. Intracellular Zn 2+ concentrations of the treated cells were measured by using Zinquin ethyl ester as described in Methods. The values obtained are expressed as fold changes over the average value of untreated cells. All the experiments described above were performed three times in duplicates.

    Journal: Scientific Reports

    Article Title: Increase of intracellular Zn 2+ concentration directly inhibits phospholipase Cε and suppresses inflammation and tumour formation in mice

    doi: 10.1038/s41598-025-25886-5

    Figure Lengend Snippet: Zinc as an Active Principle of ZPT. (A) Chemical structures of dipyrithione and sodium pyrithione are shown. The activities of varying concentrations of ZPT, ZnSO 4 , dipyrithione and sodium pyrithione to inhibit the hydrolysis of Compound 1 by purified PLCε were measured as described in Methods. ( B ) The activities of varying concentrations of ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε, PLCβ4, PLCδ1 or PLCγ1 were measured as described in Methods. (C) The activities of 5 µM ZnSO 4 to inhibit the hydrolysis of Compound 1 by purified PLCε were measured in the presence of varying concentrations of sodium pyrithione. ( D ) Caco2 cells were treated with 5 µM ZnSO 4 in the presence or absence of 5 µM sodium pyrithione or with 5 µM ZPT for 30 min. Intracellular Zn 2+ concentrations of the treated cells were measured by using Zinquin ethyl ester as described in Methods. The values obtained are expressed as fold changes over the average value of untreated cells. All the experiments described above were performed three times in duplicates.

    Article Snippet: A human colon cancer epithelial cell line Caco2 was purchased from ATCC (HTB-37) and maintained in 5% CO 2 at 37 °C in modified Eagle’s minimum essential medium (MEM) (Nacalai tesque) supplemented with 20% fetal bovine serum (FBS) (Sigma), non-essential amino acids (Gibco) and 100 μg/ml penicillin-streptomycin (Nacalai tesque).

    Techniques: Purification

    Effect of ZPT on PKD–NF-κB Signaling and Proinflammatory Gene Expression. (A) Caco2 and SW480 cells were serum-starved for 3 h in the presence of the indicated concentrations of ZPT or a vehicle (DMSO) and subsequently stimulated by 20 µM LPA for 30 min. PKD phosphorylated at Ser916 and total PKD in the cell lysates were quantified by immunoblotting with anti-phospho-PKD (Ser916) and anti-PKD Abs, respectively, as described in Methods. Numbers below the immunoblots indicate fold increase of the phospho-PKD signals divided by the total PKD signals over that at 0 min after LPA stimulation of the control cells. Each of the experiments was performed three times yielding equivalent results. A representative result is shown. The original blots are presented in Supplementary Figures S4 and S5. (B) Caco2 cells treated with 5 µM ZPT or the vehicle as described in (A) were subjected to subcellular fractionation and the resulting nuclear and cytoplasmic fractions were subjected to immunoblotting with the anti-NF-κB p65 Ab. TATA-binding protein (TBP) and α-tubulin were used as markers for the nuclear and the cytoplasmic fractions, respectively. A fold change of the nuclear NF-κB caused by 5 µM ZPT treatment is shown in numbers. Each of the experiments was performed three times yielding equivalent results. A representative result is shown. The original blots are presented in Supplementary Figure S6. (C) Total cellular RNAs isolated from Caco2 cells treated as described in (B) were subjected to qRT-PCR for quantification of the mRNA levels of the proinflammatory molecules: CXCL1, CXCL8, CCL2, CCL20, TNF-α and COX-2, by using the b- actin mRNA as an internal control. The obtained values are expressed as relative fold changes of nuclear NF-κB normalized to TATA-binding protein (TATA), with the value from the − LPA/−ZPT condition set to 1. The experiments were performed three times in duplicates.

    Journal: Scientific Reports

    Article Title: Increase of intracellular Zn 2+ concentration directly inhibits phospholipase Cε and suppresses inflammation and tumour formation in mice

    doi: 10.1038/s41598-025-25886-5

    Figure Lengend Snippet: Effect of ZPT on PKD–NF-κB Signaling and Proinflammatory Gene Expression. (A) Caco2 and SW480 cells were serum-starved for 3 h in the presence of the indicated concentrations of ZPT or a vehicle (DMSO) and subsequently stimulated by 20 µM LPA for 30 min. PKD phosphorylated at Ser916 and total PKD in the cell lysates were quantified by immunoblotting with anti-phospho-PKD (Ser916) and anti-PKD Abs, respectively, as described in Methods. Numbers below the immunoblots indicate fold increase of the phospho-PKD signals divided by the total PKD signals over that at 0 min after LPA stimulation of the control cells. Each of the experiments was performed three times yielding equivalent results. A representative result is shown. The original blots are presented in Supplementary Figures S4 and S5. (B) Caco2 cells treated with 5 µM ZPT or the vehicle as described in (A) were subjected to subcellular fractionation and the resulting nuclear and cytoplasmic fractions were subjected to immunoblotting with the anti-NF-κB p65 Ab. TATA-binding protein (TBP) and α-tubulin were used as markers for the nuclear and the cytoplasmic fractions, respectively. A fold change of the nuclear NF-κB caused by 5 µM ZPT treatment is shown in numbers. Each of the experiments was performed three times yielding equivalent results. A representative result is shown. The original blots are presented in Supplementary Figure S6. (C) Total cellular RNAs isolated from Caco2 cells treated as described in (B) were subjected to qRT-PCR for quantification of the mRNA levels of the proinflammatory molecules: CXCL1, CXCL8, CCL2, CCL20, TNF-α and COX-2, by using the b- actin mRNA as an internal control. The obtained values are expressed as relative fold changes of nuclear NF-κB normalized to TATA-binding protein (TATA), with the value from the − LPA/−ZPT condition set to 1. The experiments were performed three times in duplicates.

    Article Snippet: A human colon cancer epithelial cell line Caco2 was purchased from ATCC (HTB-37) and maintained in 5% CO 2 at 37 °C in modified Eagle’s minimum essential medium (MEM) (Nacalai tesque) supplemented with 20% fetal bovine serum (FBS) (Sigma), non-essential amino acids (Gibco) and 100 μg/ml penicillin-streptomycin (Nacalai tesque).

    Techniques: Gene Expression, Western Blot, Control, Fractionation, Binding Assay, Isolation, Quantitative RT-PCR

    Effect of ZPT Administration on Proliferation of Xenografted Caco2 cells. Caco2 cells (5 × 10 6 cells) were implanted subcutaneously into the right flanks of female nude mice. One week later, the mice were administered intraperitoneally with ZPT, dipyrithione or the vehicle 3 days per week for 8 weeks, during which the body weight (A) and the tumour volumes (B) were measured every 7 days. The number of mice ( n ) for each group is shown in parenthesis. The number of mice ( n ) for each group is shown in parenthesis. Thereafter, the tumours were excised and weighed (C) .

    Journal: Scientific Reports

    Article Title: Increase of intracellular Zn 2+ concentration directly inhibits phospholipase Cε and suppresses inflammation and tumour formation in mice

    doi: 10.1038/s41598-025-25886-5

    Figure Lengend Snippet: Effect of ZPT Administration on Proliferation of Xenografted Caco2 cells. Caco2 cells (5 × 10 6 cells) were implanted subcutaneously into the right flanks of female nude mice. One week later, the mice were administered intraperitoneally with ZPT, dipyrithione or the vehicle 3 days per week for 8 weeks, during which the body weight (A) and the tumour volumes (B) were measured every 7 days. The number of mice ( n ) for each group is shown in parenthesis. The number of mice ( n ) for each group is shown in parenthesis. Thereafter, the tumours were excised and weighed (C) .

    Article Snippet: A human colon cancer epithelial cell line Caco2 was purchased from ATCC (HTB-37) and maintained in 5% CO 2 at 37 °C in modified Eagle’s minimum essential medium (MEM) (Nacalai tesque) supplemented with 20% fetal bovine serum (FBS) (Sigma), non-essential amino acids (Gibco) and 100 μg/ml penicillin-streptomycin (Nacalai tesque).

    Techniques: