hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hct116  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116
    Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of <t>HCT116</t> cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.
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    1) Product Images from "The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA"

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    Journal: Cancer Medicine

    doi: 10.1002/cam4.7129

    Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of HCT116 cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.
    Figure Legend Snippet: Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of HCT116 cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.

    Techniques Used: Over Expression, Western Blot, Expressing, Quantitative RT-PCR, MTT Assay, EdU Assay

    RBMS3 suppresses migration and invasion of colon cancer cells. (A, B) The transwell migration and invasion assays revealed that the overexpression of RBMS3 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). (C, D) Statistical analysis of the cell migration and invasion among different groups was conducted using the t ‐test, *** p < 0.001, **** p < 0.0001. (E, F) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups. (G, H) Statistical analysis was performed to evaluate the migration area of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups at different time points, * p < 0.05, ** p < 0.01. (I) The number of lung metastatic lesions observed under the microscope in the overexpressed RBMS3, knocked‐down RBMS3, and control groups in the tail vein lung metastasis model were statistically analyzed using the t ‐test, * p < 0.05. (J) The tail vein injection model was used to examine the influence of RBMS3 on the lung colonization of HCT116 cells in vivo, with a total of ten mice in each group. (magnification, 20×; scale bars, 500 μm; the black arrow represents the location of the metastasis).
    Figure Legend Snippet: RBMS3 suppresses migration and invasion of colon cancer cells. (A, B) The transwell migration and invasion assays revealed that the overexpression of RBMS3 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). (C, D) Statistical analysis of the cell migration and invasion among different groups was conducted using the t ‐test, *** p < 0.001, **** p < 0.0001. (E, F) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups. (G, H) Statistical analysis was performed to evaluate the migration area of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups at different time points, * p < 0.05, ** p < 0.01. (I) The number of lung metastatic lesions observed under the microscope in the overexpressed RBMS3, knocked‐down RBMS3, and control groups in the tail vein lung metastasis model were statistically analyzed using the t ‐test, * p < 0.05. (J) The tail vein injection model was used to examine the influence of RBMS3 on the lung colonization of HCT116 cells in vivo, with a total of ten mice in each group. (magnification, 20×; scale bars, 500 μm; the black arrow represents the location of the metastasis).

    Techniques Used: Migration, Over Expression, Wound Healing Assay, Microscopy, Injection, In Vivo

    LIMS1 is the key target gene regulated by RBMS3. (A) Differential expression analysis was performed on the RNA‐seq data comparing the overexpression RBMS3 HCT15 cells and the control cells (pLVX group), as well as the shRBMS3 HCT15 cells and the control cells (PLKO group). The overexpression RBMS3 group showed 2576 upregulated genes and 3796 downregulated genes, while the shRBMS3 group exhibited 872 downregulated genes and 184 upregulated genes (cutoff: FC > 1.5 or FC < 0.75, p adj < 0.05). (B) In the 506 genes that were upregulated in the overexpression of RBMS3 and downregulated in the knockdown of RBMS3, and in the 103 genes that were downregulated in the overexpression of RBMS3 and upregulated in the knockdown of RBMS3, intersection analysis was performed with the predicted RBMS3 binding genes in the RNA‐INTER database, resulting in 432 candidate genes. (C) A GO enrichment analysis of the 432 candidate genes was conducted using the Metascape database. (D) A RIP assay was performed to measure the enrichment fold of RBMS3 binding target genes using HCT15 cells, * p < 0.05, ** p < 0.01, *** p < 0.001, ns, not significant. (E) Dual luciferase assays confirmed the regulatory effect of RBMS3 on LIMS1 using HCT15 cells, * p < 0.05. (F) Western blot analysis was performed to assess the expression of LIMS1 in the control group and RBMS3 HCT15 cells, demonstrating increased LIMS1 expression with RBMS3 overexpression and decreased expression with shRBMS3 HCT15 cells (knockdown of RBMS3). (G) Treatment with Actinomycin D for 12 h revealed enhanced mRNA stability of LIMS1 in the RBMS3 overexpression group compared to the control group of HCT116 cells. (H) The stability of LIMS1 mRNA in the HCT116 cell line decreased upon RBMS3 knockdown, as observed after a 12‐h treatment with actinomycin D.
    Figure Legend Snippet: LIMS1 is the key target gene regulated by RBMS3. (A) Differential expression analysis was performed on the RNA‐seq data comparing the overexpression RBMS3 HCT15 cells and the control cells (pLVX group), as well as the shRBMS3 HCT15 cells and the control cells (PLKO group). The overexpression RBMS3 group showed 2576 upregulated genes and 3796 downregulated genes, while the shRBMS3 group exhibited 872 downregulated genes and 184 upregulated genes (cutoff: FC > 1.5 or FC < 0.75, p adj < 0.05). (B) In the 506 genes that were upregulated in the overexpression of RBMS3 and downregulated in the knockdown of RBMS3, and in the 103 genes that were downregulated in the overexpression of RBMS3 and upregulated in the knockdown of RBMS3, intersection analysis was performed with the predicted RBMS3 binding genes in the RNA‐INTER database, resulting in 432 candidate genes. (C) A GO enrichment analysis of the 432 candidate genes was conducted using the Metascape database. (D) A RIP assay was performed to measure the enrichment fold of RBMS3 binding target genes using HCT15 cells, * p < 0.05, ** p < 0.01, *** p < 0.001, ns, not significant. (E) Dual luciferase assays confirmed the regulatory effect of RBMS3 on LIMS1 using HCT15 cells, * p < 0.05. (F) Western blot analysis was performed to assess the expression of LIMS1 in the control group and RBMS3 HCT15 cells, demonstrating increased LIMS1 expression with RBMS3 overexpression and decreased expression with shRBMS3 HCT15 cells (knockdown of RBMS3). (G) Treatment with Actinomycin D for 12 h revealed enhanced mRNA stability of LIMS1 in the RBMS3 overexpression group compared to the control group of HCT116 cells. (H) The stability of LIMS1 mRNA in the HCT116 cell line decreased upon RBMS3 knockdown, as observed after a 12‐h treatment with actinomycin D.

    Techniques Used: Expressing, RNA Sequencing Assay, Over Expression, Binding Assay, Luciferase, Western Blot

    Overexpression of LIMS1 inhibits cell proliferation, migration, and invasion in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in both PLVX and LIMS1 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, *** p < 0.001. (C) LIMS1 expression was examined through qRT‐PCR in the PLVX control group and the group with LIMS1 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the LIMS1 overexpression group and the PLVX control group, *** p < 0.001. (E) Cell proliferation was analyzed using the EDU assay in the LIMS1 overexpression group and the PLVX control group. (F–I) The transwell migration and invasion assays revealed that the overexpression of LIMS1 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). Statistical analysis of the cell migration among different groups was conducted using the t ‐test, * p < 0.05, ** p < 0.01. (J–L) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups. Statistical analysis was performed to evaluate the migration area of cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups at different time points, * p < 0.05, ** p < 0.01.
    Figure Legend Snippet: Overexpression of LIMS1 inhibits cell proliferation, migration, and invasion in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in both PLVX and LIMS1 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, *** p < 0.001. (C) LIMS1 expression was examined through qRT‐PCR in the PLVX control group and the group with LIMS1 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the LIMS1 overexpression group and the PLVX control group, *** p < 0.001. (E) Cell proliferation was analyzed using the EDU assay in the LIMS1 overexpression group and the PLVX control group. (F–I) The transwell migration and invasion assays revealed that the overexpression of LIMS1 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). Statistical analysis of the cell migration among different groups was conducted using the t ‐test, * p < 0.05, ** p < 0.01. (J–L) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups. Statistical analysis was performed to evaluate the migration area of cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups at different time points, * p < 0.05, ** p < 0.01.

    Techniques Used: Over Expression, Migration, Western Blot, Expressing, Quantitative RT-PCR, MTT Assay, EdU Assay, Wound Healing Assay

    Downregulated LIMS1 recovers the effect of RBMS3 overexpression in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in PLVX, RBMS3, and RBMS3+shLIMS1 cell models. (B) The grayscale intensities of the Western blot bands were statistically analyzed, ** p < 0.01, *** p < 0.001. (C) Rescued effects of LIMS1 on cell proliferation of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated. All cells were harvested for MTT analyses at the indicated time points. Data are presented as mean ± SD, *** p < 0.001. (D, E) Rescued effects of LIMS1 on migration and invasion of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated (magnification, 100×; scale bars, 200 μm). Data are presented as means ± SD, ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: Downregulated LIMS1 recovers the effect of RBMS3 overexpression in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in PLVX, RBMS3, and RBMS3+shLIMS1 cell models. (B) The grayscale intensities of the Western blot bands were statistically analyzed, ** p < 0.01, *** p < 0.001. (C) Rescued effects of LIMS1 on cell proliferation of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated. All cells were harvested for MTT analyses at the indicated time points. Data are presented as mean ± SD, *** p < 0.001. (D, E) Rescued effects of LIMS1 on migration and invasion of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated (magnification, 100×; scale bars, 200 μm). Data are presented as means ± SD, ** p < 0.01, *** p < 0.001.

    Techniques Used: Over Expression, Western Blot, Expressing, Migration

    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
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    human colorectal  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH human colorectal
    The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and <t>HCT116</t> cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Human Colorectal, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells"

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    Journal: Molecules

    doi: 10.3390/molecules26164787

    The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and HCT116 cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and HCT116 cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the expression of Nrf2 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of Nrf2 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: SOD and GSTP in DLD-1 and HCT116 cells. ( A ) Levels of SOD and GSTP transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of SOD and GSTP proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: SOD and GSTP in DLD-1 and HCT116 cells. ( A ) Levels of SOD and GSTP transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of SOD and GSTP proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: CAT and GPx in DLD-1 and HCT116 cells. ( A ) Levels of CAT and GPx transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of CAT and GPx proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: CAT and GPx in DLD-1 and HCT116 cells. ( A ) Levels of CAT and GPx transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of CAT and GPx proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on NF-κB activation in DLD-1 and HCT116 cells. ( A ) The levels of NF-κB p50 and p65 proteins in the cytosolic fraction. ( B ) The levels of NF-κB p50 and p65 proteins in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The levels of NF-κB p50 and p65 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on NF-κB activation in DLD-1 and HCT116 cells. ( A ) The levels of NF-κB p50 and p65 proteins in the cytosolic fraction. ( B ) The levels of NF-κB p50 and p65 proteins in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The levels of NF-κB p50 and p65 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the expression of NF-κB p50 and p65 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of NF-κB p50 and p65 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected NF-κB target genes: COX-2 and iNOS in DLD-1 and HCT116 cells. ( A ) Levels of COX-2 and iNOS transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of COX-2 and iNOS proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of selected NF-κB target genes: COX-2 and iNOS in DLD-1 and HCT116 cells. ( A ) Levels of COX-2 and iNOS transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of COX-2 and iNOS proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on STAT3 activation in DLD-1 and HCT116 cells. ( A ) The level of STAT3 protein in the cytosolic fraction. ( B ) The level of STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The level of STAT3 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on STAT3 activation in DLD-1 and HCT116 cells. ( A ) The level of STAT3 protein in the cytosolic fraction. ( B ) The level of STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The level of STAT3 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the level of p-STAT3 in DLD-1 and HCT116 cells. ( A ) The level of p-STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of lamin. ( B ) The ratio of nuclear p-STAT3 and nuclear STAT3 compared with the control group. DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the level of p-STAT3 in DLD-1 and HCT116 cells. ( A ) The level of p-STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of lamin. ( B ) The ratio of nuclear p-STAT3 and nuclear STAT3 compared with the control group. DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Western Blot

    The effect of lichen-derived compounds on the expression of STAT3 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of STAT3 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected STAT3 target gene: Bcl-xl in DLD-1 and HCT116 cells. ( A ) Level of the Bcl-xl transcript. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of the Bcl-xl protein. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
    Figure Legend Snippet: The effect of lichen-derived compounds on the expression of selected STAT3 target gene: Bcl-xl in DLD-1 and HCT116 cells. ( A ) Level of the Bcl-xl transcript. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of the Bcl-xl protein. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Techniques Used: Derivative Assay, Expressing, Western Blot

    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hct116 cells  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116 cells
    Bioactivity of compounds 1 and 2 .
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Molecular Networking-Guided Isolation of New Etzionin-Type Diketopiperazine Hydroxamates from the Persian Gulf Sponge Cliona celata"

    Article Title: Molecular Networking-Guided Isolation of New Etzionin-Type Diketopiperazine Hydroxamates from the Persian Gulf Sponge Cliona celata

    Journal: Marine Drugs

    doi: 10.3390/md19080439

    Bioactivity of compounds 1 and 2 .
    Figure Legend Snippet: Bioactivity of compounds 1 and 2 .

    Techniques Used: Positive Control

    hct  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct
    A Cell expansion of lentivirally transduced SW480 or (B) <t>HCT-116</t> cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.
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    1) Product Images from "Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53"

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    Journal: Oncogene

    doi: 10.1038/s41388-021-01847-w

    A Cell expansion of lentivirally transduced SW480 or (B) HCT-116 cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.
    Figure Legend Snippet: A Cell expansion of lentivirally transduced SW480 or (B) HCT-116 cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.

    Techniques Used: Transduction, CRISPR, Construct, MANN-WHITNEY

    A Time-lapse imaging of SW480 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. Shown are cumulative cell death events over time determined by single cell tracking. P value was calculated by log-rank test. B Percentage of apoptotic SW480 cells determined by Annexin V/7-AAD staining 72 hours after TGM2 knockdown. C Percentage of Caspase-3 positive SW480 cells 72 hours after TGM2 knockdown. D – F All experiments were repeated in HCT-116 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. D Time lapse imaging showing the cumulative cell death events. E Percentage of Annexin V positive and ( F) Caspase-3 positive HCT-116 cells 72 hours after TGM2 knockdown. Results are presented as mean ± SD of three independent experiments. *** P < 0.001, Mann–Whitney U test.
    Figure Legend Snippet: A Time-lapse imaging of SW480 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. Shown are cumulative cell death events over time determined by single cell tracking. P value was calculated by log-rank test. B Percentage of apoptotic SW480 cells determined by Annexin V/7-AAD staining 72 hours after TGM2 knockdown. C Percentage of Caspase-3 positive SW480 cells 72 hours after TGM2 knockdown. D – F All experiments were repeated in HCT-116 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. D Time lapse imaging showing the cumulative cell death events. E Percentage of Annexin V positive and ( F) Caspase-3 positive HCT-116 cells 72 hours after TGM2 knockdown. Results are presented as mean ± SD of three independent experiments. *** P < 0.001, Mann–Whitney U test.

    Techniques Used: Imaging, Transduction, Single Cell Tracking, Staining, MANN-WHITNEY

    A – C Gene expression profiling by RNA-seq of SW480 cells after transduction with either shTGM2-1 or shSCRMBL. A Unsupervised hierarchical clustering of the top 1000 differentially expressed genes (DEGs) upon TGM2 knockdown across the four biological replicates. B MA plot relating p values for all differentially expressed genes between shTGM2-1 and shSCRMBL from four biological replicates. Red dots indicate significantly regulated genes (adjusted P < 0.05). List of regulated genes is presented in Supplementary Table S . C Scatter plot of gene set enrichment analysis of DEGs relating the Q-value for Hallmark gene-set signatures. The top 16 enriched pathways are shown ( P < 0.05, Fold change ≥2). The color and size of each dot represent the Rich factor and the number of DEGs mapped to the indicated pathway, respectively. D Proteome analysis of regulated proteins involved in apoptosis upon shRNA-mediated TGM2 knockdown. Representative blot of Proteome Profiler Array™-Human Apoptosis Array analysis of SW480 cells. The regulation of protein expression of phosphorylated p53 variants is shown. E – H Quantification of p53 and phosphorylated p53 (S15, S46, and S392) upon TGM2 knockdown in SW480 ( E , G ) and HCT-116 ( F , H ) cells via Simple Western technology ( n = 3; Mann–Whitney U test).
    Figure Legend Snippet: A – C Gene expression profiling by RNA-seq of SW480 cells after transduction with either shTGM2-1 or shSCRMBL. A Unsupervised hierarchical clustering of the top 1000 differentially expressed genes (DEGs) upon TGM2 knockdown across the four biological replicates. B MA plot relating p values for all differentially expressed genes between shTGM2-1 and shSCRMBL from four biological replicates. Red dots indicate significantly regulated genes (adjusted P < 0.05). List of regulated genes is presented in Supplementary Table S . C Scatter plot of gene set enrichment analysis of DEGs relating the Q-value for Hallmark gene-set signatures. The top 16 enriched pathways are shown ( P < 0.05, Fold change ≥2). The color and size of each dot represent the Rich factor and the number of DEGs mapped to the indicated pathway, respectively. D Proteome analysis of regulated proteins involved in apoptosis upon shRNA-mediated TGM2 knockdown. Representative blot of Proteome Profiler Array™-Human Apoptosis Array analysis of SW480 cells. The regulation of protein expression of phosphorylated p53 variants is shown. E – H Quantification of p53 and phosphorylated p53 (S15, S46, and S392) upon TGM2 knockdown in SW480 ( E , G ) and HCT-116 ( F , H ) cells via Simple Western technology ( n = 3; Mann–Whitney U test).

    Techniques Used: Expressing, RNA Sequencing Assay, Transduction, shRNA, Western Blot, MANN-WHITNEY

    A Representative images of proximity ligation assay (PLA) of TGM2 and p53 in SW480 cells. Cells incubated only with TGM2 antibody served as negative control (I). Protein–protein interaction of TGM2 and p53(S15) was visualized using hybridization probes labeled with Texas Red (II). Nuclei were stained with DAPI (blue). B Quantification of TGM2-p53 interaction and associated technical controls (Ctrl). Technical controls demonstrate the specificity of PLA signals. Each dot represents one cell. Mean value of PLA dots per cell is shown by the black line. C Representative images of proximity ligation assay of TGM2 and p53 in patient-derived normal epithelial cells (I) and corresponding colon cancer cells (II). D Quantification of TGM2-p53 interaction in primary patient material. (Significance was calculated using Kruskal–Wallis test). E Co-immunoprecipitation (Co-IP) of endogenous TGM2 and p53 or phosphorylated p53(S15) in SW480, HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−). F Super-resolved image of a HCT-116 cell immunostained for TGM2 (red) and p53(S15) (cyan). A zoom-in of the highlighted region is shown on the right. White regions indicate overlapping signal of TGM2 and p53(S15) (yellow arrowheads). Scale bars represent 5 µm and 1 µm, respectively.
    Figure Legend Snippet: A Representative images of proximity ligation assay (PLA) of TGM2 and p53 in SW480 cells. Cells incubated only with TGM2 antibody served as negative control (I). Protein–protein interaction of TGM2 and p53(S15) was visualized using hybridization probes labeled with Texas Red (II). Nuclei were stained with DAPI (blue). B Quantification of TGM2-p53 interaction and associated technical controls (Ctrl). Technical controls demonstrate the specificity of PLA signals. Each dot represents one cell. Mean value of PLA dots per cell is shown by the black line. C Representative images of proximity ligation assay of TGM2 and p53 in patient-derived normal epithelial cells (I) and corresponding colon cancer cells (II). D Quantification of TGM2-p53 interaction in primary patient material. (Significance was calculated using Kruskal–Wallis test). E Co-immunoprecipitation (Co-IP) of endogenous TGM2 and p53 or phosphorylated p53(S15) in SW480, HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−). F Super-resolved image of a HCT-116 cell immunostained for TGM2 (red) and p53(S15) (cyan). A zoom-in of the highlighted region is shown on the right. White regions indicate overlapping signal of TGM2 and p53(S15) (yellow arrowheads). Scale bars represent 5 µm and 1 µm, respectively.

    Techniques Used: Proximity Ligation Assay, Incubation, Negative Control, Hybridization, Labeling, Staining, Derivative Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Knock-Out

    A – C HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−) were transduced with either shTGM2-1, shTGM2-2, or shSCRMBL. Time-lapse imaging and proliferation assay were performed to determine a rescue from cell death upon TGM2 knockdown. A Fold change of cell number of HCT-116 p53 wt and HCT-116 p53 −/− cells upon TGM2 knockdown in comparison to shSCRMBL control determined at day three after transduction. Data are presented as mean ± SD of three independent experiments (** P < 0.01, Mann–Whitney U test). B Single cell tracking of HCT-116 p53 wt and HCT-116 p53 − /− cells after TGM2 knockdown with shTGM2-1 and (C) shTGM2-2. Cumulative cell death events are shown over time (*** P < 0.001, Log-rank test). D Direct visualization of p53 activation upon TGM2 knockdown by time-lapse video-microscopy. Sequence of phase contrast images, tdTOMATO fluorescence of shTGM2-1 and p53-driven destabilized GFP reporter , depicting the same field of view over the time course of 30 hours as indicated in the corresponding panels in I–VIII. The yellow circles designate tracked cells over time. (I–VIII) show corresponding sequence of fluorescence images taken at the same time points as the phase contrast images. (I) Shown are two representative HCT-116 cells. (II and III) 6-8 hours after lentiviral transduction of shTGM2-1 both HCT-116 cells express the red fluorescent tdTOMATO reporter, indicating a knockdown of TGM2. (IV-VI) Another 4–10 hours later both cells express the green fluorescent (GFP) p53 reporter, indicating the induction of p53 activity. (VII and VIII) About 24 hours after transduction both HCT-116 cells subsequently undergo apoptosis (white arrows). Movie S shows all assembled images (3 min temporal resolution) of the same sequence.
    Figure Legend Snippet: A – C HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−) were transduced with either shTGM2-1, shTGM2-2, or shSCRMBL. Time-lapse imaging and proliferation assay were performed to determine a rescue from cell death upon TGM2 knockdown. A Fold change of cell number of HCT-116 p53 wt and HCT-116 p53 −/− cells upon TGM2 knockdown in comparison to shSCRMBL control determined at day three after transduction. Data are presented as mean ± SD of three independent experiments (** P < 0.01, Mann–Whitney U test). B Single cell tracking of HCT-116 p53 wt and HCT-116 p53 − /− cells after TGM2 knockdown with shTGM2-1 and (C) shTGM2-2. Cumulative cell death events are shown over time (*** P < 0.001, Log-rank test). D Direct visualization of p53 activation upon TGM2 knockdown by time-lapse video-microscopy. Sequence of phase contrast images, tdTOMATO fluorescence of shTGM2-1 and p53-driven destabilized GFP reporter , depicting the same field of view over the time course of 30 hours as indicated in the corresponding panels in I–VIII. The yellow circles designate tracked cells over time. (I–VIII) show corresponding sequence of fluorescence images taken at the same time points as the phase contrast images. (I) Shown are two representative HCT-116 cells. (II and III) 6-8 hours after lentiviral transduction of shTGM2-1 both HCT-116 cells express the red fluorescent tdTOMATO reporter, indicating a knockdown of TGM2. (IV-VI) Another 4–10 hours later both cells express the green fluorescent (GFP) p53 reporter, indicating the induction of p53 activity. (VII and VIII) About 24 hours after transduction both HCT-116 cells subsequently undergo apoptosis (white arrows). Movie S shows all assembled images (3 min temporal resolution) of the same sequence.

    Techniques Used: Knock-Out, Transduction, Imaging, Proliferation Assay, MANN-WHITNEY, Single Cell Tracking, Activation Assay, Microscopy, Sequencing, Fluorescence, Activity Assay

    hct116  (CLS Cell Lines Service GmbH)


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    CLS Cell Lines Service GmbH hct116
    Peptide profiling and anti-proliferative screening of camel whey protein hydrolysates (P-4.3 and P-5.2). ( a ) RP-UPLC peptide profile of CWP and their pepsin generated hydrolysates P-5.2 and P-4.3. ( b ) Camel whey protein hydrolysates P-4.3 and P-5.2 inhibit growth of <t>HCT116</t> cells. Viability of HCT116 cells after treatment with increasing concentrations of the CWPHs P-4.3 and P-5.2 for a period of 48 h. 231 μg/ml is the IC 50 for CWPH P-4.3, 221 μg/ml is the IC 50 for CWPH P-5.2. ( c ) Quantitative distribution of HCT116 cells in different phases of the cell cycle after treatment with camel CWPH P-4.3 (231 μg/ml) over a period of 24 h, 48 h and 72 h. Statistical analysis was carried out by student’s t-test using GraphPad Prism software and p < 0.05 was considered as statistically significant. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.
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    1) Product Images from "Camel whey protein hydrolysates induced G2/M cellcycle arrest in human colorectal carcinoma"

    Article Title: Camel whey protein hydrolysates induced G2/M cellcycle arrest in human colorectal carcinoma

    Journal: Scientific Reports

    doi: 10.1038/s41598-021-86391-z

    Peptide profiling and anti-proliferative screening of camel whey protein hydrolysates (P-4.3 and P-5.2). ( a ) RP-UPLC peptide profile of CWP and their pepsin generated hydrolysates P-5.2 and P-4.3. ( b ) Camel whey protein hydrolysates P-4.3 and P-5.2 inhibit growth of HCT116 cells. Viability of HCT116 cells after treatment with increasing concentrations of the CWPHs P-4.3 and P-5.2 for a period of 48 h. 231 μg/ml is the IC 50 for CWPH P-4.3, 221 μg/ml is the IC 50 for CWPH P-5.2. ( c ) Quantitative distribution of HCT116 cells in different phases of the cell cycle after treatment with camel CWPH P-4.3 (231 μg/ml) over a period of 24 h, 48 h and 72 h. Statistical analysis was carried out by student’s t-test using GraphPad Prism software and p < 0.05 was considered as statistically significant. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.
    Figure Legend Snippet: Peptide profiling and anti-proliferative screening of camel whey protein hydrolysates (P-4.3 and P-5.2). ( a ) RP-UPLC peptide profile of CWP and their pepsin generated hydrolysates P-5.2 and P-4.3. ( b ) Camel whey protein hydrolysates P-4.3 and P-5.2 inhibit growth of HCT116 cells. Viability of HCT116 cells after treatment with increasing concentrations of the CWPHs P-4.3 and P-5.2 for a period of 48 h. 231 μg/ml is the IC 50 for CWPH P-4.3, 221 μg/ml is the IC 50 for CWPH P-5.2. ( c ) Quantitative distribution of HCT116 cells in different phases of the cell cycle after treatment with camel CWPH P-4.3 (231 μg/ml) over a period of 24 h, 48 h and 72 h. Statistical analysis was carried out by student’s t-test using GraphPad Prism software and p < 0.05 was considered as statistically significant. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.

    Techniques Used: Generated, Software

    Inhibitory effect of CWPH P-4.3 on cell cycle progressive markers in HCT116 cells. ( a , c ) Western blot analysis of cell cycle regulatory proteins from HCT116 treated with CWPH P-4.3 (231 μg/ml) over a period of 24 h, 48 h and 72 h. ( b , d ) Each band intensity was quantified to analyze the protein expression using ImageJ, normalized relative to their respective loading control bands. Values are expressed as ratio of untreated control in log fold. Statistical analysis was carried out by student’s t-test using GraphPad Prism software and p < 0.05 was considered as statistically significant. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.
    Figure Legend Snippet: Inhibitory effect of CWPH P-4.3 on cell cycle progressive markers in HCT116 cells. ( a , c ) Western blot analysis of cell cycle regulatory proteins from HCT116 treated with CWPH P-4.3 (231 μg/ml) over a period of 24 h, 48 h and 72 h. ( b , d ) Each band intensity was quantified to analyze the protein expression using ImageJ, normalized relative to their respective loading control bands. Values are expressed as ratio of untreated control in log fold. Statistical analysis was carried out by student’s t-test using GraphPad Prism software and p < 0.05 was considered as statistically significant. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.

    Techniques Used: Western Blot, Expressing, Software

    Camel whey protein hydrolysates induce G2/M cellcycle arrest in HCT116 cells. This graphical abstract shows the molecular mechanism employed by the camel whey protein hydrolysates in inducing anti-proliferative effect on the human colorectal cancer cells implicating PLK1 as a potential target.
    Figure Legend Snippet: Camel whey protein hydrolysates induce G2/M cellcycle arrest in HCT116 cells. This graphical abstract shows the molecular mechanism employed by the camel whey protein hydrolysates in inducing anti-proliferative effect on the human colorectal cancer cells implicating PLK1 as a potential target.

    Techniques Used:

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    CLS Cell Lines Service GmbH hct116 cells
    Hct116 Cells, supplied by CLS Cell Lines Service GmbH, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of <t>HCT116</t> cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.
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    CLS Cell Lines Service GmbH human colorectal
    The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and <t>HCT116</t> cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).
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    A Cell expansion of lentivirally transduced SW480 or (B) <t>HCT-116</t> cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.
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    Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of HCT116 cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.

    Journal: Cancer Medicine

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    doi: 10.1002/cam4.7129

    Figure Lengend Snippet: Overexpression of RBMS3 inhibits colon cancer proliferation. (A) Western blot analysis was conducted to evaluate the expression level of RBMS3 in both PLVX and RBMS3 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, * p < 0.05. (C) RBMS3 expression was examined through qRT‐PCR in the PLVX control group and the group with RBMS3 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the RBMS3 overexpression group and the PLVX control group, ** p < 0.01. (E) Cell proliferation was analyzed using the EDU assay in the RBMS3 overexpression group and the PLVX control group. (F) An experimental study employing a subcutaneous murine model was conducted to assess the growth condition of HCT116 cells inoculated with overexpressed RBMS3, knocked‐down RBMS3, and the control. Six mice were used in each group for the analysis. (G) Tumor weight was compared among the control group, RBMS3 group, and RBMS3‐sh1 group, * p < 0.05, ** p < 0.01. (H) The tumor growth curve over time was plotted for the control, RBMS3, and RBMS3‐sh1 groups, * p < 0.05, ** p < 0.01.

    Article Snippet: In this investigation, we employed three distinct cell lines, namely HCT15, HCT116, and 293T, sourced from the esteemed Cell Lines Service of Cellcook Biotech Co., Ltd., situated in Guangzhou, China.

    Techniques: Over Expression, Western Blot, Expressing, Quantitative RT-PCR, MTT Assay, EdU Assay

    RBMS3 suppresses migration and invasion of colon cancer cells. (A, B) The transwell migration and invasion assays revealed that the overexpression of RBMS3 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). (C, D) Statistical analysis of the cell migration and invasion among different groups was conducted using the t ‐test, *** p < 0.001, **** p < 0.0001. (E, F) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups. (G, H) Statistical analysis was performed to evaluate the migration area of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups at different time points, * p < 0.05, ** p < 0.01. (I) The number of lung metastatic lesions observed under the microscope in the overexpressed RBMS3, knocked‐down RBMS3, and control groups in the tail vein lung metastasis model were statistically analyzed using the t ‐test, * p < 0.05. (J) The tail vein injection model was used to examine the influence of RBMS3 on the lung colonization of HCT116 cells in vivo, with a total of ten mice in each group. (magnification, 20×; scale bars, 500 μm; the black arrow represents the location of the metastasis).

    Journal: Cancer Medicine

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    doi: 10.1002/cam4.7129

    Figure Lengend Snippet: RBMS3 suppresses migration and invasion of colon cancer cells. (A, B) The transwell migration and invasion assays revealed that the overexpression of RBMS3 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). (C, D) Statistical analysis of the cell migration and invasion among different groups was conducted using the t ‐test, *** p < 0.001, **** p < 0.0001. (E, F) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups. (G, H) Statistical analysis was performed to evaluate the migration area of HCT15 cells in the overexpressed RBMS3, knocked‐down RBMS3, and control groups at different time points, * p < 0.05, ** p < 0.01. (I) The number of lung metastatic lesions observed under the microscope in the overexpressed RBMS3, knocked‐down RBMS3, and control groups in the tail vein lung metastasis model were statistically analyzed using the t ‐test, * p < 0.05. (J) The tail vein injection model was used to examine the influence of RBMS3 on the lung colonization of HCT116 cells in vivo, with a total of ten mice in each group. (magnification, 20×; scale bars, 500 μm; the black arrow represents the location of the metastasis).

    Article Snippet: In this investigation, we employed three distinct cell lines, namely HCT15, HCT116, and 293T, sourced from the esteemed Cell Lines Service of Cellcook Biotech Co., Ltd., situated in Guangzhou, China.

    Techniques: Migration, Over Expression, Wound Healing Assay, Microscopy, Injection, In Vivo

    LIMS1 is the key target gene regulated by RBMS3. (A) Differential expression analysis was performed on the RNA‐seq data comparing the overexpression RBMS3 HCT15 cells and the control cells (pLVX group), as well as the shRBMS3 HCT15 cells and the control cells (PLKO group). The overexpression RBMS3 group showed 2576 upregulated genes and 3796 downregulated genes, while the shRBMS3 group exhibited 872 downregulated genes and 184 upregulated genes (cutoff: FC > 1.5 or FC < 0.75, p adj < 0.05). (B) In the 506 genes that were upregulated in the overexpression of RBMS3 and downregulated in the knockdown of RBMS3, and in the 103 genes that were downregulated in the overexpression of RBMS3 and upregulated in the knockdown of RBMS3, intersection analysis was performed with the predicted RBMS3 binding genes in the RNA‐INTER database, resulting in 432 candidate genes. (C) A GO enrichment analysis of the 432 candidate genes was conducted using the Metascape database. (D) A RIP assay was performed to measure the enrichment fold of RBMS3 binding target genes using HCT15 cells, * p < 0.05, ** p < 0.01, *** p < 0.001, ns, not significant. (E) Dual luciferase assays confirmed the regulatory effect of RBMS3 on LIMS1 using HCT15 cells, * p < 0.05. (F) Western blot analysis was performed to assess the expression of LIMS1 in the control group and RBMS3 HCT15 cells, demonstrating increased LIMS1 expression with RBMS3 overexpression and decreased expression with shRBMS3 HCT15 cells (knockdown of RBMS3). (G) Treatment with Actinomycin D for 12 h revealed enhanced mRNA stability of LIMS1 in the RBMS3 overexpression group compared to the control group of HCT116 cells. (H) The stability of LIMS1 mRNA in the HCT116 cell line decreased upon RBMS3 knockdown, as observed after a 12‐h treatment with actinomycin D.

    Journal: Cancer Medicine

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    doi: 10.1002/cam4.7129

    Figure Lengend Snippet: LIMS1 is the key target gene regulated by RBMS3. (A) Differential expression analysis was performed on the RNA‐seq data comparing the overexpression RBMS3 HCT15 cells and the control cells (pLVX group), as well as the shRBMS3 HCT15 cells and the control cells (PLKO group). The overexpression RBMS3 group showed 2576 upregulated genes and 3796 downregulated genes, while the shRBMS3 group exhibited 872 downregulated genes and 184 upregulated genes (cutoff: FC > 1.5 or FC < 0.75, p adj < 0.05). (B) In the 506 genes that were upregulated in the overexpression of RBMS3 and downregulated in the knockdown of RBMS3, and in the 103 genes that were downregulated in the overexpression of RBMS3 and upregulated in the knockdown of RBMS3, intersection analysis was performed with the predicted RBMS3 binding genes in the RNA‐INTER database, resulting in 432 candidate genes. (C) A GO enrichment analysis of the 432 candidate genes was conducted using the Metascape database. (D) A RIP assay was performed to measure the enrichment fold of RBMS3 binding target genes using HCT15 cells, * p < 0.05, ** p < 0.01, *** p < 0.001, ns, not significant. (E) Dual luciferase assays confirmed the regulatory effect of RBMS3 on LIMS1 using HCT15 cells, * p < 0.05. (F) Western blot analysis was performed to assess the expression of LIMS1 in the control group and RBMS3 HCT15 cells, demonstrating increased LIMS1 expression with RBMS3 overexpression and decreased expression with shRBMS3 HCT15 cells (knockdown of RBMS3). (G) Treatment with Actinomycin D for 12 h revealed enhanced mRNA stability of LIMS1 in the RBMS3 overexpression group compared to the control group of HCT116 cells. (H) The stability of LIMS1 mRNA in the HCT116 cell line decreased upon RBMS3 knockdown, as observed after a 12‐h treatment with actinomycin D.

    Article Snippet: In this investigation, we employed three distinct cell lines, namely HCT15, HCT116, and 293T, sourced from the esteemed Cell Lines Service of Cellcook Biotech Co., Ltd., situated in Guangzhou, China.

    Techniques: Expressing, RNA Sequencing Assay, Over Expression, Binding Assay, Luciferase, Western Blot

    Overexpression of LIMS1 inhibits cell proliferation, migration, and invasion in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in both PLVX and LIMS1 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, *** p < 0.001. (C) LIMS1 expression was examined through qRT‐PCR in the PLVX control group and the group with LIMS1 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the LIMS1 overexpression group and the PLVX control group, *** p < 0.001. (E) Cell proliferation was analyzed using the EDU assay in the LIMS1 overexpression group and the PLVX control group. (F–I) The transwell migration and invasion assays revealed that the overexpression of LIMS1 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). Statistical analysis of the cell migration among different groups was conducted using the t ‐test, * p < 0.05, ** p < 0.01. (J–L) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups. Statistical analysis was performed to evaluate the migration area of cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups at different time points, * p < 0.05, ** p < 0.01.

    Journal: Cancer Medicine

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    doi: 10.1002/cam4.7129

    Figure Lengend Snippet: Overexpression of LIMS1 inhibits cell proliferation, migration, and invasion in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in both PLVX and LIMS1 overexpression cell models, PLVX was used as the control group. (B) The grayscale intensities of the Western blot bands were statistically analyzed, *** p < 0.001. (C) LIMS1 expression was examined through qRT‐PCR in the PLVX control group and the group with LIMS1 overexpression, *** p < 0.001. (D) Cell proliferation was assessed using the MTT assay in both the LIMS1 overexpression group and the PLVX control group, *** p < 0.001. (E) Cell proliferation was analyzed using the EDU assay in the LIMS1 overexpression group and the PLVX control group. (F–I) The transwell migration and invasion assays revealed that the overexpression of LIMS1 exerts an inhibitory effect on the migration and invasion of HCT15 and HCT116 cells (magnification, 100×; scale bars, 200 μm). Statistical analysis of the cell migration among different groups was conducted using the t ‐test, * p < 0.05, ** p < 0.01. (J–L) The scratch assay was employed to assess the migration of HCT15 cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups. Statistical analysis was performed to evaluate the migration area of cells in the overexpressed LIMS1, knocked‐down LIMS1, and control groups at different time points, * p < 0.05, ** p < 0.01.

    Article Snippet: In this investigation, we employed three distinct cell lines, namely HCT15, HCT116, and 293T, sourced from the esteemed Cell Lines Service of Cellcook Biotech Co., Ltd., situated in Guangzhou, China.

    Techniques: Over Expression, Migration, Western Blot, Expressing, Quantitative RT-PCR, MTT Assay, EdU Assay, Wound Healing Assay

    Downregulated LIMS1 recovers the effect of RBMS3 overexpression in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in PLVX, RBMS3, and RBMS3+shLIMS1 cell models. (B) The grayscale intensities of the Western blot bands were statistically analyzed, ** p < 0.01, *** p < 0.001. (C) Rescued effects of LIMS1 on cell proliferation of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated. All cells were harvested for MTT analyses at the indicated time points. Data are presented as mean ± SD, *** p < 0.001. (D, E) Rescued effects of LIMS1 on migration and invasion of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated (magnification, 100×; scale bars, 200 μm). Data are presented as means ± SD, ** p < 0.01, *** p < 0.001.

    Journal: Cancer Medicine

    Article Title: The RNA ‐binding protein RBMS3 inhibits the progression of colon cancer by regulating the stability of LIMS1 mRNA

    doi: 10.1002/cam4.7129

    Figure Lengend Snippet: Downregulated LIMS1 recovers the effect of RBMS3 overexpression in colon cancer. (A) Western blot analysis was conducted to evaluate the expression level of LIMS1 in PLVX, RBMS3, and RBMS3+shLIMS1 cell models. (B) The grayscale intensities of the Western blot bands were statistically analyzed, ** p < 0.01, *** p < 0.001. (C) Rescued effects of LIMS1 on cell proliferation of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated. All cells were harvested for MTT analyses at the indicated time points. Data are presented as mean ± SD, *** p < 0.001. (D, E) Rescued effects of LIMS1 on migration and invasion of HCT15 and HCT116 cells upon RBMS3 overexpression were evaluated (magnification, 100×; scale bars, 200 μm). Data are presented as means ± SD, ** p < 0.01, *** p < 0.001.

    Article Snippet: In this investigation, we employed three distinct cell lines, namely HCT15, HCT116, and 293T, sourced from the esteemed Cell Lines Service of Cellcook Biotech Co., Ltd., situated in Guangzhou, China.

    Techniques: Over Expression, Western Blot, Expressing, Migration

    The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and HCT116 cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on Nrf2 activation in DLD-1 and HCT116 cells. ( A ) The level of Nrf2 protein in the cytosolic fraction. ( B ) The level of Nrf2 protein in the nuclear fraction. ( C ) The level of p-Nrf2 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A – C ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( D ) The level of Nrf2 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the expression of Nrf2 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of Nrf2 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: SOD and GSTP in DLD-1 and HCT116 cells. ( A ) Levels of SOD and GSTP transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of SOD and GSTP proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: SOD and GSTP in DLD-1 and HCT116 cells. ( A ) Levels of SOD and GSTP transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of SOD and GSTP proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: CAT and GPx in DLD-1 and HCT116 cells. ( A ) Levels of CAT and GPx transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of CAT and GPx proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of selected Nrf2 target genes: CAT and GPx in DLD-1 and HCT116 cells. ( A ) Levels of CAT and GPx transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of CAT and GPx proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on NF-κB activation in DLD-1 and HCT116 cells. ( A ) The levels of NF-κB p50 and p65 proteins in the cytosolic fraction. ( B ) The levels of NF-κB p50 and p65 proteins in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The levels of NF-κB p50 and p65 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on NF-κB activation in DLD-1 and HCT116 cells. ( A ) The levels of NF-κB p50 and p65 proteins in the cytosolic fraction. ( B ) The levels of NF-κB p50 and p65 proteins in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The levels of NF-κB p50 and p65 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the expression of NF-κB p50 and p65 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of NF-κB p50 and p65 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected NF-κB target genes: COX-2 and iNOS in DLD-1 and HCT116 cells. ( A ) Levels of COX-2 and iNOS transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of COX-2 and iNOS proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of selected NF-κB target genes: COX-2 and iNOS in DLD-1 and HCT116 cells. ( A ) Levels of COX-2 and iNOS transcripts. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Levels of COX-2 and iNOS proteins. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing, Western Blot

    The effect of lichen-derived compounds on STAT3 activation in DLD-1 and HCT116 cells. ( A ) The level of STAT3 protein in the cytosolic fraction. ( B ) The level of STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The level of STAT3 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on STAT3 activation in DLD-1 and HCT116 cells. ( A ) The level of STAT3 protein in the cytosolic fraction. ( B ) The level of STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs ( A , B ). Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin or lamin. ( C ) The level of STAT3 binding to DNA. Results are presented as the means ± SEM from three separate experiments percentage of control). Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Activation Assay, Western Blot, Binding Assay

    The effect of lichen-derived compounds on the level of p-STAT3 in DLD-1 and HCT116 cells. ( A ) The level of p-STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of lamin. ( B ) The ratio of nuclear p-STAT3 and nuclear STAT3 compared with the control group. DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the level of p-STAT3 in DLD-1 and HCT116 cells. ( A ) The level of p-STAT3 protein in the nuclear fraction. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of lamin. ( B ) The ratio of nuclear p-STAT3 and nuclear STAT3 compared with the control group. DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Western Blot

    The effect of lichen-derived compounds on the expression of STAT3 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of STAT3 in DLD-1 and HCT116 cells. The values (fold of control) are presented as the means ± SEM from three separate experiments. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing

    The effect of lichen-derived compounds on the expression of selected STAT3 target gene: Bcl-xl in DLD-1 and HCT116 cells. ( A ) Level of the Bcl-xl transcript. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of the Bcl-xl protein. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Journal: Molecules

    Article Title: Lichen-Derived Depsides and Depsidones Modulate the Nrf2, NF-κB and STAT3 Signaling Pathways in Colorectal Cancer Cells

    doi: 10.3390/molecules26164787

    Figure Lengend Snippet: The effect of lichen-derived compounds on the expression of selected STAT3 target gene: Bcl-xl in DLD-1 and HCT116 cells. ( A ) Level of the Bcl-xl transcript. The values (fold of control) are presented as the means ± SEM from three separate experiments. ( B ) Level of the Bcl-xl protein. Representative Western immunoblots are presented under the graphs. Results (means ± SEM from three separate experiments) are presented as a fold change to control after normalization against the level of actin. Asterisks (*) denote statistically significant changes from the control group ( p ≤ 0.05). DMSO , vehicle control; Cap50 , caperatic acid (50 µM); Atra50 , atranorin (50 µM); Leca50 , lecanoric acid (50 µM); Squam50 , squamatic acid (50 µM); Phys25 , physodic acid (25 µM); Salaz50 , salazinic acid (50 µM).

    Article Snippet: Human colorectal (HCT116 and DLD-1) cancer cells were obtained from the European Collection of Authenticated Cell Culture (Cell Lines Service, Eppelheim, Germany).

    Techniques: Derivative Assay, Expressing, Western Blot

    A Cell expansion of lentivirally transduced SW480 or (B) HCT-116 cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.

    Journal: Oncogene

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    doi: 10.1038/s41388-021-01847-w

    Figure Lengend Snippet: A Cell expansion of lentivirally transduced SW480 or (B) HCT-116 cells with two independent shRNAs against TGM2 (shTGM2-1, shTGM2-2) or control (shSCRMBL). C Cell expansion of SW480 and (D) HCT-116 cells after transduction with CRISPR/Cas9 constructs (TGM2 gRNA) against TGM2 or non-target (NT) control. E Mean number of tumorspheres after TGM2 knockdown in SW480 and HCT-116 cells. Data are presented as mean ± SD of at least three independent experiments. F Representative microphotographs of tumorspheres of SW480 cells 14 days after transduction with shTGM2-1, shTGM2-2, or control (shSCRMBL). Shown are fluorescent (tdTOMATO) and brightfield microphotographs. Scale bar, 200 µm. * P < 0.05; ** P < 0.01, Mann–Whitney U test.

    Article Snippet: The human colorectal cancer cell lines SW480 and HCT-116 were obtained from CLS Cell Lines Service GmbH (Eppelheim, Germany).

    Techniques: Transduction, CRISPR, Construct, MANN-WHITNEY

    A Time-lapse imaging of SW480 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. Shown are cumulative cell death events over time determined by single cell tracking. P value was calculated by log-rank test. B Percentage of apoptotic SW480 cells determined by Annexin V/7-AAD staining 72 hours after TGM2 knockdown. C Percentage of Caspase-3 positive SW480 cells 72 hours after TGM2 knockdown. D – F All experiments were repeated in HCT-116 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. D Time lapse imaging showing the cumulative cell death events. E Percentage of Annexin V positive and ( F) Caspase-3 positive HCT-116 cells 72 hours after TGM2 knockdown. Results are presented as mean ± SD of three independent experiments. *** P < 0.001, Mann–Whitney U test.

    Journal: Oncogene

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    doi: 10.1038/s41388-021-01847-w

    Figure Lengend Snippet: A Time-lapse imaging of SW480 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. Shown are cumulative cell death events over time determined by single cell tracking. P value was calculated by log-rank test. B Percentage of apoptotic SW480 cells determined by Annexin V/7-AAD staining 72 hours after TGM2 knockdown. C Percentage of Caspase-3 positive SW480 cells 72 hours after TGM2 knockdown. D – F All experiments were repeated in HCT-116 cells transduced with shTGM2-1, shTGM2-2 or shSCRMBL. D Time lapse imaging showing the cumulative cell death events. E Percentage of Annexin V positive and ( F) Caspase-3 positive HCT-116 cells 72 hours after TGM2 knockdown. Results are presented as mean ± SD of three independent experiments. *** P < 0.001, Mann–Whitney U test.

    Article Snippet: The human colorectal cancer cell lines SW480 and HCT-116 were obtained from CLS Cell Lines Service GmbH (Eppelheim, Germany).

    Techniques: Imaging, Transduction, Single Cell Tracking, Staining, MANN-WHITNEY

    A – C Gene expression profiling by RNA-seq of SW480 cells after transduction with either shTGM2-1 or shSCRMBL. A Unsupervised hierarchical clustering of the top 1000 differentially expressed genes (DEGs) upon TGM2 knockdown across the four biological replicates. B MA plot relating p values for all differentially expressed genes between shTGM2-1 and shSCRMBL from four biological replicates. Red dots indicate significantly regulated genes (adjusted P < 0.05). List of regulated genes is presented in Supplementary Table S . C Scatter plot of gene set enrichment analysis of DEGs relating the Q-value for Hallmark gene-set signatures. The top 16 enriched pathways are shown ( P < 0.05, Fold change ≥2). The color and size of each dot represent the Rich factor and the number of DEGs mapped to the indicated pathway, respectively. D Proteome analysis of regulated proteins involved in apoptosis upon shRNA-mediated TGM2 knockdown. Representative blot of Proteome Profiler Array™-Human Apoptosis Array analysis of SW480 cells. The regulation of protein expression of phosphorylated p53 variants is shown. E – H Quantification of p53 and phosphorylated p53 (S15, S46, and S392) upon TGM2 knockdown in SW480 ( E , G ) and HCT-116 ( F , H ) cells via Simple Western technology ( n = 3; Mann–Whitney U test).

    Journal: Oncogene

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    doi: 10.1038/s41388-021-01847-w

    Figure Lengend Snippet: A – C Gene expression profiling by RNA-seq of SW480 cells after transduction with either shTGM2-1 or shSCRMBL. A Unsupervised hierarchical clustering of the top 1000 differentially expressed genes (DEGs) upon TGM2 knockdown across the four biological replicates. B MA plot relating p values for all differentially expressed genes between shTGM2-1 and shSCRMBL from four biological replicates. Red dots indicate significantly regulated genes (adjusted P < 0.05). List of regulated genes is presented in Supplementary Table S . C Scatter plot of gene set enrichment analysis of DEGs relating the Q-value for Hallmark gene-set signatures. The top 16 enriched pathways are shown ( P < 0.05, Fold change ≥2). The color and size of each dot represent the Rich factor and the number of DEGs mapped to the indicated pathway, respectively. D Proteome analysis of regulated proteins involved in apoptosis upon shRNA-mediated TGM2 knockdown. Representative blot of Proteome Profiler Array™-Human Apoptosis Array analysis of SW480 cells. The regulation of protein expression of phosphorylated p53 variants is shown. E – H Quantification of p53 and phosphorylated p53 (S15, S46, and S392) upon TGM2 knockdown in SW480 ( E , G ) and HCT-116 ( F , H ) cells via Simple Western technology ( n = 3; Mann–Whitney U test).

    Article Snippet: The human colorectal cancer cell lines SW480 and HCT-116 were obtained from CLS Cell Lines Service GmbH (Eppelheim, Germany).

    Techniques: Expressing, RNA Sequencing Assay, Transduction, shRNA, Western Blot, MANN-WHITNEY

    A Representative images of proximity ligation assay (PLA) of TGM2 and p53 in SW480 cells. Cells incubated only with TGM2 antibody served as negative control (I). Protein–protein interaction of TGM2 and p53(S15) was visualized using hybridization probes labeled with Texas Red (II). Nuclei were stained with DAPI (blue). B Quantification of TGM2-p53 interaction and associated technical controls (Ctrl). Technical controls demonstrate the specificity of PLA signals. Each dot represents one cell. Mean value of PLA dots per cell is shown by the black line. C Representative images of proximity ligation assay of TGM2 and p53 in patient-derived normal epithelial cells (I) and corresponding colon cancer cells (II). D Quantification of TGM2-p53 interaction in primary patient material. (Significance was calculated using Kruskal–Wallis test). E Co-immunoprecipitation (Co-IP) of endogenous TGM2 and p53 or phosphorylated p53(S15) in SW480, HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−). F Super-resolved image of a HCT-116 cell immunostained for TGM2 (red) and p53(S15) (cyan). A zoom-in of the highlighted region is shown on the right. White regions indicate overlapping signal of TGM2 and p53(S15) (yellow arrowheads). Scale bars represent 5 µm and 1 µm, respectively.

    Journal: Oncogene

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    doi: 10.1038/s41388-021-01847-w

    Figure Lengend Snippet: A Representative images of proximity ligation assay (PLA) of TGM2 and p53 in SW480 cells. Cells incubated only with TGM2 antibody served as negative control (I). Protein–protein interaction of TGM2 and p53(S15) was visualized using hybridization probes labeled with Texas Red (II). Nuclei were stained with DAPI (blue). B Quantification of TGM2-p53 interaction and associated technical controls (Ctrl). Technical controls demonstrate the specificity of PLA signals. Each dot represents one cell. Mean value of PLA dots per cell is shown by the black line. C Representative images of proximity ligation assay of TGM2 and p53 in patient-derived normal epithelial cells (I) and corresponding colon cancer cells (II). D Quantification of TGM2-p53 interaction in primary patient material. (Significance was calculated using Kruskal–Wallis test). E Co-immunoprecipitation (Co-IP) of endogenous TGM2 and p53 or phosphorylated p53(S15) in SW480, HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−). F Super-resolved image of a HCT-116 cell immunostained for TGM2 (red) and p53(S15) (cyan). A zoom-in of the highlighted region is shown on the right. White regions indicate overlapping signal of TGM2 and p53(S15) (yellow arrowheads). Scale bars represent 5 µm and 1 µm, respectively.

    Article Snippet: The human colorectal cancer cell lines SW480 and HCT-116 were obtained from CLS Cell Lines Service GmbH (Eppelheim, Germany).

    Techniques: Proximity Ligation Assay, Incubation, Negative Control, Hybridization, Labeling, Staining, Derivative Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Knock-Out

    A – C HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−) were transduced with either shTGM2-1, shTGM2-2, or shSCRMBL. Time-lapse imaging and proliferation assay were performed to determine a rescue from cell death upon TGM2 knockdown. A Fold change of cell number of HCT-116 p53 wt and HCT-116 p53 −/− cells upon TGM2 knockdown in comparison to shSCRMBL control determined at day three after transduction. Data are presented as mean ± SD of three independent experiments (** P < 0.01, Mann–Whitney U test). B Single cell tracking of HCT-116 p53 wt and HCT-116 p53 − /− cells after TGM2 knockdown with shTGM2-1 and (C) shTGM2-2. Cumulative cell death events are shown over time (*** P < 0.001, Log-rank test). D Direct visualization of p53 activation upon TGM2 knockdown by time-lapse video-microscopy. Sequence of phase contrast images, tdTOMATO fluorescence of shTGM2-1 and p53-driven destabilized GFP reporter , depicting the same field of view over the time course of 30 hours as indicated in the corresponding panels in I–VIII. The yellow circles designate tracked cells over time. (I–VIII) show corresponding sequence of fluorescence images taken at the same time points as the phase contrast images. (I) Shown are two representative HCT-116 cells. (II and III) 6-8 hours after lentiviral transduction of shTGM2-1 both HCT-116 cells express the red fluorescent tdTOMATO reporter, indicating a knockdown of TGM2. (IV-VI) Another 4–10 hours later both cells express the green fluorescent (GFP) p53 reporter, indicating the induction of p53 activity. (VII and VIII) About 24 hours after transduction both HCT-116 cells subsequently undergo apoptosis (white arrows). Movie S shows all assembled images (3 min temporal resolution) of the same sequence.

    Journal: Oncogene

    Article Title: Transglutaminase 2 promotes tumorigenicity of colon cancer cells by inactivation of the tumor suppressor p53

    doi: 10.1038/s41388-021-01847-w

    Figure Lengend Snippet: A – C HCT-116 p53 wildtype cells (wt) and HCT-116 p53 knockout cells (−/−) were transduced with either shTGM2-1, shTGM2-2, or shSCRMBL. Time-lapse imaging and proliferation assay were performed to determine a rescue from cell death upon TGM2 knockdown. A Fold change of cell number of HCT-116 p53 wt and HCT-116 p53 −/− cells upon TGM2 knockdown in comparison to shSCRMBL control determined at day three after transduction. Data are presented as mean ± SD of three independent experiments (** P < 0.01, Mann–Whitney U test). B Single cell tracking of HCT-116 p53 wt and HCT-116 p53 − /− cells after TGM2 knockdown with shTGM2-1 and (C) shTGM2-2. Cumulative cell death events are shown over time (*** P < 0.001, Log-rank test). D Direct visualization of p53 activation upon TGM2 knockdown by time-lapse video-microscopy. Sequence of phase contrast images, tdTOMATO fluorescence of shTGM2-1 and p53-driven destabilized GFP reporter , depicting the same field of view over the time course of 30 hours as indicated in the corresponding panels in I–VIII. The yellow circles designate tracked cells over time. (I–VIII) show corresponding sequence of fluorescence images taken at the same time points as the phase contrast images. (I) Shown are two representative HCT-116 cells. (II and III) 6-8 hours after lentiviral transduction of shTGM2-1 both HCT-116 cells express the red fluorescent tdTOMATO reporter, indicating a knockdown of TGM2. (IV-VI) Another 4–10 hours later both cells express the green fluorescent (GFP) p53 reporter, indicating the induction of p53 activity. (VII and VIII) About 24 hours after transduction both HCT-116 cells subsequently undergo apoptosis (white arrows). Movie S shows all assembled images (3 min temporal resolution) of the same sequence.

    Article Snippet: The human colorectal cancer cell lines SW480 and HCT-116 were obtained from CLS Cell Lines Service GmbH (Eppelheim, Germany).

    Techniques: Knock-Out, Transduction, Imaging, Proliferation Assay, MANN-WHITNEY, Single Cell Tracking, Activation Assay, Microscopy, Sequencing, Fluorescence, Activity Assay