nci h226  (ATCC)


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    ATCC nci h226
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Nci H226, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nci h226/product/ATCC
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nci h226 - by Bioz Stars, 2024-05
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    1) Product Images from "Streptococcus pneumoniae promotes lung cancer development and progression"

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    Journal: iScience

    doi: 10.1016/j.isci.2022.105923

    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Figure Legend Snippet: SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Techniques Used: Binding Assay, Expressing, Western Blot, Infection, Mutagenesis, Staining

    SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.
    Figure Legend Snippet: SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.

    Techniques Used: Mutagenesis, Expressing, Incubation, Migration, Western Blot, Plasmid Preparation, Sequencing

    SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Figure Legend Snippet: SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Techniques Used: Expressing, Western Blot, Incubation, Plasmid Preparation


    Figure Legend Snippet:

    Techniques Used: Recombinant, Modification, Plasmid Preparation, Software

    crl 5826 nci h2087 atcc  (ATCC)


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    Structured Review

    ATCC crl 5826 nci h2087 atcc
    Crl 5826 Nci H2087 Atcc, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/crl 5826 nci h2087 atcc/product/ATCC
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    crl 5826 nci h2087 atcc - by Bioz Stars, 2024-05
    86/100 stars

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    nci h226  (ATCC)


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    Structured Review

    ATCC nci h226
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Nci H226, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nci h226/product/ATCC
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nci h226 - by Bioz Stars, 2024-05
    99/100 stars

    Images

    1) Product Images from "Streptococcus pneumoniae promotes lung cancer development and progression"

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    Journal: iScience

    doi: 10.1016/j.isci.2022.105923

    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Figure Legend Snippet: SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Techniques Used: Binding Assay, Expressing, Western Blot, Infection, Mutagenesis, Staining

    SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.
    Figure Legend Snippet: SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.

    Techniques Used: Mutagenesis, Expressing, Incubation, Migration, Western Blot, Plasmid Preparation, Sequencing

    SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Figure Legend Snippet: SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Techniques Used: Expressing, Western Blot, Incubation, Plasmid Preparation


    Figure Legend Snippet:

    Techniques Used: Recombinant, Modification, Plasmid Preparation, Software

    nci h226  (ATCC)


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    ATCC nci h226
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    ATCC crl
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    nci h22  (ATCC)


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    ATCC nci h22
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    nci h226  (ATCC)


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    ATCC nci h226
    In vitro growth inhibition and lethality obtained from the single dose (10 µM) test of compounds 5a – h .
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    1) Product Images from "New Insights into the Structural Requirements of Isatin-Derived Pro-Apoptotic Agents against Acute Myeloid Leukemia"

    Article Title: New Insights into the Structural Requirements of Isatin-Derived Pro-Apoptotic Agents against Acute Myeloid Leukemia

    Journal: Pharmaceuticals

    doi: 10.3390/ph15121579

    In vitro growth inhibition and lethality obtained from the single dose (10 µM) test of compounds 5a – h .
    Figure Legend Snippet: In vitro growth inhibition and lethality obtained from the single dose (10 µM) test of compounds 5a – h .

    Techniques Used: In Vitro, Inhibition

    nci h226 human squamous cell carcinoma cell lines  (ATCC)


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    ATCC nci h226 human squamous cell carcinoma cell lines
    (A,B) <t>NCI-H226</t> and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.
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    1) Product Images from "Attenuation of Eph Receptor Kinase Activation in Cancer Cells by Coexpressed Ephrin Ligands"

    Article Title: Attenuation of Eph Receptor Kinase Activation in Cancer Cells by Coexpressed Ephrin Ligands

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0081445

    (A,B) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.
    Figure Legend Snippet: (A,B) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.

    Techniques Used: Infection, Western Blot, Expressing, Immunoprecipitation

    (A) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. The histograms show the binding of ephrin-A5 AP to NCI-H226 cells and ephrin-A3 AP to A549 cells, revealing that ephrin-A3 coexpression prevents the binding of ephrin AP proteins to EphA3. Normalized means from 2 experiments (each with triplicate samples) ± SE are shown. **p<0.01 by one-way ANOVA and Dunnett’s post-hoc test for the comparison with cells expressing only EphA3. The immunoblots show expression of EphA3, ephrin-A3, and β-tubulin as loading control in cell lysates, verifying that ephrin-A3 coexpression did not reduce EphA3 levels. In fact, EphA3 levels appeared higher in A549 cells co-expressing ephrin-A3. The white space indicates removal of an irrelevant lane. (B) Cell surface biotinylation followed by an ELISA where EphA3 was captured with an immobilized antibody and its biotinylation detected with streptavidin-HRP reveals a similar fraction of EphA3 on the surface of cells expressing EphA3 alone or together with ephrin-A3. The histogram shows means from 2 experiments (each with triplicate samples) ± SE. Incubation with twice as much lysates yielded similar results, indicating that maximal EphA3 binding to the antibody immobilized in the wells was achieved. **p<0.01 by one-way ANOVA and Tukey’s post-hoc test for the comparison with cells expressing mCherry and ZsGreen; p>0.05 for the comparison of cells expressing EphA3 with and without ephrin-A3. (C) EphA3 Fc was used for pull-downs from conditioned medium and lysates of A549 or H226 cells infected with the indicated lentiviruses. By immunoblotting with an anti-dsRed antibody, ephrin-A3 was detected only in the lysates. The pull-downs were also probed for Fc to verify the levels of EphA3 Fc. (D) Surface proteins were biotinylated in cells infected with lentiviruses encoding mCherry, mCherry-ephrin-A3, or mCherry-ephrin-A3 together with EphA3 and ZsGreen. mCherry-ephrin-A3 immunoprecipitates (with anti-dsRed antibody) were probed with streptavidin-HRP, demonstrating similar cell surface levels of ephrin-A3 expressed alone or together with EphA3. IgG, control immunoprecipitate with non-immune IgGs. Lysates were probed for mCherry-ephrin-A3 with anti-dsRed antibody.
    Figure Legend Snippet: (A) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. The histograms show the binding of ephrin-A5 AP to NCI-H226 cells and ephrin-A3 AP to A549 cells, revealing that ephrin-A3 coexpression prevents the binding of ephrin AP proteins to EphA3. Normalized means from 2 experiments (each with triplicate samples) ± SE are shown. **p<0.01 by one-way ANOVA and Dunnett’s post-hoc test for the comparison with cells expressing only EphA3. The immunoblots show expression of EphA3, ephrin-A3, and β-tubulin as loading control in cell lysates, verifying that ephrin-A3 coexpression did not reduce EphA3 levels. In fact, EphA3 levels appeared higher in A549 cells co-expressing ephrin-A3. The white space indicates removal of an irrelevant lane. (B) Cell surface biotinylation followed by an ELISA where EphA3 was captured with an immobilized antibody and its biotinylation detected with streptavidin-HRP reveals a similar fraction of EphA3 on the surface of cells expressing EphA3 alone or together with ephrin-A3. The histogram shows means from 2 experiments (each with triplicate samples) ± SE. Incubation with twice as much lysates yielded similar results, indicating that maximal EphA3 binding to the antibody immobilized in the wells was achieved. **p<0.01 by one-way ANOVA and Tukey’s post-hoc test for the comparison with cells expressing mCherry and ZsGreen; p>0.05 for the comparison of cells expressing EphA3 with and without ephrin-A3. (C) EphA3 Fc was used for pull-downs from conditioned medium and lysates of A549 or H226 cells infected with the indicated lentiviruses. By immunoblotting with an anti-dsRed antibody, ephrin-A3 was detected only in the lysates. The pull-downs were also probed for Fc to verify the levels of EphA3 Fc. (D) Surface proteins were biotinylated in cells infected with lentiviruses encoding mCherry, mCherry-ephrin-A3, or mCherry-ephrin-A3 together with EphA3 and ZsGreen. mCherry-ephrin-A3 immunoprecipitates (with anti-dsRed antibody) were probed with streptavidin-HRP, demonstrating similar cell surface levels of ephrin-A3 expressed alone or together with EphA3. IgG, control immunoprecipitate with non-immune IgGs. Lysates were probed for mCherry-ephrin-A3 with anti-dsRed antibody.

    Techniques Used: Infection, Binding Assay, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Incubation

    nci h226  (ATCC)


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    ATCC nci h226
    A. Pictures were acquired at the beginning of the experiment (t = 0, immediately after wounding) and from the same field at the end of the experiment (t = 24 h for this example from the Calu-1 cell line). B. Quantification of wound closure for the three cell lines (BEAS-2B, <t>NCI-H226</t> and Calu-1). Wound sizes were measured at the beginning and end of the experiment to calculate the percentage of wound closure for control and SOX2 over-expressing cells for each of the three cell lines. SOX2 over-expression significantly stimulates cell migration compared to control cells (student's t-test).
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    1) Product Images from "SOX2 Is an Oncogene Activated by Recurrent 3q26.3 Amplifications in Human Lung Squamous Cell Carcinomas"

    Article Title: SOX2 Is an Oncogene Activated by Recurrent 3q26.3 Amplifications in Human Lung Squamous Cell Carcinomas

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0008960

    A. Pictures were acquired at the beginning of the experiment (t = 0, immediately after wounding) and from the same field at the end of the experiment (t = 24 h for this example from the Calu-1 cell line). B. Quantification of wound closure for the three cell lines (BEAS-2B, NCI-H226 and Calu-1). Wound sizes were measured at the beginning and end of the experiment to calculate the percentage of wound closure for control and SOX2 over-expressing cells for each of the three cell lines. SOX2 over-expression significantly stimulates cell migration compared to control cells (student's t-test).
    Figure Legend Snippet: A. Pictures were acquired at the beginning of the experiment (t = 0, immediately after wounding) and from the same field at the end of the experiment (t = 24 h for this example from the Calu-1 cell line). B. Quantification of wound closure for the three cell lines (BEAS-2B, NCI-H226 and Calu-1). Wound sizes were measured at the beginning and end of the experiment to calculate the percentage of wound closure for control and SOX2 over-expressing cells for each of the three cell lines. SOX2 over-expression significantly stimulates cell migration compared to control cells (student's t-test).

    Techniques Used: Expressing, Over Expression, Migration

    A. Tumor incidence upon subcutaneous implantation of human lung squamous control- and SOX2-transduced cell lines in nude mice. For each cell line, the number of tumors that developed is represented with respect to the number of injections for each cell type (control or SOX2-transduced, n = 4 injected animals each). Tumor incidence is unchanged for the NCI-H226 highly tumorigenic cell line, whereas BEAS-2B cells become tumorigenic upon Sox2 over-expression. B. Hematoxylin and Eosin (H&E) staining of a representative area of a BEAS-2B-Sox2 subcutaneous tumor (magnification = 100×). A majority of the tumor area (around 80%) has typical traits of poorly differentiated basaloid variants of squamous cell carcinoma. C. H&E staining of representative areas of the same BEAS-2B-Sox2 subcutaneous tumor as in panel B (magnification = 100×). Around 20% of the tumor area has typical traits of poorly to moderately differentiated squamous cell carcinoma, with individual cell keratinization. D. H&E staining of one BEAS-2B-Sox2 subcutaneous tumor (magnification = 50×). In this case, local tumor cell invasion into the dermis was observed (arrowheads). E. Immunohistochemistry for SOX2, Keratins 5/6 and Ki67 (left, middle and right panels, respectively; magnifications = 200×). Tumors homogeneously express SOX2 and Ki67 and heterogeneously express Keratins 5/6, which are squamous cell differentiation markers.
    Figure Legend Snippet: A. Tumor incidence upon subcutaneous implantation of human lung squamous control- and SOX2-transduced cell lines in nude mice. For each cell line, the number of tumors that developed is represented with respect to the number of injections for each cell type (control or SOX2-transduced, n = 4 injected animals each). Tumor incidence is unchanged for the NCI-H226 highly tumorigenic cell line, whereas BEAS-2B cells become tumorigenic upon Sox2 over-expression. B. Hematoxylin and Eosin (H&E) staining of a representative area of a BEAS-2B-Sox2 subcutaneous tumor (magnification = 100×). A majority of the tumor area (around 80%) has typical traits of poorly differentiated basaloid variants of squamous cell carcinoma. C. H&E staining of representative areas of the same BEAS-2B-Sox2 subcutaneous tumor as in panel B (magnification = 100×). Around 20% of the tumor area has typical traits of poorly to moderately differentiated squamous cell carcinoma, with individual cell keratinization. D. H&E staining of one BEAS-2B-Sox2 subcutaneous tumor (magnification = 50×). In this case, local tumor cell invasion into the dermis was observed (arrowheads). E. Immunohistochemistry for SOX2, Keratins 5/6 and Ki67 (left, middle and right panels, respectively; magnifications = 200×). Tumors homogeneously express SOX2 and Ki67 and heterogeneously express Keratins 5/6, which are squamous cell differentiation markers.

    Techniques Used: Injection, Over Expression, Staining, Immunohistochemistry, Cell Differentiation

    nci h226 nsclc  (ATCC)


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    ATCC nci h226 nsclc
    Percentage of in vitro tumor cell lines growth at 10 μM for compounds
    Nci H226 Nsclc, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines"

    Article Title: Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines

    Journal: Scientia Pharmaceutica

    doi: 10.3797/scipharm.1211-08

    Percentage of in vitro tumor cell lines growth at 10 μM for compounds
    Figure Legend Snippet: Percentage of in vitro tumor cell lines growth at 10 μM for compounds

    Techniques Used: In Vitro

    The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)
    Figure Legend Snippet: The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)

    Techniques Used:

    nci h226 nsclc  (ATCC)


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    Structured Review

    ATCC nci h226 nsclc
    Percentage of in vitro tumor cell lines growth at 10 μM for compounds
    Nci H226 Nsclc, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines"

    Article Title: Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines

    Journal: Scientia Pharmaceutica

    doi: 10.3797/scipharm.1211-08

    Percentage of in vitro tumor cell lines growth at 10 μM for compounds
    Figure Legend Snippet: Percentage of in vitro tumor cell lines growth at 10 μM for compounds

    Techniques Used: In Vitro

    The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)
    Figure Legend Snippet: The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)

    Techniques Used:

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  • 99
    ATCC nci h226
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Nci H226, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    ATCC crl 5826 nci h2087 atcc
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Crl 5826 Nci H2087 Atcc, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    crl  (ATCC)
    99
    ATCC crl
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Crl, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC nci h22
    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines <t>(H226,</t> H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.
    Nci H22, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC nci h226 human squamous cell carcinoma cell lines
    (A,B) <t>NCI-H226</t> and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.
    Nci H226 Human Squamous Cell Carcinoma Cell Lines, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC nci h226 nsclc
    Percentage of in vitro tumor cell lines growth at 10 μM for compounds
    Nci H226 Nsclc, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Journal: iScience

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    doi: 10.1016/j.isci.2022.105923

    Figure Lengend Snippet: SP attaches to and invades lung cancer cells via binding PspC to PAFR (A) PAFR expression was determined in cancer cell lines (H226, H460, and H1299) and a normal lung epithelial cell line (BEAS-2B) by Western blot. GAPDH was used as the loading control. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. H460 and H1299 cells had a higher level of PAFR expression compared with H226 cells and BEAS-2B cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) SP adhered to and invaded the PAFR-expressing cells (H226 and H1299). Bacteria were added to cells at a multiplicity of infection (MOI) of 10 for 1 h. The PspC-deficient mutant SP and heat-killed SP were defective for attachment and invasion compared to wild-type SP and the PspA-deficient mutant SP . E. faecalis did not attach to and invade lung cancer cells. Cells treated with PBS were used as negative controls. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) FISH analysis of SP using an Alexa Fluor 594-conjugated specific probe (Red) to SP . 4′,6-diamidino-2-phenylindole (DAPI) was used to visualize nuclear DNA of cells. Original magnification, X400. Three independent experiments were performed with consistent results. H460 and H1299 cells showed positive staining for SP (Red signals). Scale bar, 10 μm. (D) The depletion of PAFR in H460 and H1299 cells by using siRNA reduced attachment and invasion of SP . Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) The PAFR inhibitor, WEB2086, suppressed attachment and invasion of SP to H460 and H1299 cells in a dose-dependent manner (10, 30, and 60 μM and 1,000 μM WEB2086 were used). ∗p < 0.01. (F) Enforced expression of PAFR in H226 cells increased attachment and invasion of wild-type SP and PspA-deficient mutant SP , but not PspC-deficient mutant SP . All the results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Article Snippet: NCI-H226 , ATCC , CRL-5826.

    Techniques: Binding Assay, Expressing, Western Blot, Infection, Mutagenesis, Staining

    SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.

    Journal: iScience

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    doi: 10.1016/j.isci.2022.105923

    Figure Lengend Snippet: SP promotes the tumorigenicity of lung cancer by integrating PspC and PAFR (A) Wild-type and PspA-deficient mutant SPs stimulated proliferation of PAFR-expressing lung cancer cells (H460 and H1299) compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis . Cells were incubated with bacteria at an MOI of 1000:1 for up to 48 h. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (B) Wild-type and PspA-deficient mutant SPs promoted migration of PAFR-expressing lung cancer cells, compared to untreated cells or those incubated with PspC-deficient mutant SP , heat-killed SP, and E. faecalis after 48-h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PAFR in PAFR-expressing lung cancer cells, H460, and H1299 cells. Western blots showed that PAFR expression level was effectively reduced. (D) SP -stimulated cell proliferation was inhibited by the depletion of PAFR in H460 and H1299 cells. Left panel showed the results of H460 cells with depletion of PAFR that were treated differently. Right panel displayed the results of H1299 cells with depletion of PAFR that were treated differently. (E) SP -stimulated cell migration was suppressed by the depletion of PAFR in H460 and H1299. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. Red columns showed the results of H460 or H1299 cancer cells without depletion of PAFR. Blue columns indicated the results of H460 or H1299 cancer cells with depletion of PAFR. The depletion of PAFR in H460 and H1299 cancer cells decreased the effect of SP on cell migration. (F) SP -stimulated cell proliferation of H460 and H1299 cells was inhibited by the PAFR inhibitor, WEB2086 (WEB), in a dose-dependent manner. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (G) SP -stimulated cell migration of H460 and H1299 was inhibited by WEB2086. (H) H226 cells were forced to overexpress PAFR by using a PAFR-overexpressing plasmid. A vector expressing sequence lacking homology to the human genome databases was used as a control. SP -stimulated cell proliferation was elevated by enforced PAFR expression in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (I) SP -stimulated cell migration was elevated by enforced PAFR expression in H226 cells after 48 h treatment. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. The red column was wild-type H226 cancer cells that had a low expression level of PAFR. The blue column was H226 cancer cells with forced PAFR expression.

    Article Snippet: NCI-H226 , ATCC , CRL-5826.

    Techniques: Mutagenesis, Expressing, Incubation, Migration, Western Blot, Plasmid Preparation, Sequencing

    SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Journal: iScience

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    doi: 10.1016/j.isci.2022.105923

    Figure Lengend Snippet: SP promotes lung tumorigenesis by stimulating PI3K/AKT and NF-kB signaling pathways (A) PAFR-expressing H460 and H1299 cells treated with SP were analyzed by Western blot to determine expression of PI3K, AKT, and NF-kB. The cancer cells incubated with SP had higher expression levels of PI3K, AKT, and NF-kB compared with cells treated with PBS after 48 h treatment. Band intensity was determined by using ImageJ, and the ratio of each band was normalized to the corresponding GAPDH and shown below each band. SP activated PI3K, AKT, and NF-kB in H460 and H1299 cells. (B) siRNA was used to deplete PAFR in H460 and H1299. The cells were treated with SP . SP-induced activations of PI3K, AKT, and NF-kB were inhibited by the depletion of PAFR in the cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (C) siRNA was used to deplete PI3K, AKT, and NF-kB in H460 and H1299, respectively. The deletion of PI3K, AKT, or NF-kB decreased the SP -stimulated cell proliferation in the cancer cells. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (D) PCR array was used to analyze the inflammatory cytokine gene expression. SP activated pro-inflammatory cytokines (IL-1β, IL-4, IL-6, IL-8, IL-11, IL-12, TNF-α, and MCP-1) (Red). Expression levels of the cytokines in the cells treated with PBS were designated as “1” (Blue). The results are presented as the mean ± SD of three different experiments with triplicates. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA. (E) Forced expression of PAFR in H226 cells was done by using PAFR-overexpressing plasmid. Enforced PAFR expression in the cancer cells increased SP-stimulated activations of PI3K, AKT, and NF-kB determined by Western Blots. (F) Enforced PAFR expression in H226 cells activated cytokines in H226 cancer cells (Red). Expression levels of the cytokines in the H226 with forced PAFR expression treated with PBS (Blue) were designated as “1”. Data presented as mean ± SEM (n = 3); ∗p < 0.01 by one-way ANOVA.

    Article Snippet: NCI-H226 , ATCC , CRL-5826.

    Techniques: Expressing, Western Blot, Incubation, Plasmid Preparation

    Journal: iScience

    Article Title: Streptococcus pneumoniae promotes lung cancer development and progression

    doi: 10.1016/j.isci.2022.105923

    Figure Lengend Snippet:

    Article Snippet: NCI-H226 , ATCC , CRL-5826.

    Techniques: Recombinant, Modification, Plasmid Preparation, Software

    (A,B) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.

    Journal: PLoS ONE

    Article Title: Attenuation of Eph Receptor Kinase Activation in Cancer Cells by Coexpressed Ephrin Ligands

    doi: 10.1371/journal.pone.0081445

    Figure Lengend Snippet: (A,B) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. EphA3 immunoprecipitates were probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA3. Lysates were probed for mCherry-ephrin-A3 with an anti-dsRed antibody that also recognizes mCherry, for EphA3, and for β-tubulin as loading control. The histograms show normalized means ± SE quantified from 3 immunoblots in both A and B. In one of the A549 experiments used for quantification, the cells were stimulated with ephrin-A5 Fc. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing both EphA3 and ephrin-A3 with ephrin-A3 Fc-treated cells expressing only EphA3. Of note, EphA3 levels were higher in A549 cells co-expressing ephrin-A3/ephrin-B2 (see also , , and ), suggesting that this receptor may be stabilized by the coexpressed ephrins. (C) A549 cells were infected with a lentivirus encoding mCherry-ephrin-A3 or mCherry as a control. Immunoprecipitated endogenous EphA2 was probed by immunoblotting for phosphotyrosine (PTyr) and reprobed for EphA2. Lysates were probed with an anti-dsRed antibody and β-tubulin as loading control. The histogram shows normalized means ± SE quantified from 3 immunoblots. **p<0.01 by one sample t test for the comparison of ephrin-A3 Fc-treated cells expressing or not expressing ephrin-A3.

    Article Snippet: The A549 human lung adenocarcinoma and NCI-H226 human squamous cell carcinoma cell lines (ATCC) were grown in Roswell Park Memorial Institute (RPMI) culture medium with the same supplements used for DMEM.

    Techniques: Infection, Western Blot, Expressing, Immunoprecipitation

    (A) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. The histograms show the binding of ephrin-A5 AP to NCI-H226 cells and ephrin-A3 AP to A549 cells, revealing that ephrin-A3 coexpression prevents the binding of ephrin AP proteins to EphA3. Normalized means from 2 experiments (each with triplicate samples) ± SE are shown. **p<0.01 by one-way ANOVA and Dunnett’s post-hoc test for the comparison with cells expressing only EphA3. The immunoblots show expression of EphA3, ephrin-A3, and β-tubulin as loading control in cell lysates, verifying that ephrin-A3 coexpression did not reduce EphA3 levels. In fact, EphA3 levels appeared higher in A549 cells co-expressing ephrin-A3. The white space indicates removal of an irrelevant lane. (B) Cell surface biotinylation followed by an ELISA where EphA3 was captured with an immobilized antibody and its biotinylation detected with streptavidin-HRP reveals a similar fraction of EphA3 on the surface of cells expressing EphA3 alone or together with ephrin-A3. The histogram shows means from 2 experiments (each with triplicate samples) ± SE. Incubation with twice as much lysates yielded similar results, indicating that maximal EphA3 binding to the antibody immobilized in the wells was achieved. **p<0.01 by one-way ANOVA and Tukey’s post-hoc test for the comparison with cells expressing mCherry and ZsGreen; p>0.05 for the comparison of cells expressing EphA3 with and without ephrin-A3. (C) EphA3 Fc was used for pull-downs from conditioned medium and lysates of A549 or H226 cells infected with the indicated lentiviruses. By immunoblotting with an anti-dsRed antibody, ephrin-A3 was detected only in the lysates. The pull-downs were also probed for Fc to verify the levels of EphA3 Fc. (D) Surface proteins were biotinylated in cells infected with lentiviruses encoding mCherry, mCherry-ephrin-A3, or mCherry-ephrin-A3 together with EphA3 and ZsGreen. mCherry-ephrin-A3 immunoprecipitates (with anti-dsRed antibody) were probed with streptavidin-HRP, demonstrating similar cell surface levels of ephrin-A3 expressed alone or together with EphA3. IgG, control immunoprecipitate with non-immune IgGs. Lysates were probed for mCherry-ephrin-A3 with anti-dsRed antibody.

    Journal: PLoS ONE

    Article Title: Attenuation of Eph Receptor Kinase Activation in Cancer Cells by Coexpressed Ephrin Ligands

    doi: 10.1371/journal.pone.0081445

    Figure Lengend Snippet: (A) NCI-H226 and A549 lung cancer cells were infected with a lentivirus encoding EphA3 and ZsGreen alone or together with a lentivirus encoding mCherry-ephrin-A3; control cells were infected with lentiviruses encoding ZsGreen and mCherry. The histograms show the binding of ephrin-A5 AP to NCI-H226 cells and ephrin-A3 AP to A549 cells, revealing that ephrin-A3 coexpression prevents the binding of ephrin AP proteins to EphA3. Normalized means from 2 experiments (each with triplicate samples) ± SE are shown. **p<0.01 by one-way ANOVA and Dunnett’s post-hoc test for the comparison with cells expressing only EphA3. The immunoblots show expression of EphA3, ephrin-A3, and β-tubulin as loading control in cell lysates, verifying that ephrin-A3 coexpression did not reduce EphA3 levels. In fact, EphA3 levels appeared higher in A549 cells co-expressing ephrin-A3. The white space indicates removal of an irrelevant lane. (B) Cell surface biotinylation followed by an ELISA where EphA3 was captured with an immobilized antibody and its biotinylation detected with streptavidin-HRP reveals a similar fraction of EphA3 on the surface of cells expressing EphA3 alone or together with ephrin-A3. The histogram shows means from 2 experiments (each with triplicate samples) ± SE. Incubation with twice as much lysates yielded similar results, indicating that maximal EphA3 binding to the antibody immobilized in the wells was achieved. **p<0.01 by one-way ANOVA and Tukey’s post-hoc test for the comparison with cells expressing mCherry and ZsGreen; p>0.05 for the comparison of cells expressing EphA3 with and without ephrin-A3. (C) EphA3 Fc was used for pull-downs from conditioned medium and lysates of A549 or H226 cells infected with the indicated lentiviruses. By immunoblotting with an anti-dsRed antibody, ephrin-A3 was detected only in the lysates. The pull-downs were also probed for Fc to verify the levels of EphA3 Fc. (D) Surface proteins were biotinylated in cells infected with lentiviruses encoding mCherry, mCherry-ephrin-A3, or mCherry-ephrin-A3 together with EphA3 and ZsGreen. mCherry-ephrin-A3 immunoprecipitates (with anti-dsRed antibody) were probed with streptavidin-HRP, demonstrating similar cell surface levels of ephrin-A3 expressed alone or together with EphA3. IgG, control immunoprecipitate with non-immune IgGs. Lysates were probed for mCherry-ephrin-A3 with anti-dsRed antibody.

    Article Snippet: The A549 human lung adenocarcinoma and NCI-H226 human squamous cell carcinoma cell lines (ATCC) were grown in Roswell Park Memorial Institute (RPMI) culture medium with the same supplements used for DMEM.

    Techniques: Infection, Binding Assay, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay, Incubation

    Percentage of in vitro tumor cell lines growth at 10 μM for compounds

    Journal: Scientia Pharmaceutica

    Article Title: Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines

    doi: 10.3797/scipharm.1211-08

    Figure Lengend Snippet: Percentage of in vitro tumor cell lines growth at 10 μM for compounds

    Article Snippet: 3.20 , 30.8 , , −22.19–76.81 , 34.45 (A549/ATCC/nscLC), 47.80 (EKVX/nscLC), 31.79 (HOP-62/nscLC), −20.29 (HOP-92/nscLC), 53.15 (NCI-H226/nscLC), 56.08 (NCI-H23/nscLC), 49.63 (NCI-H322M/nscLC), 6.93 (NCI-H460/nscLC), 18.28 (NCI-H522/nscLC), 48.35 (COLO 205/ColC), 28.33 (HCT-116/ColC), 37.98 (HCT-15/ColC), 12.96 (HT29/ColC), 28.18 (KM12/ColC), 18.19 (SW-620/ColC), 52.47 (BT-549/BC), −8.25 (HS 578T/BC), 0.99 (MCF7/BC), 54.69 (MDA-MB-231/ATCC/BC), −8.47 (MDA-MB-435/BC), 66.42 (NCI/ADR-RES/BC), 50.41 (T-47D/BC), 43.70 (IGROV1/OV), 8.02 (OVCAR-3/OV), 52.75 (OVCAR-4/OV), 24.28 (OVCAR-8/OV), 59.20 (SK-OV-3/OV), 16.34 (CCRF-CEM/L), −22.19 (HL-60(TB)/L), 13.53 (K-562/L), 30.40 (MOLT-4/L), 24.50 (RPMI-8226/L), 6.80 (SR/L), 34.92 (786-0/RC), −8.58 (A498/RC), 39.91 (ACHN/RC), 28.32 (CAKI-1/RC), 15.38 (RXF 393/RC), 56.09 (SN12C/RC), 59.47 (TK-10/RC), 54.96 (UO-31/RC), 42.29 (LOX IMVI/M), 40.18 (M14/M), 18.32 (MALME-3M/M), 63.78 (SK-MEL-2/M), 59.92 (SK-M EL-28/M), −9.71 (SK-MEL-5/M), 33.49 (UACC-257/M), 49.90 (UACC-62/M), 40.89 (DU-145/PC), 44.69 (SF-268/CNSC), −21.73 (SF-295/CNSC), 16.51 (SF-539/CNSC), 44.03 (SNB-19/CNSC), 27.05 (SNB-75/CNSC),.

    Techniques: In Vitro

    The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)

    Journal: Scientia Pharmaceutica

    Article Title: Synthesis and Anticancer Activity of 2-(Alkyl-, Alkaryl-, Aryl-, Hetaryl-)-[1,2,4]triazolo[1,5- c ]quinazolines

    doi: 10.3797/scipharm.1211-08

    Figure Lengend Snippet: The influence of compounds on the growth of individual tumor cell lines (GI 50 ≤1.00 μM)

    Article Snippet: 3.20 , 30.8 , , −22.19–76.81 , 34.45 (A549/ATCC/nscLC), 47.80 (EKVX/nscLC), 31.79 (HOP-62/nscLC), −20.29 (HOP-92/nscLC), 53.15 (NCI-H226/nscLC), 56.08 (NCI-H23/nscLC), 49.63 (NCI-H322M/nscLC), 6.93 (NCI-H460/nscLC), 18.28 (NCI-H522/nscLC), 48.35 (COLO 205/ColC), 28.33 (HCT-116/ColC), 37.98 (HCT-15/ColC), 12.96 (HT29/ColC), 28.18 (KM12/ColC), 18.19 (SW-620/ColC), 52.47 (BT-549/BC), −8.25 (HS 578T/BC), 0.99 (MCF7/BC), 54.69 (MDA-MB-231/ATCC/BC), −8.47 (MDA-MB-435/BC), 66.42 (NCI/ADR-RES/BC), 50.41 (T-47D/BC), 43.70 (IGROV1/OV), 8.02 (OVCAR-3/OV), 52.75 (OVCAR-4/OV), 24.28 (OVCAR-8/OV), 59.20 (SK-OV-3/OV), 16.34 (CCRF-CEM/L), −22.19 (HL-60(TB)/L), 13.53 (K-562/L), 30.40 (MOLT-4/L), 24.50 (RPMI-8226/L), 6.80 (SR/L), 34.92 (786-0/RC), −8.58 (A498/RC), 39.91 (ACHN/RC), 28.32 (CAKI-1/RC), 15.38 (RXF 393/RC), 56.09 (SN12C/RC), 59.47 (TK-10/RC), 54.96 (UO-31/RC), 42.29 (LOX IMVI/M), 40.18 (M14/M), 18.32 (MALME-3M/M), 63.78 (SK-MEL-2/M), 59.92 (SK-M EL-28/M), −9.71 (SK-MEL-5/M), 33.49 (UACC-257/M), 49.90 (UACC-62/M), 40.89 (DU-145/PC), 44.69 (SF-268/CNSC), −21.73 (SF-295/CNSC), 16.51 (SF-539/CNSC), 44.03 (SNB-19/CNSC), 27.05 (SNB-75/CNSC),.

    Techniques: