a498  (ATCC)


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    ATCC a498
    Effects of luteolin on <t>A498</t> and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
    A498, 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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    1) Product Images from "Induction of Apoptosis by Luteolin Involving Akt Inactivation in Human 786-O Renal Cell Carcinoma Cells"

    Article Title: Induction of Apoptosis by Luteolin Involving Akt Inactivation in Human 786-O Renal Cell Carcinoma Cells

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2013/109105

    Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
    Figure Legend Snippet: Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.

    Techniques Used: Isolation, Caspase-3 Assay, Western Blot

    a498 htb 44  (ATCC)


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    ATCC a498 htb 44
    A498 Htb 44, 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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    a498 htb 44  (ATCC)


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    ATCC a498 htb 44
    A498 Htb 44, 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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    a498 htb 44  (ATCC)


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    ATCC a498 htb 44
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    a498 htb 44 cell lines  (ATCC)


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    ATCC a498 htb 44 cell lines
    A498 Htb 44 Cell Lines, 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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    a498  (ATCC)


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    ATCC a498
    Effects of luteolin on <t>A498</t> and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
    A498, 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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    1) Product Images from "Induction of Apoptosis by Luteolin Involving Akt Inactivation in Human 786-O Renal Cell Carcinoma Cells"

    Article Title: Induction of Apoptosis by Luteolin Involving Akt Inactivation in Human 786-O Renal Cell Carcinoma Cells

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2013/109105

    Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
    Figure Legend Snippet: Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.

    Techniques Used: Isolation, Caspase-3 Assay, Western Blot

    a498  (ATCC)


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    ATCC a498
    Everolimus (RAD001) induces autophagy in RCCs. Notes: ( A , B ) 786-O and <t>A498</t> cell lines were treated by RAD001 with different concentrations (0, 0.01, 0.1, 1, 10, and 20 μmol/L) for 24 hours. ( A ) Immunoblotting showed that RAD001 induced autophagy indicators including upregulation of LC3-II/I and downregulation of p62 in a dose-dependent manner. ( B ) Quantification of the immunoblots. * P <0.05 versus 0 μmol/L group. n=3. ( C , D ) 786-O and A498 cell lines were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( C ) Immunoblotting showed that RAD001 induced autophagy in 786-O and A498 cells as time prolonged, which peaked at 8 hours. ( D ) Quantification of the immunoblots. * P <0.05 versus 0 hour group. n=3. Abbreviation: RCCs, renal cell carcinoma cells.
    A498, 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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    1) Product Images from "Attenuation of everolimus-induced cytotoxicity by a protective autophagic pathway involving ERK activation in renal cell carcinoma cells"

    Article Title: Attenuation of everolimus-induced cytotoxicity by a protective autophagic pathway involving ERK activation in renal cell carcinoma cells

    Journal: Drug Design, Development and Therapy

    doi: 10.2147/DDDT.S160557

    Everolimus (RAD001) induces autophagy in RCCs. Notes: ( A , B ) 786-O and A498 cell lines were treated by RAD001 with different concentrations (0, 0.01, 0.1, 1, 10, and 20 μmol/L) for 24 hours. ( A ) Immunoblotting showed that RAD001 induced autophagy indicators including upregulation of LC3-II/I and downregulation of p62 in a dose-dependent manner. ( B ) Quantification of the immunoblots. * P <0.05 versus 0 μmol/L group. n=3. ( C , D ) 786-O and A498 cell lines were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( C ) Immunoblotting showed that RAD001 induced autophagy in 786-O and A498 cells as time prolonged, which peaked at 8 hours. ( D ) Quantification of the immunoblots. * P <0.05 versus 0 hour group. n=3. Abbreviation: RCCs, renal cell carcinoma cells.
    Figure Legend Snippet: Everolimus (RAD001) induces autophagy in RCCs. Notes: ( A , B ) 786-O and A498 cell lines were treated by RAD001 with different concentrations (0, 0.01, 0.1, 1, 10, and 20 μmol/L) for 24 hours. ( A ) Immunoblotting showed that RAD001 induced autophagy indicators including upregulation of LC3-II/I and downregulation of p62 in a dose-dependent manner. ( B ) Quantification of the immunoblots. * P <0.05 versus 0 μmol/L group. n=3. ( C , D ) 786-O and A498 cell lines were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( C ) Immunoblotting showed that RAD001 induced autophagy in 786-O and A498 cells as time prolonged, which peaked at 8 hours. ( D ) Quantification of the immunoblots. * P <0.05 versus 0 hour group. n=3. Abbreviation: RCCs, renal cell carcinoma cells.

    Techniques Used: Western Blot

    Inhibition of autophagy enhances RAD001-induced cytotoxicity, RAD001-induced activation of ERK signaling pathway in RCCs. Notes: 786-O and A498 cells were pretreated with CQ (autophagy inhibitor) (10 mmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( A ) MTT assay showed that RAD001 impaired cell viability of 786-O and A498 cells in a dose-dependent manner. n=3. ( B ) Immunoblotting of LC3-II/I and p62 showed that CQ could restore the downregulation of p62, but would not impair the upregulation of LC3-II/I because CQ blocks autophagy at the lysosomal degradation step. ( C ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control. # P <0.05 versus RAD001 group. n=3. ( D ) MTT assay displayed that autophagy inhibition by CQ promoted RAD001-induced cytotoxicity in 786-O and A498 cells. * P <0.05 versus control. # P <0.05 versus RAD001 group. n=3. ( E ) The apoptosis indicator cleave-PARP detected by immunoblot indicated that cells apoptosis was increased in 786-O and A498 cells after CQ intervention, compared to the RAD001 group. ( F ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. 786-O and A498 cells were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( G ) Immunoblotting analyzed the JNK, p38, and ERK signaling molecules in 786-O and A498 cells after RAD001 treatment. ( H ) Quantification of the immunoblots. * P <0.05 versus 0 hour group. n=3. Abbreviations: CQ, chloroquine; Con, control; RCCs, renal cell carcinoma cells; ERK, extracellular signal-regulated kinase; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; PARP, poly ADP ribose polymerase; JNK, c-Jun N-terminal kinase.
    Figure Legend Snippet: Inhibition of autophagy enhances RAD001-induced cytotoxicity, RAD001-induced activation of ERK signaling pathway in RCCs. Notes: 786-O and A498 cells were pretreated with CQ (autophagy inhibitor) (10 mmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( A ) MTT assay showed that RAD001 impaired cell viability of 786-O and A498 cells in a dose-dependent manner. n=3. ( B ) Immunoblotting of LC3-II/I and p62 showed that CQ could restore the downregulation of p62, but would not impair the upregulation of LC3-II/I because CQ blocks autophagy at the lysosomal degradation step. ( C ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control. # P <0.05 versus RAD001 group. n=3. ( D ) MTT assay displayed that autophagy inhibition by CQ promoted RAD001-induced cytotoxicity in 786-O and A498 cells. * P <0.05 versus control. # P <0.05 versus RAD001 group. n=3. ( E ) The apoptosis indicator cleave-PARP detected by immunoblot indicated that cells apoptosis was increased in 786-O and A498 cells after CQ intervention, compared to the RAD001 group. ( F ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. 786-O and A498 cells were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( G ) Immunoblotting analyzed the JNK, p38, and ERK signaling molecules in 786-O and A498 cells after RAD001 treatment. ( H ) Quantification of the immunoblots. * P <0.05 versus 0 hour group. n=3. Abbreviations: CQ, chloroquine; Con, control; RCCs, renal cell carcinoma cells; ERK, extracellular signal-regulated kinase; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; PARP, poly ADP ribose polymerase; JNK, c-Jun N-terminal kinase.

    Techniques Used: Inhibition, Activation Assay, MTT Assay, Western Blot

    Selumetinib (AZD6244) significantly enhances RAD001-induced apoptosis of RCCs. Notes: 786-O and A498 cells were pretreated with AZD6244 (1 μmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( A ) Immunoblotting showed that AZD6244 significantly inhibited the activation of ERK pathway in 786-O and A498 cells. ( B ) Quantification of the immunoblots. ( C ) MTT assay detected the effect of AZD6244 on cell viability of 786-O and A498 cells, which suggested that AZD6244 effectively blunts RAD001-induced cell viability. ( D ) Immunoblotting demonstrates that AZD6244 could effectively restore upregulation of LC3-II/I and downregulation of p62 induced by RAD001 in 786-O and A498 cells. ( E ) Densitometric analysis was performed to quantify the immunoblots. ( F ) Immunoblot analysis indicated that combination treatment of RAD001 with AZD6244 could increase cleave-PARP level in 786-O and A498 cells, compared to the RAD001 group. ( G ) Densitometric analysis was performed to quantify the cleave-PARP immunoblots. ( H ) The difference of apoptosis determined by flow cytometry showed that AZD6244 significantly increased RAD001-induced cells apoptosis in 786-O and A498 cell lines. ( I ) Quantification of the apoptosis proportion. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. Abbreviations: RCCs, renal cell carcinoma cells; ERK, extracellular signal-regulated kinase; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; PARP, poly ADP ribose polymerase; FITC, fluorescein isothiocyanate; PI, propidium iodide; RAD001, everolimus; AZD6244, selumetinib; Con, control.
    Figure Legend Snippet: Selumetinib (AZD6244) significantly enhances RAD001-induced apoptosis of RCCs. Notes: 786-O and A498 cells were pretreated with AZD6244 (1 μmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( A ) Immunoblotting showed that AZD6244 significantly inhibited the activation of ERK pathway in 786-O and A498 cells. ( B ) Quantification of the immunoblots. ( C ) MTT assay detected the effect of AZD6244 on cell viability of 786-O and A498 cells, which suggested that AZD6244 effectively blunts RAD001-induced cell viability. ( D ) Immunoblotting demonstrates that AZD6244 could effectively restore upregulation of LC3-II/I and downregulation of p62 induced by RAD001 in 786-O and A498 cells. ( E ) Densitometric analysis was performed to quantify the immunoblots. ( F ) Immunoblot analysis indicated that combination treatment of RAD001 with AZD6244 could increase cleave-PARP level in 786-O and A498 cells, compared to the RAD001 group. ( G ) Densitometric analysis was performed to quantify the cleave-PARP immunoblots. ( H ) The difference of apoptosis determined by flow cytometry showed that AZD6244 significantly increased RAD001-induced cells apoptosis in 786-O and A498 cell lines. ( I ) Quantification of the apoptosis proportion. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. Abbreviations: RCCs, renal cell carcinoma cells; ERK, extracellular signal-regulated kinase; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; PARP, poly ADP ribose polymerase; FITC, fluorescein isothiocyanate; PI, propidium iodide; RAD001, everolimus; AZD6244, selumetinib; Con, control.

    Techniques Used: Western Blot, Activation Assay, MTT Assay, Flow Cytometry

    ERK mediated autophagy through upregulating Beclin-1 and p-Bcl-2 expression. Notes: ( A , B ) 786-O and A498 cells were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( A ) Immunoblotting showed that RAD001 induced upregulation of downstream signaling molecules of the ERK pathway including Beclin-1 and Bcl-2 in 786-O and A498 cells in a time-dependent manner. ( B ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus 0 hour group. n=3. ( C , D ) 786-O and A498 cells were pretreated with AZD6244 (1 μmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( C ) Immunoblotting showed that AZD6244 significantly decreased protein levels of Beclin-1 and Bcl-2 in 786-O and A498 cells. ( D ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. Abbreviations: ERK, extracellular signal-regulated kinase; RAD001, everolimus.
    Figure Legend Snippet: ERK mediated autophagy through upregulating Beclin-1 and p-Bcl-2 expression. Notes: ( A , B ) 786-O and A498 cells were treated by RAD001 for 0, 1, 2, 4, and 8 hours. ( A ) Immunoblotting showed that RAD001 induced upregulation of downstream signaling molecules of the ERK pathway including Beclin-1 and Bcl-2 in 786-O and A498 cells in a time-dependent manner. ( B ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus 0 hour group. n=3. ( C , D ) 786-O and A498 cells were pretreated with AZD6244 (1 μmol/L) for 30 minutes and then treated with RAD001 for 8 hours. ( C ) Immunoblotting showed that AZD6244 significantly decreased protein levels of Beclin-1 and Bcl-2 in 786-O and A498 cells. ( D ) Densitometric analysis was performed to quantify the immunoblots. * P <0.05 versus control group. # P <0.05 versus RAD001 group. n=3. Abbreviations: ERK, extracellular signal-regulated kinase; RAD001, everolimus.

    Techniques Used: Expressing, Western Blot

    a498  (ATCC)


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    ATCC a498
    A498, 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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    a498 cells  (ATCC)


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    ATCC a498 cells
    (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in <t>A498</t> cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.
    A498 Cells, 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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    1) Product Images from "Quantitative Proteomics Identifies the Myb-Binding Protein p160 as a Novel Target of the von Hippel-Lindau Tumor Suppressor"

    Article Title: Quantitative Proteomics Identifies the Myb-Binding Protein p160 as a Novel Target of the von Hippel-Lindau Tumor Suppressor

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0016975

    (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in A498 cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.
    Figure Legend Snippet: (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in A498 cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.

    Techniques Used: Expressing, Western Blot, Transfection, Infection, Plasmid Preparation, Immunoprecipitation, SDS Page, Produced, Purification, In Vitro, Incubation, In Vivo, Luciferase, shRNA

    a498  (ATCC)


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    ATCC a498
    A498, 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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    human rcc a498 cell  (ATCC)


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    ATCC human rcc a498 cell
    Cell viability and antiproliferative effect of acetylshikonin against <t>A498</t> and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).
    Human Rcc A498 Cell, 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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    1) Product Images from "Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation"

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2022/9139338

    Cell viability and antiproliferative effect of acetylshikonin against A498 and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).
    Figure Legend Snippet: Cell viability and antiproliferative effect of acetylshikonin against A498 and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Techniques Used: MTT Assay, Cell Counting, Quantitation Assay

    Cell cycle progression analysis and annexin V/PI double-staining analysis of A498 and ACHN cells treated with acetylshikonin. (a) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with propidium iodide (PI) for a flow cytometric analysis of DNA content. The distribution and percentage of cells in G0/1, S, and G2/M phases of the cell cycle were indicated. (b) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with annexin V and PI for apoptotic analysis. The percentages of apoptotic cells are indicated on the plots. The percentages of each portion were represented in bar graphs. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).
    Figure Legend Snippet: Cell cycle progression analysis and annexin V/PI double-staining analysis of A498 and ACHN cells treated with acetylshikonin. (a) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with propidium iodide (PI) for a flow cytometric analysis of DNA content. The distribution and percentage of cells in G0/1, S, and G2/M phases of the cell cycle were indicated. (b) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with annexin V and PI for apoptotic analysis. The percentages of apoptotic cells are indicated on the plots. The percentages of each portion were represented in bar graphs. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Techniques Used: Double Staining, Staining

    Analysis of protein expression level in A498 and ACHN cells treated with acetylshikonin by western blot analysis. (a) Cells were treated with different concentrations of acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 24 h, and western blot was performed to measure pro- or antiapoptotic protein expression level using specific antibodies. β -Actin was used for a gel loading control. (b) Nuclear localization of FOXO3 and p27 proteins from the cytoplasm in A498 and ACHN cells treated with acetylshikonin. Nuclear fractional western blotting results of A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M). The cytoplasmic and nucleic protein contents of FOXO3 and p27 were analyzed by western blotting using specific antibodies. GAPDH and Lamin A/C were used as loading control proteins for the cytoplasm and nucleus, respectively.
    Figure Legend Snippet: Analysis of protein expression level in A498 and ACHN cells treated with acetylshikonin by western blot analysis. (a) Cells were treated with different concentrations of acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 24 h, and western blot was performed to measure pro- or antiapoptotic protein expression level using specific antibodies. β -Actin was used for a gel loading control. (b) Nuclear localization of FOXO3 and p27 proteins from the cytoplasm in A498 and ACHN cells treated with acetylshikonin. Nuclear fractional western blotting results of A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M). The cytoplasmic and nucleic protein contents of FOXO3 and p27 were analyzed by western blotting using specific antibodies. GAPDH and Lamin A/C were used as loading control proteins for the cytoplasm and nucleus, respectively.

    Techniques Used: Expressing, Western Blot

    ROS generation in A498 and ACHN cells, treated with acetylshikonin. (a) Intracellular ROS generations in A498 and ACHN cells were measured by using DCFH-DA (10 μ M) and flow cytometry after 4 h of treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Mean fluorescence intensity (MFI) at each concentration is indicated on each plot. Bar graph represents the quantitation of the MFI. The vector control MFI was set at 100%. The data represent the mean ± SD of three independent experiments. (b) Cell viability of A498 and ACHN cells was analyzed by using MTT after 24 h of the treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0.05 and ∗∗ p < 0.01, respectively). Number sign indicates a significant difference of NAC-treated cells from acetylshikonin-treated cells ( # p < 0 : 05). (c) Protein expressions of apoptotic proteins and mitochondrial protein were evaluated in acetylshikonin-treated A498 and ACHN cells with or without NAC.
    Figure Legend Snippet: ROS generation in A498 and ACHN cells, treated with acetylshikonin. (a) Intracellular ROS generations in A498 and ACHN cells were measured by using DCFH-DA (10 μ M) and flow cytometry after 4 h of treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Mean fluorescence intensity (MFI) at each concentration is indicated on each plot. Bar graph represents the quantitation of the MFI. The vector control MFI was set at 100%. The data represent the mean ± SD of three independent experiments. (b) Cell viability of A498 and ACHN cells was analyzed by using MTT after 24 h of the treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0.05 and ∗∗ p < 0.01, respectively). Number sign indicates a significant difference of NAC-treated cells from acetylshikonin-treated cells ( # p < 0 : 05). (c) Protein expressions of apoptotic proteins and mitochondrial protein were evaluated in acetylshikonin-treated A498 and ACHN cells with or without NAC.

    Techniques Used: Flow Cytometry, Fluorescence, Concentration Assay, Quantitation Assay, Plasmid Preparation

    Cell viability and antiproliferative effect of acetylshikonin treatment combined with CYP2J2 siRNA transfection against RCC. The A498 and ACHN cells were transfected with control or CYP2J2 siRNA and additionally treated with 1 μ M acetylshikonin. (a) Graphical data from GEPIA displays the overall survival and disease-free survival (DFS) analysis of kidney renal papillary cell carcinoma (KIRP) patients with high (red) or low (blue) level of CYP2J2 expression. (b) Cytotoxic effect was analyzed at 24, 48, and 72 h after treatment. The proliferation rates were determined by using the MTT assay. (c) The cell numbers were analyzed by the cell counting assay after 0, 24, 48, and 72 h. (d) Colony forming assay of A498 and ACHN cells for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively). (e) Western blot analysis of control or CYP2J2 siRNA transfected A498 and ACHN cells followed by 1 μ M acetylshikonin treatment for 24 h. β -Actin is used for a gel loading control.
    Figure Legend Snippet: Cell viability and antiproliferative effect of acetylshikonin treatment combined with CYP2J2 siRNA transfection against RCC. The A498 and ACHN cells were transfected with control or CYP2J2 siRNA and additionally treated with 1 μ M acetylshikonin. (a) Graphical data from GEPIA displays the overall survival and disease-free survival (DFS) analysis of kidney renal papillary cell carcinoma (KIRP) patients with high (red) or low (blue) level of CYP2J2 expression. (b) Cytotoxic effect was analyzed at 24, 48, and 72 h after treatment. The proliferation rates were determined by using the MTT assay. (c) The cell numbers were analyzed by the cell counting assay after 0, 24, 48, and 72 h. (d) Colony forming assay of A498 and ACHN cells for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively). (e) Western blot analysis of control or CYP2J2 siRNA transfected A498 and ACHN cells followed by 1 μ M acetylshikonin treatment for 24 h. β -Actin is used for a gel loading control.

    Techniques Used: Transfection, Expressing, MTT Assay, Cell Counting, Quantitation Assay, Western Blot

    Schematic diagram of acetylshikonin-induced apoptosis pathway in RCC A498 and ACHN cells.
    Figure Legend Snippet: Schematic diagram of acetylshikonin-induced apoptosis pathway in RCC A498 and ACHN cells.

    Techniques Used:

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    99
    ATCC a498
    Effects of luteolin on <t>A498</t> and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
    A498, 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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    ATCC a498 htb 44
    Effects of luteolin on <t>A498</t> and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
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    ATCC a498 htb 44 cell lines
    Effects of luteolin on <t>A498</t> and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.
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    ATCC a498 cells
    (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in <t>A498</t> cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.
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    ATCC human rcc a498 cell
    Cell viability and antiproliferative effect of acetylshikonin against <t>A498</t> and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).
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    Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Induction of Apoptosis by Luteolin Involving Akt Inactivation in Human 786-O Renal Cell Carcinoma Cells

    doi: 10.1155/2013/109105

    Figure Lengend Snippet: Effects of luteolin on A498 and ACHN cells. A498 and ACHN cells were treated with various concentrations of luteolin for 24 h. Cell viability was determined by MTS reduction assay (a). Protein extracts were isolated and subjected to fluorogenic caspase-3 assay. The intensity of fluorescent signals was expressed as arbitrary unit (b). * P < 0.05 and ** P < 0.01 versus medium control, n = 4. Protein extracts were isolated and subjected to Western blot analysis with indicated antibodies. One of three independent experiments is shown (c). An additional band of HSP90 was indicated by arrow.

    Article Snippet: Human RCC cell lines, 786-O (ATCC CRL1932), A498 (ATCC HTB-44), and ACHN (ATCC CRL-1611) were cultured in Dulbecco's modified Eagle medium (DMEM) supplemented with 10% fetal bovine serum (FBS), 100 U/mL penicillin, and 100 μ g/mL streptomycin and were maintained in a humidified incubator with 5% CO 2 .

    Techniques: Isolation, Caspase-3 Assay, Western Blot

    (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in A498 cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.

    Journal: PLoS ONE

    Article Title: Quantitative Proteomics Identifies the Myb-Binding Protein p160 as a Novel Target of the von Hippel-Lindau Tumor Suppressor

    doi: 10.1371/journal.pone.0016975

    Figure Lengend Snippet: (A) Increased p160 protein expression upon iron chelation. Mouse Balb/c3T3 fibroblasts were treated with or without 100 µM desferrioxamine (DFO, iron chelator) for 24 hours and the p160 and tubulin expression was analyzed by immunoblotting using 30 µg whole cell lysate. (B) VHL degrades p160 by a proteasome-dependent mechanism. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 10 µM MG-132 for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (C) Degradation of p160 by VHL is abolished by iron chelation. 293T cells were transfected with FLAG-p160 with or without VHL. Where indicated, the transfected cells were treated with 100 µM desferrioxamine (DFO) for 12 hours. The expression of FLAG-p160 was examined by immunoblotting using 30 µg whole cell lysate. (D) Degradation of endogenous p160 by VHL in 786-O cells. VHL-null 786-O renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (E) Degradation of endogenous p160 by VHL in A498 cells. VHL-null A498 renal carcinoma cells were infected with VHL or empty adenovirus vector and 48 hours after infection, the expression of p160, HIF-2α, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (F) Effect of VHL knockdown on p160 expression. Balb/c3T3 cells were transfected with control or VHL siRNA and 72 hours after transfection, the expression of p160, VHL, and tubulin was analyzed by immunoblotting using 30 µg whole cell lysate. (G) VHL directly binds p160. FLAG-p160 was immunoprecipitated from transfected 293T cells (FLAG empty vector as control), fractionated by SDS-PAGE, and transferred to nitrocellulose membrane. Triplicate protein blots were probed with anti-p160 antibody (left), bacterially-produced purified GST-VHL (middle), or GST (right). (H) In vitro ubiquitination of p160 by VHL. In vitro translated p160 was incubated at 30°C with the extract of VHL-null 786-O cells and ATP-regenerating system in the presence or absence of GST-VHL and ubiquitin as indicated. Aliquots were removed at indicated times and were analyzed for protein ubiquitination. 0 minute samples were removed after assembling the reaction mixture at room temperature without incubation at 30°C. Ubiquitinated p160 is indicated by asterisks. (I) Effect of VHL knockdown on p160 ubiquitination in vivo. Left: 293T cells were transfected with FLAG-VHL and luciferase shRNA or VHL shRNA expression vector and 48 hours after transfection, the expression of FLAG-VHL was analyzed by anti-FLAG immunoblotting. Right: 293T cells were transfected with FLAG-p160, HA-ubiquitin, luciferase shRNA, or VHL shRNA where indicated, and FLAG-p160 was immunoprecipitated by anti-FLAG antibody and was analyzed by anti-HA or anti-FLAG immunoblotting.

    Article Snippet: Balb/c3T3, 293T, 786-O, and A498 cells were obtained from ATCC.

    Techniques: Expressing, Western Blot, Transfection, Infection, Plasmid Preparation, Immunoprecipitation, SDS Page, Produced, Purification, In Vitro, Incubation, In Vivo, Luciferase, shRNA

    Cell viability and antiproliferative effect of acetylshikonin against A498 and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: Cell viability and antiproliferative effect of acetylshikonin against A498 and ACHN cells. (a) Dose- and time-dependent cytotoxic effect of acetylshikonin (0, 1.25, 2.5, 5, 10, and 20 μ M) against A498 and ACHN cells after 24, 48, and 72 h treatment. The proliferation rates were determined by the MTT assay. (b) The cell numbers were analyzed by the cell counting assay after A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 0, 24, 48, and 72 h. (c) Colony forming assay of A498 and ACHN cells treated with acetylshikonin (0 and 1.25 μ M) for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: MTT Assay, Cell Counting, Quantitation Assay

    Cell cycle progression analysis and annexin V/PI double-staining analysis of A498 and ACHN cells treated with acetylshikonin. (a) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with propidium iodide (PI) for a flow cytometric analysis of DNA content. The distribution and percentage of cells in G0/1, S, and G2/M phases of the cell cycle were indicated. (b) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with annexin V and PI for apoptotic analysis. The percentages of apoptotic cells are indicated on the plots. The percentages of each portion were represented in bar graphs. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: Cell cycle progression analysis and annexin V/PI double-staining analysis of A498 and ACHN cells treated with acetylshikonin. (a) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with propidium iodide (PI) for a flow cytometric analysis of DNA content. The distribution and percentage of cells in G0/1, S, and G2/M phases of the cell cycle were indicated. (b) The cells were treated with 0, 1.25, 2.5, and 5 μ M of acetylshikonin for 24 and 48 h and stained with annexin V and PI for apoptotic analysis. The percentages of apoptotic cells are indicated on the plots. The percentages of each portion were represented in bar graphs. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively).

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: Double Staining, Staining

    Analysis of protein expression level in A498 and ACHN cells treated with acetylshikonin by western blot analysis. (a) Cells were treated with different concentrations of acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 24 h, and western blot was performed to measure pro- or antiapoptotic protein expression level using specific antibodies. β -Actin was used for a gel loading control. (b) Nuclear localization of FOXO3 and p27 proteins from the cytoplasm in A498 and ACHN cells treated with acetylshikonin. Nuclear fractional western blotting results of A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M). The cytoplasmic and nucleic protein contents of FOXO3 and p27 were analyzed by western blotting using specific antibodies. GAPDH and Lamin A/C were used as loading control proteins for the cytoplasm and nucleus, respectively.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: Analysis of protein expression level in A498 and ACHN cells treated with acetylshikonin by western blot analysis. (a) Cells were treated with different concentrations of acetylshikonin (0, 1.25, 2.5, and 5 μ M) for 24 h, and western blot was performed to measure pro- or antiapoptotic protein expression level using specific antibodies. β -Actin was used for a gel loading control. (b) Nuclear localization of FOXO3 and p27 proteins from the cytoplasm in A498 and ACHN cells treated with acetylshikonin. Nuclear fractional western blotting results of A498 and ACHN cells treated with acetylshikonin (0, 1.25, 2.5, and 5 μ M). The cytoplasmic and nucleic protein contents of FOXO3 and p27 were analyzed by western blotting using specific antibodies. GAPDH and Lamin A/C were used as loading control proteins for the cytoplasm and nucleus, respectively.

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: Expressing, Western Blot

    ROS generation in A498 and ACHN cells, treated with acetylshikonin. (a) Intracellular ROS generations in A498 and ACHN cells were measured by using DCFH-DA (10 μ M) and flow cytometry after 4 h of treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Mean fluorescence intensity (MFI) at each concentration is indicated on each plot. Bar graph represents the quantitation of the MFI. The vector control MFI was set at 100%. The data represent the mean ± SD of three independent experiments. (b) Cell viability of A498 and ACHN cells was analyzed by using MTT after 24 h of the treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0.05 and ∗∗ p < 0.01, respectively). Number sign indicates a significant difference of NAC-treated cells from acetylshikonin-treated cells ( # p < 0 : 05). (c) Protein expressions of apoptotic proteins and mitochondrial protein were evaluated in acetylshikonin-treated A498 and ACHN cells with or without NAC.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: ROS generation in A498 and ACHN cells, treated with acetylshikonin. (a) Intracellular ROS generations in A498 and ACHN cells were measured by using DCFH-DA (10 μ M) and flow cytometry after 4 h of treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Mean fluorescence intensity (MFI) at each concentration is indicated on each plot. Bar graph represents the quantitation of the MFI. The vector control MFI was set at 100%. The data represent the mean ± SD of three independent experiments. (b) Cell viability of A498 and ACHN cells was analyzed by using MTT after 24 h of the treatment with acetylshikonin (0, 1.25, 2.5, and 5 μ M) with or without NAC. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0.05 and ∗∗ p < 0.01, respectively). Number sign indicates a significant difference of NAC-treated cells from acetylshikonin-treated cells ( # p < 0 : 05). (c) Protein expressions of apoptotic proteins and mitochondrial protein were evaluated in acetylshikonin-treated A498 and ACHN cells with or without NAC.

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: Flow Cytometry, Fluorescence, Concentration Assay, Quantitation Assay, Plasmid Preparation

    Cell viability and antiproliferative effect of acetylshikonin treatment combined with CYP2J2 siRNA transfection against RCC. The A498 and ACHN cells were transfected with control or CYP2J2 siRNA and additionally treated with 1 μ M acetylshikonin. (a) Graphical data from GEPIA displays the overall survival and disease-free survival (DFS) analysis of kidney renal papillary cell carcinoma (KIRP) patients with high (red) or low (blue) level of CYP2J2 expression. (b) Cytotoxic effect was analyzed at 24, 48, and 72 h after treatment. The proliferation rates were determined by using the MTT assay. (c) The cell numbers were analyzed by the cell counting assay after 0, 24, 48, and 72 h. (d) Colony forming assay of A498 and ACHN cells for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively). (e) Western blot analysis of control or CYP2J2 siRNA transfected A498 and ACHN cells followed by 1 μ M acetylshikonin treatment for 24 h. β -Actin is used for a gel loading control.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: Cell viability and antiproliferative effect of acetylshikonin treatment combined with CYP2J2 siRNA transfection against RCC. The A498 and ACHN cells were transfected with control or CYP2J2 siRNA and additionally treated with 1 μ M acetylshikonin. (a) Graphical data from GEPIA displays the overall survival and disease-free survival (DFS) analysis of kidney renal papillary cell carcinoma (KIRP) patients with high (red) or low (blue) level of CYP2J2 expression. (b) Cytotoxic effect was analyzed at 24, 48, and 72 h after treatment. The proliferation rates were determined by using the MTT assay. (c) The cell numbers were analyzed by the cell counting assay after 0, 24, 48, and 72 h. (d) Colony forming assay of A498 and ACHN cells for 14 days. The bar graphs represent a quantitation of the colonies. Data are represented with the mean ± SD of triplicated results. Single and double asterisks indicate significant differences from the control cells ( ∗ p < 0 : 05 and ∗∗ p < 0 : 01, respectively). (e) Western blot analysis of control or CYP2J2 siRNA transfected A498 and ACHN cells followed by 1 μ M acetylshikonin treatment for 24 h. β -Actin is used for a gel loading control.

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: Transfection, Expressing, MTT Assay, Cell Counting, Quantitation Assay, Western Blot

    Schematic diagram of acetylshikonin-induced apoptosis pathway in RCC A498 and ACHN cells.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Acetylshikonin, A Novel CYP2J2 Inhibitor, Induces Apoptosis in RCC Cells via FOXO3 Activation and ROS Elevation

    doi: 10.1155/2022/9139338

    Figure Lengend Snippet: Schematic diagram of acetylshikonin-induced apoptosis pathway in RCC A498 and ACHN cells.

    Article Snippet: Human RCC A498 cell (from ATCC, Manassas, VA, USA) was maintained in RPMI 1640 media, and ACHN cell (from ATCC, Manassas, VA, USA) was maintained in DMEM high glucose, both supplemented with 10% fetal bovine serum (FBS) and 1% antibiotics (streptomycin/penicillin) at standard conditions (37°C in a humidified incubator containing 5% CO 2 in air).

    Techniques: