bcl-2 Search Results


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  • 93
    Thermo Fisher bcl 2 hs00236329
    Bcl 2 Hs00236329, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bcl2  (Abcam)
    93
    Abcam bcl2
    Protein levels of DNMT3b, <t>BCL2,</t> and VEGFA in PFC of depressed suicide (n = 18) and normal control (n = 17) subjects. Protein samples from tissue lysates were subjected to 10% polyacrylamide gel electrophoresis and transferred to enhanced chemiluminescence–nitrocellulose membranes, which were then incubated with primary antibody specific for DNMT3b, BCL2, VEGFA or β-actin and corresponding secondary antibody. The suicide group was compared with the control group. DMNT3b was strongly up-regulated (2.4-fold) in the depressed suicide group ( a p = 1×10 −11 ), VEGFA showed no significant change (1.03-fold, b p = 0.4) and BCL2 was strongly down-regulated (0.57 of control, c p = 2.4×10 −14 ). C = Controls; DS = Depressed suicide.
    Bcl2, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 1461 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cell Signaling Technology Inc bcl2
    Augmentation of apoptosis by peptide-NT. Sensitive MIP101 or RKO and 5-FU resistant MIP/5FU and RKO/5FU cells were incubated with peptide-NT 100 ng/ml +/− 5-FU 5 µM for 24 hrs and assayed for ( A ) caspase 3/7 levels, or ( B ) cell viability by MTT assays. ( C ) Immunoblots showing the ability of peptide-NT to interfere with the interaction between caspase 8 and <t>Bcl2:</t> MIP/5FU cells were incubated with peptide-NT or scramble control peptides 1 or 2 for 24 hrs; cell pellets were collected 24 hrs later for co-immunoprecipitation studies.
    Bcl2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 2195 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bcl2/product/Cell Signaling Technology Inc
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    99
    Abcam anti bcl 2
    Downregulation of <t>Bcl-2</t> and Cyclin-D1 enhance apoptosis of osteoblast. A. Cell apoptosis of osteoblast in each group. B. Of cell apoptosis rate in each group. All data were expressed as means ± SD. Significance is noted at these thresholds: *P
    Anti Bcl 2, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1764 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam antibodies against bcl 2
    Lidocaine induced inhibition of growth and metastasis of MKN45 cells were attenuated by miR-145 silence. a miR-145 expression was decreased after transfection with miR-145 inhibitor. miR-145 knockdown ( b ) increased cell proliferation, ( c ) up-regulated Cyclin D1 expression and down-regulated p21 expression, ( d ) inhibited apoptosis, ( e ) increased <t>Bcl-2</t> expression, decreased cleaved-Caspase-3, -7, and -9 expression. miR-145 knockdown ( f ) increased migration, ( g ) up-regulated MMP-2 and MMP-9 expression, ( h ) increased invasion, and ( i ) up-regulated Vimentin. * p
    Antibodies Against Bcl 2, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 200 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam bcl 2 primary antibodies
    The RNA or protein expression changes of lung cancer cells with lnc-BMPl-1 over-expression vs. NC cells, the CSE vs. DMSO treated 16HBE cells, and 5-AzaC or TSA treatment. ( A ) The protein expression of <t>Bcl-2,</t> Cav-1 and DNMT3a in different lung cancer cell lines with lnc-BMP1-1 over-expression vs. NC cells; the protein expression were detected using western blotting analyses, protein expression was normalized against GAPDH or α-tubulin protein; the value above each band indicates the fold change of protein expression relative to their control; ( B ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 5 th passage; ( C ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 10 th passage; ( D ) The expression of lnc-BMP1-1 , Cav-1 were reduced in CSE treated 16HBE cells both in 5 th and 10 th passage, and made greater decline in 10 th than in 5 th passage (the same gene was compared in 5 th and 10 th generation of CSE treated 16HBE cells, #P
    Bcl 2 Primary Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Cell Signaling Technology Inc anti bcl2
    Apoptosis related pathway is involved in DEAB-induced anti-cancer effect. (A) Expressions of Bax and <t>Bcl2</t> in BxPC3, MiaPaCa2 and Panc1 cells treated or untreated with DEAB were detected by western blotting. β-actin was used as a control. Data are representative of four independent experiments. * P
    Anti Bcl2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 879 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc bcl2 antibody
    The transmembrane domain of <t>Bcl2</t> is critical for its interaction with SHP. (A) Diagram showing the domain structure of Bcl2 protein. (B) Top, GST pull-down assay to determine the interaction domain of Bcl2 with SHP and the effect of AHPN on the in vitro interaction of Bcl2 with SHP. Bcl2wt, ΔTM, ΔBH1, ΔBH2, and ΔBH3 proteins were detected using an antibody against the N-terminus of Bcl2. ΔBH4 and Δloop plasmids contain a myc epitope, and these proteins were detected using an anti-Myc antibody. Bottom, Bcl2 band intensities were measured by densitometry, and the values were normalized by dividing by the GST-SHP Int intensities. The values for intensities relative to Bcl2 wt (set as 1) were plotted. Data are represented as mean ± SEM (*, P
    Bcl2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    ABclonal bcl 2
    SOS1 silencing reversed USP22-induced changes in gastric cancer cell behavior and RAS signaling. USP22-overexpressing SGC7901 cells were transfected with shSOS1. a Cell proliferation, apoptosis, migration, and invasion were evaluated. b , c Western blot analysis was performed to measure protein levels of USP22, SOS1, Ras, ERK, p-ERK, c-myc, PI3K, AKT, p-AKT, BAD, and <t>bcl-2</t> in SGC7901 cells and tumor tissue. GAPDH was used as an internal control. * P
    Bcl 2, supplied by ABclonal, used in various techniques. Bioz Stars score: 91/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Novus Biologicals anti bcl2
    ABT-737 induces autophagy and dissociation of the <t>BECN1-BCL2</t> complex after prolonged, but not shorter duration treatment, in wild-type or in Bax and Bak1 KO MEFs. ( A ) Western blot detection of BAX and BAK1 in wild-type (WT) MEFS and in MEFS lacking either BAX ( Bax −/− ), BAK1 ( Bak1 −/− ), or both BAX and BAK1 (DKO). ( B ) Cell death (as measured by flow cytometric staining of propidium iodide ( PI ) uptake) of WT or Bax Bak1 DKO MEFs following treatment with the indicated dose of staurosporine (STS) treatment for the indicated duration. Results represent mean ± s.d. of triplicate samples. ( C ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell types treated with rapamycin (1 μM, 4 h) in the presence or absence of 50 nM Baf A1. GAPDH was used as a loading control. ( D ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with rapamycin (1 μM, 4 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( E ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( D ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( F ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell type treated with the indicated dose of ABT-737 for 12 h. GAPDH was used as a loading control. ( G ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with ABT-737 (10 μM, 12 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( H ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( G ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( I ) Immunoprecipitation of endogenous BECN1 with endogenous BCL2 in WT or Bax Bak1 DKO MEF cells following the indicated treatment. Cells were subjected to starvation (HBSS, 4 h), or ABT-737 for 12 h or 48 h. Western blot detection of LC3B-I to LC3B-II conversion and levels of SQSTM1 were performed to assess autophagy in the same samples used for immunoprecipitation of BECN1-BCL2 complexes. ACTB is shown as a loading control. For ( B ), ( E ) and ( H ), NS = not significant, and *** = P
    Anti Bcl2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 88/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti bcl2 antibody
    Propofol effect on apoptosis-associated proteins in TG-treated ARPE-19 cells. (A) Representative western blot for <t>Bcl2.</t> (B) Propofol attenuated the Bcl2 downregulation induced by TG in ARPE-19 cells. ARPE-19 cells were precubated with propofol for 12 h at different concentration, the treated with 1 μM TG for 12 h. The data are presented as the mean ± SEM from three independent experiments. Statistical analysis was performed by one-way analysis of variance with all pairwise multiple comparison procedures done by Tukey test. # p
    Anti Bcl2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Boster Bio anti bcl2 antibody
    Propofol effect on apoptosis-associated proteins in TG-treated ARPE-19 cells. (A) Representative western blot for <t>Bcl2.</t> (B) Propofol attenuated the Bcl2 downregulation induced by TG in ARPE-19 cells. ARPE-19 cells were precubated with propofol for 12 h at different concentration, the treated with 1 μM TG for 12 h. The data are presented as the mean ± SEM from three independent experiments. Statistical analysis was performed by one-way analysis of variance with all pairwise multiple comparison procedures done by Tukey test. # p
    Anti Bcl2 Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Protein levels of DNMT3b, BCL2, and VEGFA in PFC of depressed suicide (n = 18) and normal control (n = 17) subjects. Protein samples from tissue lysates were subjected to 10% polyacrylamide gel electrophoresis and transferred to enhanced chemiluminescence–nitrocellulose membranes, which were then incubated with primary antibody specific for DNMT3b, BCL2, VEGFA or β-actin and corresponding secondary antibody. The suicide group was compared with the control group. DMNT3b was strongly up-regulated (2.4-fold) in the depressed suicide group ( a p = 1×10 −11 ), VEGFA showed no significant change (1.03-fold, b p = 0.4) and BCL2 was strongly down-regulated (0.57 of control, c p = 2.4×10 −14 ). C = Controls; DS = Depressed suicide.

    Journal: PLoS ONE

    Article Title: MicroRNA Expression Is Down-Regulated and Reorganized in Prefrontal Cortex of Depressed Suicide Subjects

    doi: 10.1371/journal.pone.0033201

    Figure Lengend Snippet: Protein levels of DNMT3b, BCL2, and VEGFA in PFC of depressed suicide (n = 18) and normal control (n = 17) subjects. Protein samples from tissue lysates were subjected to 10% polyacrylamide gel electrophoresis and transferred to enhanced chemiluminescence–nitrocellulose membranes, which were then incubated with primary antibody specific for DNMT3b, BCL2, VEGFA or β-actin and corresponding secondary antibody. The suicide group was compared with the control group. DMNT3b was strongly up-regulated (2.4-fold) in the depressed suicide group ( a p = 1×10 −11 ), VEGFA showed no significant change (1.03-fold, b p = 0.4) and BCL2 was strongly down-regulated (0.57 of control, c p = 2.4×10 −14 ). C = Controls; DS = Depressed suicide.

    Article Snippet: Ratios of optical densities of DNMT3b, BCL2, or VEGFA to β-actin were calculated.

    Techniques: Polyacrylamide Gel Electrophoresis, Incubation

    Effects of TAT-survivin on Bcl-2 expression in H9c2 cardiac myocytes. H9c2 cardiac myocytes were treated with 1 µM of TAT-survivin for 1 hour and then subjected to doxorubicin treatment for 24 hours. A: whole cell lysates were immunoblotted with anti-Bax or anti-Bcl-2 antibody. B: total RNA was purified from cells and subjected to RT-PCR using primers specific for Bcl-2. C: mitochondrial and cytoplasm fractions were prepared, and equal amounts of protein were separated by SDS-PAGE gel. The release of Smac and cytochrome C from mitochondria was detected using an anti-Smac and anti-cytochrome C antibody. D: equal amounts of nuclear protein were separated by SDS-PAGE gel, and immunoblot analysis was performed using anti-phospho-CREB or anti-CREB antibody. E: whole cell lysates were immunoblotted with anti-phospho-p38 or anti-p38 antibody. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis, RNA: ribonucleic acid, CREB: cyclic adenosine monophosphate response elements-binding protein.

    Journal: Korean Circulation Journal

    Article Title: Protective Effect of Survivin in Doxorubicin-Induced Cell Death in H9c2 Cardiac Myocytes

    doi: 10.4070/kcj.2013.43.6.400

    Figure Lengend Snippet: Effects of TAT-survivin on Bcl-2 expression in H9c2 cardiac myocytes. H9c2 cardiac myocytes were treated with 1 µM of TAT-survivin for 1 hour and then subjected to doxorubicin treatment for 24 hours. A: whole cell lysates were immunoblotted with anti-Bax or anti-Bcl-2 antibody. B: total RNA was purified from cells and subjected to RT-PCR using primers specific for Bcl-2. C: mitochondrial and cytoplasm fractions were prepared, and equal amounts of protein were separated by SDS-PAGE gel. The release of Smac and cytochrome C from mitochondria was detected using an anti-Smac and anti-cytochrome C antibody. D: equal amounts of nuclear protein were separated by SDS-PAGE gel, and immunoblot analysis was performed using anti-phospho-CREB or anti-CREB antibody. E: whole cell lysates were immunoblotted with anti-phospho-p38 or anti-p38 antibody. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis, RNA: ribonucleic acid, CREB: cyclic adenosine monophosphate response elements-binding protein.

    Article Snippet: A previous study has also reported that activation of p38 MAP kinase in apoptotic cells correlates with reduced expression of Bcl-2 and survivin.

    Techniques: Expressing, Purification, Reverse Transcription Polymerase Chain Reaction, SDS Page, Polyacrylamide Gel Electrophoresis, Binding Assay

    Augmentation of apoptosis by peptide-NT. Sensitive MIP101 or RKO and 5-FU resistant MIP/5FU and RKO/5FU cells were incubated with peptide-NT 100 ng/ml +/− 5-FU 5 µM for 24 hrs and assayed for ( A ) caspase 3/7 levels, or ( B ) cell viability by MTT assays. ( C ) Immunoblots showing the ability of peptide-NT to interfere with the interaction between caspase 8 and Bcl2: MIP/5FU cells were incubated with peptide-NT or scramble control peptides 1 or 2 for 24 hrs; cell pellets were collected 24 hrs later for co-immunoprecipitation studies.

    Journal: PLoS ONE

    Article Title: A Peptide of SPARC Interferes with the Interaction between Caspase8 and Bcl2 to Resensitize Chemoresistant Tumors and Enhance Their Regression In Vivo

    doi: 10.1371/journal.pone.0026390

    Figure Lengend Snippet: Augmentation of apoptosis by peptide-NT. Sensitive MIP101 or RKO and 5-FU resistant MIP/5FU and RKO/5FU cells were incubated with peptide-NT 100 ng/ml +/− 5-FU 5 µM for 24 hrs and assayed for ( A ) caspase 3/7 levels, or ( B ) cell viability by MTT assays. ( C ) Immunoblots showing the ability of peptide-NT to interfere with the interaction between caspase 8 and Bcl2: MIP/5FU cells were incubated with peptide-NT or scramble control peptides 1 or 2 for 24 hrs; cell pellets were collected 24 hrs later for co-immunoprecipitation studies.

    Article Snippet: Tumor xenografts of MIP/ZEO, MIP/SP, MIP/SP-N, MIP/SP-F, and MIP/SP-C subcutaneously implanted cells were paraffin-embedded and processed and stained with Hematoxylin and Eosin (H & E), and cleaved caspase 3. (TIF) Click here for additional data file. siRNA optimization for Bid and Bcl2; and interaction between Bcl2 and caspase 8 in various resistant cells.

    Techniques: Incubation, MTT Assay, Western Blot, Immunoprecipitation

    A model: SPARC-mediated apoptosis. A schematic of SPARC and Bcl2 interacting with caspase 8 to influence apoptosis. In this study, we demonstrate that in an environment low in SPARC, Bcl2 interacts with caspase 8 to inhibit apoptosis. However, in the presence of SPARC or its N-terminus, these proteins interact with caspase 8 to inhibit its interaction with Bcl2, leading to an augmentation of the apoptotic cascade.

    Journal: PLoS ONE

    Article Title: A Peptide of SPARC Interferes with the Interaction between Caspase8 and Bcl2 to Resensitize Chemoresistant Tumors and Enhance Their Regression In Vivo

    doi: 10.1371/journal.pone.0026390

    Figure Lengend Snippet: A model: SPARC-mediated apoptosis. A schematic of SPARC and Bcl2 interacting with caspase 8 to influence apoptosis. In this study, we demonstrate that in an environment low in SPARC, Bcl2 interacts with caspase 8 to inhibit apoptosis. However, in the presence of SPARC or its N-terminus, these proteins interact with caspase 8 to inhibit its interaction with Bcl2, leading to an augmentation of the apoptotic cascade.

    Article Snippet: Tumor xenografts of MIP/ZEO, MIP/SP, MIP/SP-N, MIP/SP-F, and MIP/SP-C subcutaneously implanted cells were paraffin-embedded and processed and stained with Hematoxylin and Eosin (H & E), and cleaved caspase 3. (TIF) Click here for additional data file. siRNA optimization for Bid and Bcl2; and interaction between Bcl2 and caspase 8 in various resistant cells.

    Techniques:

    SPARC and Bcl2 both interact with caspase 8 with opposing effects. ( A ) In resistant MIP/5FU cells, caspase 8 interacts with Bcl2 and this is also observed in other resistant colorectal (RKO/5FU, RKO/CPT, RKO/CIS), pancreatic (MiaPaca/CPT) and breast cancer (MCF/CIS) cell lines ( B ). The Bcl2-caspase 8 interaction can be eliminated following exposure to rSPARC (100 ng/mL) (denoted as “*”). C ) The interaction between Bcl2-caspase 8 occurs at the N-terminus of caspase 8 as cells incubated with antibodies blocking the N-terminus of caspase 8 (N-term, 1.5–3 µg) prevented this Bcl2-caspase 8 interaction. D ) Bcl2-caspase 8 interaction is abolished after exposure to 100 ng/mL rSPARC in resistant MIP/5FU and MiaPaca/CPT cells. ( E ) Chemoresistant MIP/5FU cells transfected with Bcl2 siRNA to reduce Bcl2 expression are now responsive to 1000 µM 5-FU (+), especially in combination with incremental concentrations of rSPARC (20–100 ng/ml). Results represent mean ± s.e. (n = 3 independent studies). Student's t-test, statistically significant when p

    Journal: PLoS ONE

    Article Title: A Peptide of SPARC Interferes with the Interaction between Caspase8 and Bcl2 to Resensitize Chemoresistant Tumors and Enhance Their Regression In Vivo

    doi: 10.1371/journal.pone.0026390

    Figure Lengend Snippet: SPARC and Bcl2 both interact with caspase 8 with opposing effects. ( A ) In resistant MIP/5FU cells, caspase 8 interacts with Bcl2 and this is also observed in other resistant colorectal (RKO/5FU, RKO/CPT, RKO/CIS), pancreatic (MiaPaca/CPT) and breast cancer (MCF/CIS) cell lines ( B ). The Bcl2-caspase 8 interaction can be eliminated following exposure to rSPARC (100 ng/mL) (denoted as “*”). C ) The interaction between Bcl2-caspase 8 occurs at the N-terminus of caspase 8 as cells incubated with antibodies blocking the N-terminus of caspase 8 (N-term, 1.5–3 µg) prevented this Bcl2-caspase 8 interaction. D ) Bcl2-caspase 8 interaction is abolished after exposure to 100 ng/mL rSPARC in resistant MIP/5FU and MiaPaca/CPT cells. ( E ) Chemoresistant MIP/5FU cells transfected with Bcl2 siRNA to reduce Bcl2 expression are now responsive to 1000 µM 5-FU (+), especially in combination with incremental concentrations of rSPARC (20–100 ng/ml). Results represent mean ± s.e. (n = 3 independent studies). Student's t-test, statistically significant when p

    Article Snippet: Tumor xenografts of MIP/ZEO, MIP/SP, MIP/SP-N, MIP/SP-F, and MIP/SP-C subcutaneously implanted cells were paraffin-embedded and processed and stained with Hematoxylin and Eosin (H & E), and cleaved caspase 3. (TIF) Click here for additional data file. siRNA optimization for Bid and Bcl2; and interaction between Bcl2 and caspase 8 in various resistant cells.

    Techniques: Cycling Probe Technology, Incubation, Blocking Assay, Transfection, Expressing

    The DEDI-domain of caspase 8 is critical for its interaction with Bcl2. Vectors containing mutations in specific domains (DEDI, putative binding(PB), DEDII) of caspase 8 were transiently transfected into ( A ) MIP/5FU, MiaPaca/CPT or ( B ) MIP/SP cells, to determine the ability of the mutant proteins to co-IP with Bcl2 or SPARC. C ) Basal levels of caspase 8 gene expression between various cancer cell lines. D–F ) The effect of SPARC on cell viability ( D, E ) or apoptosis ( F ) in cells overexpressing mutant forms of caspase 8 was assessed. Cells were transiently transfected with wild-type caspase 8 (Csp8), mutants (DEDIm, PBm, and DEDIIm), or empty-vector (EV, control) for 48 h, followed by exposure to 100 ng/mL rSPARC for 48 h, and treated with 0 (▪) or 500 µM (□)5-FU for an additional 24 h. D–E ) In resistant cells, exposure to rSPARC and 5-FU resulted in decreased cell viability following transfection with EV-control: MIP/5FU: 90.14±2.80 (SPARC) vs. 69.89±4.64% (SPARC+5-FU) (p

    Journal: PLoS ONE

    Article Title: A Peptide of SPARC Interferes with the Interaction between Caspase8 and Bcl2 to Resensitize Chemoresistant Tumors and Enhance Their Regression In Vivo

    doi: 10.1371/journal.pone.0026390

    Figure Lengend Snippet: The DEDI-domain of caspase 8 is critical for its interaction with Bcl2. Vectors containing mutations in specific domains (DEDI, putative binding(PB), DEDII) of caspase 8 were transiently transfected into ( A ) MIP/5FU, MiaPaca/CPT or ( B ) MIP/SP cells, to determine the ability of the mutant proteins to co-IP with Bcl2 or SPARC. C ) Basal levels of caspase 8 gene expression between various cancer cell lines. D–F ) The effect of SPARC on cell viability ( D, E ) or apoptosis ( F ) in cells overexpressing mutant forms of caspase 8 was assessed. Cells were transiently transfected with wild-type caspase 8 (Csp8), mutants (DEDIm, PBm, and DEDIIm), or empty-vector (EV, control) for 48 h, followed by exposure to 100 ng/mL rSPARC for 48 h, and treated with 0 (▪) or 500 µM (□)5-FU for an additional 24 h. D–E ) In resistant cells, exposure to rSPARC and 5-FU resulted in decreased cell viability following transfection with EV-control: MIP/5FU: 90.14±2.80 (SPARC) vs. 69.89±4.64% (SPARC+5-FU) (p

    Article Snippet: Tumor xenografts of MIP/ZEO, MIP/SP, MIP/SP-N, MIP/SP-F, and MIP/SP-C subcutaneously implanted cells were paraffin-embedded and processed and stained with Hematoxylin and Eosin (H & E), and cleaved caspase 3. (TIF) Click here for additional data file. siRNA optimization for Bid and Bcl2; and interaction between Bcl2 and caspase 8 in various resistant cells.

    Techniques: Binding Assay, Transfection, Cycling Probe Technology, Mutagenesis, Co-Immunoprecipitation Assay, Expressing, Plasmid Preparation

    Treatment with SS-31 alleviated the neural apoptosis. (a, b) The TUNEL assay was employed to analyze the apoptotic index 1 day after TBI. SS-31 treatment significantly reduced the percentage of apoptotic neurons. n = 6 per group. (c) Western blot showed the pro- and antiapoptotic proteins in the contusion cortex. (d–f) Expression of the P53, Bcl-2, and cleaved caspase 3 protein levels were normalized to the level of β -actin. P53 and cleaved caspase 3 were significantly decreased while the Bcl-2 protein level was increased in the TBI + SS-31 group compared with the vehicle group. n = 6 per group. Scale bar 50 μ m. Data are presented as mean ± SEM; ∗∗∗ P

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: SS-31 Provides Neuroprotection by Reversing Mitochondrial Dysfunction after Traumatic Brain Injury

    doi: 10.1155/2018/4783602

    Figure Lengend Snippet: Treatment with SS-31 alleviated the neural apoptosis. (a, b) The TUNEL assay was employed to analyze the apoptotic index 1 day after TBI. SS-31 treatment significantly reduced the percentage of apoptotic neurons. n = 6 per group. (c) Western blot showed the pro- and antiapoptotic proteins in the contusion cortex. (d–f) Expression of the P53, Bcl-2, and cleaved caspase 3 protein levels were normalized to the level of β -actin. P53 and cleaved caspase 3 were significantly decreased while the Bcl-2 protein level was increased in the TBI + SS-31 group compared with the vehicle group. n = 6 per group. Scale bar 50 μ m. Data are presented as mean ± SEM; ∗∗∗ P

    Article Snippet: The dilution ratio of used antibodies was listed as follows: eIF2α (1 : 1000, CST), p-eIF2α (1 : 1000, CST), Bcl-2 (1 : 1000, CST), Bax (1 : 1000, CST), cytochrome c (1 : 1000, CST), P53 (1 : 500, Proteintech), PGC-1α (1 : 2000, Proteintech), SIRT1 (1 : 1000, CST), H3 (1 : 1000, CST), and β -actin (1 : 5000, Bioworld).

    Techniques: TUNEL Assay, Western Blot, Expressing

    Downregulation of Bcl-2 and Cyclin-D1 enhance apoptosis of osteoblast. A. Cell apoptosis of osteoblast in each group. B. Of cell apoptosis rate in each group. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Journal: American Journal of Translational Research

    Article Title: Downregulation of microRNA-16-5p accelerates fracture healing by promoting proliferation and inhibiting apoptosis of osteoblasts in patients with traumatic brain injury

    doi:

    Figure Lengend Snippet: Downregulation of Bcl-2 and Cyclin-D1 enhance apoptosis of osteoblast. A. Cell apoptosis of osteoblast in each group. B. Of cell apoptosis rate in each group. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Article Snippet: The primary antibodies used were anti-collagen I (1:500, Abcam, USA), anti-Bcl-2 (1:1,000, Abcam, USA), and anti-Cyclin-D1 (1:500, Abcam, USA).

    Techniques:

    Reduction of Bcl-2/Cyclin-D1 suppressed osteoblast proliferation. A. Western blot analysis of control, siRNA-NC, siRNA-Bcl-2, and siRNA-Cyclin-D1 transfection on expression of Bcl-2 and Cyclin-D1 level. B. Cytotoxicity of Bcl-2/Cyclin-D1 on MC3T3-E1 cells. C. The distribution of cell cycles after 24 h treatment. D. Downregulation of Bcl-2/Cyclin-D1 induced cell cycle arrest at the G1 phase. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Journal: American Journal of Translational Research

    Article Title: Downregulation of microRNA-16-5p accelerates fracture healing by promoting proliferation and inhibiting apoptosis of osteoblasts in patients with traumatic brain injury

    doi:

    Figure Lengend Snippet: Reduction of Bcl-2/Cyclin-D1 suppressed osteoblast proliferation. A. Western blot analysis of control, siRNA-NC, siRNA-Bcl-2, and siRNA-Cyclin-D1 transfection on expression of Bcl-2 and Cyclin-D1 level. B. Cytotoxicity of Bcl-2/Cyclin-D1 on MC3T3-E1 cells. C. The distribution of cell cycles after 24 h treatment. D. Downregulation of Bcl-2/Cyclin-D1 induced cell cycle arrest at the G1 phase. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Article Snippet: The primary antibodies used were anti-collagen I (1:500, Abcam, USA), anti-Bcl-2 (1:1,000, Abcam, USA), and anti-Cyclin-D1 (1:500, Abcam, USA).

    Techniques: Western Blot, Transfection, Expressing

    miR-16-5p targets Bcl-2 and Cyclin-D1 to functionally inhibit osteoblast activity in vitro. A. Effect of endogenous miR-16-5p on the luciferase activity of WT Bcl-2/Cyclin-D1 3’UTR (luc-UTR), Bcl-2/Cyclin-D1 3’UTR mutant (luc-UTR-Mut), or the luciferase vector control (luc-vector) after treatment with antagomiR-16-5p in MC3T3-E1 cells. B. Effect of endogenous miR-16-5p on the luciferase activity of WT Bcl-2/Cyclin-D1 3’UTR (luc-UTR), the Bcl-2/Cyclin-D1 3’UTR mutant (luc-UTR-Mut) after treatment with antagomiR-16-5p or its negative control (antagomiR-NC) in MC3T3-E1 cells. C. RT-qPCR analysis of control, agomiR-NC, agomiR-16-5p, antagomiR-NC and antagomiR-16-5p transfection on expression of Bcl-2/Cyclin-D1 protein. D. Western blot analysis of control, agomiR-NC, agomiR-16-5p, antagomiR-NC and antagomiR-16-5p transfection on expression of Bcl-2/Cyclin-D1 protein. E. Bcl-2/Cyclin-D1 expression in serum of mice models. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Journal: American Journal of Translational Research

    Article Title: Downregulation of microRNA-16-5p accelerates fracture healing by promoting proliferation and inhibiting apoptosis of osteoblasts in patients with traumatic brain injury

    doi:

    Figure Lengend Snippet: miR-16-5p targets Bcl-2 and Cyclin-D1 to functionally inhibit osteoblast activity in vitro. A. Effect of endogenous miR-16-5p on the luciferase activity of WT Bcl-2/Cyclin-D1 3’UTR (luc-UTR), Bcl-2/Cyclin-D1 3’UTR mutant (luc-UTR-Mut), or the luciferase vector control (luc-vector) after treatment with antagomiR-16-5p in MC3T3-E1 cells. B. Effect of endogenous miR-16-5p on the luciferase activity of WT Bcl-2/Cyclin-D1 3’UTR (luc-UTR), the Bcl-2/Cyclin-D1 3’UTR mutant (luc-UTR-Mut) after treatment with antagomiR-16-5p or its negative control (antagomiR-NC) in MC3T3-E1 cells. C. RT-qPCR analysis of control, agomiR-NC, agomiR-16-5p, antagomiR-NC and antagomiR-16-5p transfection on expression of Bcl-2/Cyclin-D1 protein. D. Western blot analysis of control, agomiR-NC, agomiR-16-5p, antagomiR-NC and antagomiR-16-5p transfection on expression of Bcl-2/Cyclin-D1 protein. E. Bcl-2/Cyclin-D1 expression in serum of mice models. All data were expressed as means ± SD. Significance is noted at these thresholds: *P

    Article Snippet: The primary antibodies used were anti-collagen I (1:500, Abcam, USA), anti-Bcl-2 (1:1,000, Abcam, USA), and anti-Cyclin-D1 (1:500, Abcam, USA).

    Techniques: Activity Assay, In Vitro, Luciferase, Mutagenesis, Plasmid Preparation, Negative Control, Quantitative RT-PCR, Transfection, Expressing, Western Blot, Mouse Assay

    Inflammation- and apoptosis-related IL-6, IL-1β, Bcl-2, and Bax mRNA levels were measured by quantitative polymerase chain reaction. ##P

    Journal: American Journal of Translational Research

    Article Title: Osthole attenuates myocardial ischemia/reperfusion injury in rats by inhibiting apoptosis and inflammation

    doi:

    Figure Lengend Snippet: Inflammation- and apoptosis-related IL-6, IL-1β, Bcl-2, and Bax mRNA levels were measured by quantitative polymerase chain reaction. ##P

    Article Snippet: After blocking with 5% milk, primary antibodies against Bcl-2 (1:1000, ab59348; Abcam, Cambridge, MA, USA), Bax (1:1000, ab53154; Abcam), caspase-3 (1:1000, #9664; Cell Signaling Technology, Danvers, MA, USA), and caspase-9 (1:1000, #9507; Cell Signaling Technology) were incubated with the membranes overnight at 4°C.

    Techniques: Real-time Polymerase Chain Reaction

    The apoptosis-related proteins Bcl-2, Bax, caspase-3, and caspase-9 were measured by Western blot analysis. ##P

    Journal: American Journal of Translational Research

    Article Title: Osthole attenuates myocardial ischemia/reperfusion injury in rats by inhibiting apoptosis and inflammation

    doi:

    Figure Lengend Snippet: The apoptosis-related proteins Bcl-2, Bax, caspase-3, and caspase-9 were measured by Western blot analysis. ##P

    Article Snippet: After blocking with 5% milk, primary antibodies against Bcl-2 (1:1000, ab59348; Abcam, Cambridge, MA, USA), Bax (1:1000, ab53154; Abcam), caspase-3 (1:1000, #9664; Cell Signaling Technology, Danvers, MA, USA), and caspase-9 (1:1000, #9507; Cell Signaling Technology) were incubated with the membranes overnight at 4°C.

    Techniques: Western Blot

    Chronic ethanol consumption produces hepatic steatosis and apoptosis. (A) Triglyceride (TG) and total cholesterol (TCH) levels in serum and liver tissues. (B) Representative Oil Red O staining of liver tissues 400×. (C) The protein and mRNA levels of PPAR-α and SREBP-1c in liver tissues. (D,E) The protein levels of Bax/Bcl2, cleaved caspase 3 and cleaved caspase9 in liver tissues. β-actin served as a loading control. The values represent means ± SD ( n = 6 in CD-fed group, n = 6 in EtOH-fed group). ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: Chronic ethanol consumption produces hepatic steatosis and apoptosis. (A) Triglyceride (TG) and total cholesterol (TCH) levels in serum and liver tissues. (B) Representative Oil Red O staining of liver tissues 400×. (C) The protein and mRNA levels of PPAR-α and SREBP-1c in liver tissues. (D,E) The protein levels of Bax/Bcl2, cleaved caspase 3 and cleaved caspase9 in liver tissues. β-actin served as a loading control. The values represent means ± SD ( n = 6 in CD-fed group, n = 6 in EtOH-fed group). ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Staining

    Reducing MEG3 expression inhibits EtOH-induced hepatic apoptosis. (A,B) Effect of MEG3 on expression of protein Bax/Bcl2, cleaved caspase 3 and cleaved caspase 9 in EtOH-induced AML-12 cells. The expression of proteins were determined by western blot. β-actin served as a loading control. (C) Flow cytometry analyses of apoptosis. The abscissa represents FITC-Annexin V staining and the ordinate represents PI staining. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: Reducing MEG3 expression inhibits EtOH-induced hepatic apoptosis. (A,B) Effect of MEG3 on expression of protein Bax/Bcl2, cleaved caspase 3 and cleaved caspase 9 in EtOH-induced AML-12 cells. The expression of proteins were determined by western blot. β-actin served as a loading control. (C) Flow cytometry analyses of apoptosis. The abscissa represents FITC-Annexin V staining and the ordinate represents PI staining. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Expressing, Western Blot, Flow Cytometry, Cytometry, Staining

    Lidocaine induced inhibition of growth and metastasis of MKN45 cells were attenuated by miR-145 silence. a miR-145 expression was decreased after transfection with miR-145 inhibitor. miR-145 knockdown ( b ) increased cell proliferation, ( c ) up-regulated Cyclin D1 expression and down-regulated p21 expression, ( d ) inhibited apoptosis, ( e ) increased Bcl-2 expression, decreased cleaved-Caspase-3, -7, and -9 expression. miR-145 knockdown ( f ) increased migration, ( g ) up-regulated MMP-2 and MMP-9 expression, ( h ) increased invasion, and ( i ) up-regulated Vimentin. * p

    Journal: BMC Cancer

    Article Title: Lidocaine inhibits growth, migration and invasion of gastric carcinoma cells by up-regulation of miR-145

    doi: 10.1186/s12885-019-5431-9

    Figure Lengend Snippet: Lidocaine induced inhibition of growth and metastasis of MKN45 cells were attenuated by miR-145 silence. a miR-145 expression was decreased after transfection with miR-145 inhibitor. miR-145 knockdown ( b ) increased cell proliferation, ( c ) up-regulated Cyclin D1 expression and down-regulated p21 expression, ( d ) inhibited apoptosis, ( e ) increased Bcl-2 expression, decreased cleaved-Caspase-3, -7, and -9 expression. miR-145 knockdown ( f ) increased migration, ( g ) up-regulated MMP-2 and MMP-9 expression, ( h ) increased invasion, and ( i ) up-regulated Vimentin. * p

    Article Snippet: The membranes were incubated with the primary antibodies against Bcl-2 (ab32124), cleaved-Casapse-3 (ab49822), cleaved-Caspase-7 (ab32522), cleaved-Caspase-9 (ab52298), MMP-2 (ab37150), MMP-9 (ab73734), Vimentin (ab8978), MEK (ab32576), p-MEK (ab96379), ERK (ab32537), p-ERK (ab131438), p65 (ab16502), p-p65 (ab86299), IκBα (ab32518), p-IκBα (ab32518), and β-actin (ab8227) purchased from Abcam (Cambridge, UK) at the dilution of 1:1000.

    Techniques: Inhibition, Expressing, Transfection, Migration

    The growth of MKN45 cells was inhibited by lidocaine. Lidocaine ( a ) suppressed cell viability, ( b ) inhibited cell proliferation, ( c ) decreased Cyclin D1 expression and increased p21 expression, ( d ) promoted apoptosis, and ( e ) downregulated Bcl-2 expression, and upregulated cleaved-Caspase-3, -7, and -9 expression. Cell viability, proliferation, apoptosis were detected by Cell Counting kit-8 assay, BrdU assay and flow cytometry, respectively. The accumulated levels of CyclinD1, p21 and apoptotic proteins were analyzed by western blot. * p

    Journal: BMC Cancer

    Article Title: Lidocaine inhibits growth, migration and invasion of gastric carcinoma cells by up-regulation of miR-145

    doi: 10.1186/s12885-019-5431-9

    Figure Lengend Snippet: The growth of MKN45 cells was inhibited by lidocaine. Lidocaine ( a ) suppressed cell viability, ( b ) inhibited cell proliferation, ( c ) decreased Cyclin D1 expression and increased p21 expression, ( d ) promoted apoptosis, and ( e ) downregulated Bcl-2 expression, and upregulated cleaved-Caspase-3, -7, and -9 expression. Cell viability, proliferation, apoptosis were detected by Cell Counting kit-8 assay, BrdU assay and flow cytometry, respectively. The accumulated levels of CyclinD1, p21 and apoptotic proteins were analyzed by western blot. * p

    Article Snippet: The membranes were incubated with the primary antibodies against Bcl-2 (ab32124), cleaved-Casapse-3 (ab49822), cleaved-Caspase-7 (ab32522), cleaved-Caspase-9 (ab52298), MMP-2 (ab37150), MMP-9 (ab73734), Vimentin (ab8978), MEK (ab32576), p-MEK (ab96379), ERK (ab32537), p-ERK (ab131438), p65 (ab16502), p-p65 (ab86299), IκBα (ab32518), p-IκBα (ab32518), and β-actin (ab8227) purchased from Abcam (Cambridge, UK) at the dilution of 1:1000.

    Techniques: Expressing, Cell Counting, BrdU Staining, Flow Cytometry, Cytometry, Western Blot

    The RNA or protein expression changes of lung cancer cells with lnc-BMPl-1 over-expression vs. NC cells, the CSE vs. DMSO treated 16HBE cells, and 5-AzaC or TSA treatment. ( A ) The protein expression of Bcl-2, Cav-1 and DNMT3a in different lung cancer cell lines with lnc-BMP1-1 over-expression vs. NC cells; the protein expression were detected using western blotting analyses, protein expression was normalized against GAPDH or α-tubulin protein; the value above each band indicates the fold change of protein expression relative to their control; ( B ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 5 th passage; ( C ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 10 th passage; ( D ) The expression of lnc-BMP1-1 , Cav-1 were reduced in CSE treated 16HBE cells both in 5 th and 10 th passage, and made greater decline in 10 th than in 5 th passage (the same gene was compared in 5 th and 10 th generation of CSE treated 16HBE cells, #P

    Journal: Aging (Albany NY)

    Article Title: Down expression of lnc-BMP1-1 decreases that of Caveolin-1 is associated with the lung cancer susceptibility and cigarette smoking history

    doi: 10.18632/aging.102633

    Figure Lengend Snippet: The RNA or protein expression changes of lung cancer cells with lnc-BMPl-1 over-expression vs. NC cells, the CSE vs. DMSO treated 16HBE cells, and 5-AzaC or TSA treatment. ( A ) The protein expression of Bcl-2, Cav-1 and DNMT3a in different lung cancer cell lines with lnc-BMP1-1 over-expression vs. NC cells; the protein expression were detected using western blotting analyses, protein expression was normalized against GAPDH or α-tubulin protein; the value above each band indicates the fold change of protein expression relative to their control; ( B ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 5 th passage; ( C ) The cell viability of CSE (vs. DMSO) treated 16HBE cells at 10 th passage; ( D ) The expression of lnc-BMP1-1 , Cav-1 were reduced in CSE treated 16HBE cells both in 5 th and 10 th passage, and made greater decline in 10 th than in 5 th passage (the same gene was compared in 5 th and 10 th generation of CSE treated 16HBE cells, #P

    Article Snippet: Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), α-tubulin primary antibodies were purchased from Cell Signaling Technology (Beverly, MA, USA); Cav-1, DNMT3a and Bcl-2 primary antibodies were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Over Expression, Western Blot

    Myocardial Bcl-2 and Bax expression. ( A ) Bcl-2 and Bax protein expressions detected by Western blotting; ( B ) Relative protein expression level of Bcl-2; ( C ) Relative protein expression level of Bax; ( a ) control group; ( b ) 1 μM picroside II pretreatment group; ( c ) 10 μM picroside II pretreatment group; and ( d ) 100 μM picroside II pretreatment group. Notes: Values represent mean ± standard deviation; n=3; * P

    Journal: Drug Design, Development and Therapy

    Article Title: Protective effect of picroside II on myocardial ischemia reperfusion injury in rats

    doi: 10.2147/DDDT.S62355

    Figure Lengend Snippet: Myocardial Bcl-2 and Bax expression. ( A ) Bcl-2 and Bax protein expressions detected by Western blotting; ( B ) Relative protein expression level of Bcl-2; ( C ) Relative protein expression level of Bax; ( a ) control group; ( b ) 1 μM picroside II pretreatment group; ( c ) 10 μM picroside II pretreatment group; and ( d ) 100 μM picroside II pretreatment group. Notes: Values represent mean ± standard deviation; n=3; * P

    Article Snippet: The membranes were blocked with 5% skim milk followed by incubation overnight at 4°C with the antibodies Bcl-2 (1:1000) and Bax (1:1000; Abcam, Cambridge, UK) and Akt (1:500), β-actin (1:1000), phospho-Akt (at Ser473, 1:500), eNOS (1:500), and phospho-eNOS (at Ser1177, 1:500; Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Expressing, Western Blot, Standard Deviation

    Apoptosis related pathway is involved in DEAB-induced anti-cancer effect. (A) Expressions of Bax and Bcl2 in BxPC3, MiaPaCa2 and Panc1 cells treated or untreated with DEAB were detected by western blotting. β-actin was used as a control. Data are representative of four independent experiments. * P

    Journal: Experimental and Therapeutic Medicine

    Article Title: N,N-diethylaminobenzaldehyde targets aldehyde dehydrogenase to eradicate human pancreatic cancer cells

    doi: 10.3892/etm.2020.8691

    Figure Lengend Snippet: Apoptosis related pathway is involved in DEAB-induced anti-cancer effect. (A) Expressions of Bax and Bcl2 in BxPC3, MiaPaCa2 and Panc1 cells treated or untreated with DEAB were detected by western blotting. β-actin was used as a control. Data are representative of four independent experiments. * P

    Article Snippet: The primary antibodies of target proteins were as follows: Anti-B cell lymphoma 2 (Bcl2) associated X protein (Bax; Cell Signaling Technology, Inc.; cat. no. CST 5023T; 1:1,000), anti-Bcl2 (Cell Signaling Technology, Inc.; cat. no. CST 2872; 1:1,000) and anti-β-actin (Affinity Biosciences; cat. no. T0022; 1:1,000).

    Techniques: Western Blot

    The transmembrane domain of Bcl2 is critical for its interaction with SHP. (A) Diagram showing the domain structure of Bcl2 protein. (B) Top, GST pull-down assay to determine the interaction domain of Bcl2 with SHP and the effect of AHPN on the in vitro interaction of Bcl2 with SHP. Bcl2wt, ΔTM, ΔBH1, ΔBH2, and ΔBH3 proteins were detected using an antibody against the N-terminus of Bcl2. ΔBH4 and Δloop plasmids contain a myc epitope, and these proteins were detected using an anti-Myc antibody. Bottom, Bcl2 band intensities were measured by densitometry, and the values were normalized by dividing by the GST-SHP Int intensities. The values for intensities relative to Bcl2 wt (set as 1) were plotted. Data are represented as mean ± SEM (*, P

    Journal: PLoS ONE

    Article Title: Characterization of the Mitochondrial Localization of the Nuclear Receptor SHP and Regulation of Its Subcellular Distribution by Interaction with Bcl2 and HNF4?

    doi: 10.1371/journal.pone.0068491

    Figure Lengend Snippet: The transmembrane domain of Bcl2 is critical for its interaction with SHP. (A) Diagram showing the domain structure of Bcl2 protein. (B) Top, GST pull-down assay to determine the interaction domain of Bcl2 with SHP and the effect of AHPN on the in vitro interaction of Bcl2 with SHP. Bcl2wt, ΔTM, ΔBH1, ΔBH2, and ΔBH3 proteins were detected using an antibody against the N-terminus of Bcl2. ΔBH4 and Δloop plasmids contain a myc epitope, and these proteins were detected using an anti-Myc antibody. Bottom, Bcl2 band intensities were measured by densitometry, and the values were normalized by dividing by the GST-SHP Int intensities. The values for intensities relative to Bcl2 wt (set as 1) were plotted. Data are represented as mean ± SEM (*, P

    Article Snippet: The VDAC antibody (#4661), COX IV antibody (#4850), Hsp60 antibody (#4870), Cyto c antibody (#4280), PARP antibody (#9532), Bcl2 antibody (#2870), myc antibody (#2278), GFP antibody (#2955), GST antibody(#2625), and HNF4α antibody (#3113) were purchased from Cell Signaling.

    Techniques: Pull Down Assay, In Vitro

    SHP protein is localized on the mitochondrial outer membrane. (A) Western blots to detect Flag-mSHP, VADC, COXIV, HSP60, and Cyto C proteins using specific antibodies for each protein, with the exception of SHP, which was detected with an anti-Flag antibody. Huh7 cells were transfected with Flag-mSHP (20 µg, 15 cm plate), and five plates were used to harvest protein. Differential centrifugation was used to isolate the mitochondria-enriched precipitate fraction (P1), microsome-enriched precipitate fraction (P2), and cytosolic supernatant fraction (S); the whole cell lysate (W) was used for comparison. (B) Alkaline digestion of mitochondrial membrane fraction (P m ) and soluble fraction (S m ) and Western blots to determine Flag-mSHP, VADC, COXIV, HSP60, and Cyto C proteins. (C) Trypsin protection assays and Western blots to determine Flag-mSHP, VADC, Bcl2, and Cyto C proteins in mitochondria. Abbreviations: mito, mitochondria; mem, membrane; solu, soluble; peri, peripheral; pt, protein.

    Journal: PLoS ONE

    Article Title: Characterization of the Mitochondrial Localization of the Nuclear Receptor SHP and Regulation of Its Subcellular Distribution by Interaction with Bcl2 and HNF4?

    doi: 10.1371/journal.pone.0068491

    Figure Lengend Snippet: SHP protein is localized on the mitochondrial outer membrane. (A) Western blots to detect Flag-mSHP, VADC, COXIV, HSP60, and Cyto C proteins using specific antibodies for each protein, with the exception of SHP, which was detected with an anti-Flag antibody. Huh7 cells were transfected with Flag-mSHP (20 µg, 15 cm plate), and five plates were used to harvest protein. Differential centrifugation was used to isolate the mitochondria-enriched precipitate fraction (P1), microsome-enriched precipitate fraction (P2), and cytosolic supernatant fraction (S); the whole cell lysate (W) was used for comparison. (B) Alkaline digestion of mitochondrial membrane fraction (P m ) and soluble fraction (S m ) and Western blots to determine Flag-mSHP, VADC, COXIV, HSP60, and Cyto C proteins. (C) Trypsin protection assays and Western blots to determine Flag-mSHP, VADC, Bcl2, and Cyto C proteins in mitochondria. Abbreviations: mito, mitochondria; mem, membrane; solu, soluble; peri, peripheral; pt, protein.

    Article Snippet: The VDAC antibody (#4661), COX IV antibody (#4850), Hsp60 antibody (#4870), Cyto c antibody (#4280), PARP antibody (#9532), Bcl2 antibody (#2870), myc antibody (#2278), GFP antibody (#2955), GST antibody(#2625), and HNF4α antibody (#3113) were purchased from Cell Signaling.

    Techniques: Western Blot, Transfection, Centrifugation

    SHP interacts with Bcl2 primarily through its interaction domain in vitro . (A) Diagram showing GST-mSHP deletion constructs. (B) Left, GST pull-down assay to determine the in vitro interaction of SHP with Bcl2. GST or GST-mSHP full-length or deletion mutants used in the reactions were indicated by asterisks. The interaction of Bcl2 with GST-mSHP proteins was detected by Western blots using a Bcl2 antibody. Right, band intensities were measured by densitometry and normalized to each corresponding GST-mSHP fusion protein. Data are represented as mean ± SEM (#, P

    Journal: PLoS ONE

    Article Title: Characterization of the Mitochondrial Localization of the Nuclear Receptor SHP and Regulation of Its Subcellular Distribution by Interaction with Bcl2 and HNF4?

    doi: 10.1371/journal.pone.0068491

    Figure Lengend Snippet: SHP interacts with Bcl2 primarily through its interaction domain in vitro . (A) Diagram showing GST-mSHP deletion constructs. (B) Left, GST pull-down assay to determine the in vitro interaction of SHP with Bcl2. GST or GST-mSHP full-length or deletion mutants used in the reactions were indicated by asterisks. The interaction of Bcl2 with GST-mSHP proteins was detected by Western blots using a Bcl2 antibody. Right, band intensities were measured by densitometry and normalized to each corresponding GST-mSHP fusion protein. Data are represented as mean ± SEM (#, P

    Article Snippet: The VDAC antibody (#4661), COX IV antibody (#4850), Hsp60 antibody (#4870), Cyto c antibody (#4280), PARP antibody (#9532), Bcl2 antibody (#2870), myc antibody (#2278), GFP antibody (#2955), GST antibody(#2625), and HNF4α antibody (#3113) were purchased from Cell Signaling.

    Techniques: In Vitro, Construct, Pull Down Assay, Western Blot

    miR-15b impact on target gene BCL2 protein expression. A. miR-15b impact on BCL2 protein expression; B. miR-15b impact on BCL2 protein expression analysis * P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: MiR-15b mediates liver cancer cells proliferation through targeting BCL-2

    doi:

    Figure Lengend Snippet: miR-15b impact on target gene BCL2 protein expression. A. miR-15b impact on BCL2 protein expression; B. miR-15b impact on BCL2 protein expression analysis * P

    Article Snippet: BCL2 primary antibody and HRP-tagged IgG secondary antibody were bought from Cell Signaling (USA).

    Techniques: Expressing

    miR-15b impact on target gene BCL2 mRNA expression.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: MiR-15b mediates liver cancer cells proliferation through targeting BCL-2

    doi:

    Figure Lengend Snippet: miR-15b impact on target gene BCL2 mRNA expression.

    Article Snippet: BCL2 primary antibody and HRP-tagged IgG secondary antibody were bought from Cell Signaling (USA).

    Techniques: Expressing

    SOS1 silencing reversed USP22-induced changes in gastric cancer cell behavior and RAS signaling. USP22-overexpressing SGC7901 cells were transfected with shSOS1. a Cell proliferation, apoptosis, migration, and invasion were evaluated. b , c Western blot analysis was performed to measure protein levels of USP22, SOS1, Ras, ERK, p-ERK, c-myc, PI3K, AKT, p-AKT, BAD, and bcl-2 in SGC7901 cells and tumor tissue. GAPDH was used as an internal control. * P

    Journal: Cancer Cell International

    Article Title: Ubiquitin-specific peptide 22 acts as an oncogene in gastric cancer in a son of sevenless 1-dependent manner

    doi: 10.1186/s12935-020-1137-y

    Figure Lengend Snippet: SOS1 silencing reversed USP22-induced changes in gastric cancer cell behavior and RAS signaling. USP22-overexpressing SGC7901 cells were transfected with shSOS1. a Cell proliferation, apoptosis, migration, and invasion were evaluated. b , c Western blot analysis was performed to measure protein levels of USP22, SOS1, Ras, ERK, p-ERK, c-myc, PI3K, AKT, p-AKT, BAD, and bcl-2 in SGC7901 cells and tumor tissue. GAPDH was used as an internal control. * P

    Article Snippet: The membrane was then incubated with primary antibody to human USP22 (Abcam), SOS1 (Abcam), Ras, ERK, p-ERK, c-myc, PI3K, p-PI3K, AKT, p-AKT, BAD (Cell signaling Technology, Danvers, MA, USA), BCL-2 (ABclonal Technology, Woburn, MA, USA), or GAPDH (Abways Biotechnology, Shanghai, China) overnight at 4 °C, followed by 3 washes with Tris-buffered saline containing 0.1% Tween 20 (TBST).

    Techniques: Transfection, Migration, Western Blot

    ABT-737 induces autophagy and dissociation of the BECN1-BCL2 complex after prolonged, but not shorter duration treatment, in wild-type or in Bax and Bak1 KO MEFs. ( A ) Western blot detection of BAX and BAK1 in wild-type (WT) MEFS and in MEFS lacking either BAX ( Bax −/− ), BAK1 ( Bak1 −/− ), or both BAX and BAK1 (DKO). ( B ) Cell death (as measured by flow cytometric staining of propidium iodide ( PI ) uptake) of WT or Bax Bak1 DKO MEFs following treatment with the indicated dose of staurosporine (STS) treatment for the indicated duration. Results represent mean ± s.d. of triplicate samples. ( C ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell types treated with rapamycin (1 μM, 4 h) in the presence or absence of 50 nM Baf A1. GAPDH was used as a loading control. ( D ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with rapamycin (1 μM, 4 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( E ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( D ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( F ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell type treated with the indicated dose of ABT-737 for 12 h. GAPDH was used as a loading control. ( G ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with ABT-737 (10 μM, 12 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( H ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( G ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( I ) Immunoprecipitation of endogenous BECN1 with endogenous BCL2 in WT or Bax Bak1 DKO MEF cells following the indicated treatment. Cells were subjected to starvation (HBSS, 4 h), or ABT-737 for 12 h or 48 h. Western blot detection of LC3B-I to LC3B-II conversion and levels of SQSTM1 were performed to assess autophagy in the same samples used for immunoprecipitation of BECN1-BCL2 complexes. ACTB is shown as a loading control. For ( B ), ( E ) and ( H ), NS = not significant, and *** = P

    Journal: Autophagy

    Article Title: BAX and BAK1 are dispensable for ABT-737-induced dissociation of the BCL2-BECN1 complex and autophagy

    doi: 10.1080/15548627.2015.1017191

    Figure Lengend Snippet: ABT-737 induces autophagy and dissociation of the BECN1-BCL2 complex after prolonged, but not shorter duration treatment, in wild-type or in Bax and Bak1 KO MEFs. ( A ) Western blot detection of BAX and BAK1 in wild-type (WT) MEFS and in MEFS lacking either BAX ( Bax −/− ), BAK1 ( Bak1 −/− ), or both BAX and BAK1 (DKO). ( B ) Cell death (as measured by flow cytometric staining of propidium iodide ( PI ) uptake) of WT or Bax Bak1 DKO MEFs following treatment with the indicated dose of staurosporine (STS) treatment for the indicated duration. Results represent mean ± s.d. of triplicate samples. ( C ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell types treated with rapamycin (1 μM, 4 h) in the presence or absence of 50 nM Baf A1. GAPDH was used as a loading control. ( D ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with rapamycin (1 μM, 4 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( E ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( D ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( F ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell type treated with the indicated dose of ABT-737 for 12 h. GAPDH was used as a loading control. ( G ) Representative photomicrographs of WT MEFs or Bax Bak1 DKO MEFs stably expressing GFP-LC3B and control-treated or treated with ABT-737 (10 μM, 12 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( H ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( G ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( I ) Immunoprecipitation of endogenous BECN1 with endogenous BCL2 in WT or Bax Bak1 DKO MEF cells following the indicated treatment. Cells were subjected to starvation (HBSS, 4 h), or ABT-737 for 12 h or 48 h. Western blot detection of LC3B-I to LC3B-II conversion and levels of SQSTM1 were performed to assess autophagy in the same samples used for immunoprecipitation of BECN1-BCL2 complexes. ACTB is shown as a loading control. For ( B ), ( E ) and ( H ), NS = not significant, and *** = P

    Article Snippet: Western blot analyses of whole cell lysates in samples used for BCL2-BECN1 coimmunoprecipation were performed using the following antibodies: anti-BECN1 (sc-11427; 1:1000 dilution), anti-BCL2 (sc-7382HRP; 1:100 dilution), anti-SQSTM1 (H00008878-M01; 1:3,500 dilution), anti-LC3B (Novus Biologicals, NB100-2220; 1:1,000 dilution), and anti-ACTB/β-actin HRP (Santa Cruz Biotechnology, sc-8432HRP; 1:2,000 dilution).

    Techniques: Western Blot, Flow Cytometry, Staining, Stable Transfection, Expressing, Immunoprecipitation

    ABT-737 induces autophagy and dissociation of the BECN1-BCL2 complex in HCT116 cells lacking BAX and BAK1. ( A ) Western blot detection of BAX and BAK1 in parental HCT116 cells (WT) and in HCT116 cells lacking either BAX ( BAX −/− ), BAK1 ( BAK1 −/− ), or both BAX and BAK1 (DKO). ( B ) Cell death (as measured by flow cytometric staining of propidium iodide (PI) uptake) of WT or BAX BAK1 DKO HCT116 cells following treatment with the indicated dose of staurosporine (STS) treatment for the indicated duration. Results represent mean ± s.d. of triplicate samples. ( C ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell types treated with rapamycin (1 μM, 4 h) in the presence or absence of 50 nM Baf A1. GAPDH was used as a loading control. ( D ) Representative photomicrographs of WT HCT116 cells or BAX BAK1 DKO HCT116 cells stably expressing GFP-LC3B and control-treated or treated with rapamycin (1 μM, 4 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( E ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( D ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( F ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell type treated with the indicated dose of ABT-737 for 12 h. GAPDH was used as a loading control. ( G ) Representative photomicrographs of WT HCT116 cells and HCT116 BAX BAK1 DKO cells stably expressing GFP-LC3B and control-treated or treated with ABT-737 (10 μM, 12 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( H ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( G ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( I ) Immunoprecipitation of endogenous BECN1 with endogenous BCL2 in WT or in BAX BAK1 DKO HCT116 cells following the indicated treatment. Cells were subjected to rapamycin treatment (1 μM, 4 h), starvation (HBSS, 4 h), or the indicated dose of ABT-737 for 12 h. ACTB is shown as a loading control. For ( B ), ( E ) and ( H ), NS = not significant, and *** = P

    Journal: Autophagy

    Article Title: BAX and BAK1 are dispensable for ABT-737-induced dissociation of the BCL2-BECN1 complex and autophagy

    doi: 10.1080/15548627.2015.1017191

    Figure Lengend Snippet: ABT-737 induces autophagy and dissociation of the BECN1-BCL2 complex in HCT116 cells lacking BAX and BAK1. ( A ) Western blot detection of BAX and BAK1 in parental HCT116 cells (WT) and in HCT116 cells lacking either BAX ( BAX −/− ), BAK1 ( BAK1 −/− ), or both BAX and BAK1 (DKO). ( B ) Cell death (as measured by flow cytometric staining of propidium iodide (PI) uptake) of WT or BAX BAK1 DKO HCT116 cells following treatment with the indicated dose of staurosporine (STS) treatment for the indicated duration. Results represent mean ± s.d. of triplicate samples. ( C ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell types treated with rapamycin (1 μM, 4 h) in the presence or absence of 50 nM Baf A1. GAPDH was used as a loading control. ( D ) Representative photomicrographs of WT HCT116 cells or BAX BAK1 DKO HCT116 cells stably expressing GFP-LC3B and control-treated or treated with rapamycin (1 μM, 4 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( E ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( D ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( F ) Western blot detection of LC3B conversion and SQSTM1 degradation in the indicated cell type treated with the indicated dose of ABT-737 for 12 h. GAPDH was used as a loading control. ( G ) Representative photomicrographs of WT HCT116 cells and HCT116 BAX BAK1 DKO cells stably expressing GFP-LC3B and control-treated or treated with ABT-737 (10 μM, 12 h). Hoechst (blue) represents nuclear staining. GFP-LC3B puncta (green) correspond to autophagosomes. Scale bars: 10 μm. ( H ) Quantification of the number of GFP-LC3B puncta per cell in cells treated as in ( G ) in the absence or presence of 50 nM Baf A1. Results represent mean ± s.d. of triplicate samples (500 cells analyzed per sample). ( I ) Immunoprecipitation of endogenous BECN1 with endogenous BCL2 in WT or in BAX BAK1 DKO HCT116 cells following the indicated treatment. Cells were subjected to rapamycin treatment (1 μM, 4 h), starvation (HBSS, 4 h), or the indicated dose of ABT-737 for 12 h. ACTB is shown as a loading control. For ( B ), ( E ) and ( H ), NS = not significant, and *** = P

    Article Snippet: Western blot analyses of whole cell lysates in samples used for BCL2-BECN1 coimmunoprecipation were performed using the following antibodies: anti-BECN1 (sc-11427; 1:1000 dilution), anti-BCL2 (sc-7382HRP; 1:100 dilution), anti-SQSTM1 (H00008878-M01; 1:3,500 dilution), anti-LC3B (Novus Biologicals, NB100-2220; 1:1,000 dilution), and anti-ACTB/β-actin HRP (Santa Cruz Biotechnology, sc-8432HRP; 1:2,000 dilution).

    Techniques: Western Blot, Flow Cytometry, Staining, Stable Transfection, Expressing, Immunoprecipitation

    Propofol effect on apoptosis-associated proteins in TG-treated ARPE-19 cells. (A) Representative western blot for Bcl2. (B) Propofol attenuated the Bcl2 downregulation induced by TG in ARPE-19 cells. ARPE-19 cells were precubated with propofol for 12 h at different concentration, the treated with 1 μM TG for 12 h. The data are presented as the mean ± SEM from three independent experiments. Statistical analysis was performed by one-way analysis of variance with all pairwise multiple comparison procedures done by Tukey test. # p

    Journal: PLoS ONE

    Article Title: Propofol Decreases Endoplasmic Reticulum Stress–Mediated Apoptosis in Retinal Pigment Epithelial Cells

    doi: 10.1371/journal.pone.0157590

    Figure Lengend Snippet: Propofol effect on apoptosis-associated proteins in TG-treated ARPE-19 cells. (A) Representative western blot for Bcl2. (B) Propofol attenuated the Bcl2 downregulation induced by TG in ARPE-19 cells. ARPE-19 cells were precubated with propofol for 12 h at different concentration, the treated with 1 μM TG for 12 h. The data are presented as the mean ± SEM from three independent experiments. Statistical analysis was performed by one-way analysis of variance with all pairwise multiple comparison procedures done by Tukey test. # p

    Article Snippet: Then, the proteins were probed with anti-PERK antibody (1:200, sc-32577, Santa Cruz Biotechnology), anti-p-PERK antibody (1:200, sc-377400, Santa Cruz Biotechnology), anti-p-eIF2α antibody (1:1,000, 3597, Cell Signaling Technology), anti-ATF4 antibody (1:1,000, 11815, Cell Signaling Technology), anti-active caspase 12 antibody (1:1,000, ab62484, Abcam), anti-cleaved caspase 3 antibody (1:1,000, 9964, Cell Signaling Technology), anti-BiP antibody (1:1,000, 3177, Cell Signaling Technology), anti-ERK1/2 antibody (1:800, 9102, Cell Signaling Technology), anti-p-ERK1/2 antibody (1:800, 4370, Cell Signaling Technology), and anti-Bcl2 antibody (1:800, 15071, Cell Signaling Technology).

    Techniques: Western Blot, Concentration Assay