Journal: Cancer cell

Article Title: Synthetic Lethality of Combined Bcl-2 Inhibition and p53 Activation in AML: Mechanisms and Superior Antileukemic Efficacy

doi: 10.1016/j.ccell.2017.11.003

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Rabbit polyclonal anti-Puma (clone H-136) , Santa Cruz Biotechnology , Cat#sc-28226; RRID: AB_2064827.

Techniques: Recombinant, Imaging, Staining, Mutagenesis, Transfection, shRNA, Negative Control, Plasmid Preparation, Control, Software, In Vivo Imaging, Microscopy, Flow Cytometry

Journal: Heliyon

Article Title: Optimization of resource recovery technologies in the disassembly of waste lithium batteries: A study on selective lithium extraction

doi: 10.1016/j.heliyon.2024.e40251

Figure Lengend Snippet: Characterization analysis equipment (a. Emprean Multipurpose X-ray Scatterer; b. S8 TIGER X-ray Fluorescence Spectrometer).

Article Snippet: Scanning electron microscopy with SEM analysis, conducted with the Bruker's S8 TIGER X-ray fluorescence spectrometer ( b), allowed for detailed investigations into the microstructure and composition of the roasting residue, elucidating surface morphology and element distribution.

Techniques: Fluorescence

Journal: Breast cancer research and treatment

Article Title: Zerumbone causes Bax and Bak-mediated apoptosis in human breast cancer cells and inhibits orthotopic xenograft growth in vivo

doi: 10.1007/s10549-012-2280-5

Figure Lengend Snippet: p53 and PUMA are dispensable for zerumbone (ZER)-induced apoptosis. a Immunoblotting for PUMA (p53 upregulated mediator of apoptosis) using lysates from MDA-MB-231 and MCF-7 cells after 24 or 36 hour treatment with DMSO or ZER (20 or 40 µM). The blots were re-probed with anti-actin antibody as a loading control. Numbers on top of the immunoreactive bands represent changes in protein levels relative to corresponding DMSO-treated control. b Quantitation of apoptotic fraction (early + late apoptotic cells) in wild-type HCT-116 cells (WT) and PUMA knockout HCT-116 cells (PUMA KO) following 48 hour treatment with DMSO or indicated concentrations of ZER. Quantitation relative to DMSO-treated WT HCT-116 cells is shown. c Effect of ZER treatment on proliferation of wild-type HCT-116 cells (WT) and PUMA knockout HCT-116 cells (PUMA KO) after 48 hour treatment with DMSO or the indicated concentrations of ZER as determined by cell proliferation assay. Quantitation relative to DMSO-treated WT HCT-116 cells is shown. In panels b and c, data represent mean ± SD (n=3). Significantly different (P<0.05) compared with respective to acorresponding DMSO-treated control and bbetween WT and PUMA KO HCT-116 cells by one-way ANOVA followed by Bonferroni's multiple comparison test. d Immunoblotting for p53 protein using lysates from MCF-7 cells transiently transfected with a nonspecific control siRNA and p53-targeted siRNA and treated for 24 hours with either DMSO (control) or 20 µM of ZER. Quantitation relative to control siRNA transfected cells treated with DMSO is shown above bands. Percentage of (e) sub G0G1 fraction and (f) G2/M fractions in MCF-7 cells transiently transfected with control siRNA and p53-targeted siRNA and treated for 24 hours with DMSO (control) or 20 µM of ZER. Results shown are mean ± SD (n=3). aSignificantly different (P<0.05) compared with DMSO-treated control by one-way ANOVA followed by Bonferroni's multiple comparison test. Each experiment was done at least twice and the results were consistent.

Article Snippet: Sources of antibodies were as follows: antibodies against Cdc25C, cleaved poly-(ADP-ribose)-polymerase (PARP), and p53 were from Cell Signaling Technology (Danvers, MA); anti-cyclin B1, anti-cyclin-dependent kinase 1 (Cdk1), anti-Bak, anti-Bax, and anti-p53 upregulated mediator of apoptosis (PUMA) antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA); antibodies against Cdc25B and active Bax (for immunofluorescence microscopy) were purchased from BD Biosciences (San Diego, CA); anti-Bcl-2 antibody was from Dako-Agilent Technologies (Houston, TX); an antibody specific for detection of active Bak (for immunofluorescence microscopy) was from Calbiochem (Billerica, MA); and anti-actin antibody was from Sigma-Aldrich.

Techniques: Western Blot, Control, Quantitation Assay, Knock-Out, Proliferation Assay, Comparison, Transfection

Journal: Breast cancer research and treatment

Article Title: Zerumbone causes Bax and Bak-mediated apoptosis in human breast cancer cells and inhibits orthotopic xenograft growth in vivo

doi: 10.1007/s10549-012-2280-5

Figure Lengend Snippet: Bcl-2 overexpression failed to confer protection against zerumbone (ZER)-induced apoptosis. Immunoblotting for (a) Bcl-2 in control and ZER-treated MDA-MB-231 and MCF-7 cells and (b) Bcl-2 and cleaved PARP in MDA-MB-231 and MCF-7 cells transiently transfected with pSFFV-neo empty vector or pSFFV vector encoding for Bcl-2 and treated for 24 hours with DMSO or the indicated concentrations of ZER. Numbers on top of the immunoreactive bands represent changes in protein levels relative to corresponding DMSO-treated control (panel a) or empty vector transfected cells treated with DMSO (panel b). c Quantitation of histone-associated DNA fragment release into the cytosol, and (d) cell survival in MDA-MB-231 and MCF-7 cells transiently transfected with empty vector or pSFFV vector encoding for Bcl-2 and treated for 24 hours with DMSO or the indicated concentrations of ZER. Results shown are mean ± SD (n=3). Quantitation relative to DMSO-treated empty vector transfected cells is shown. Significantly different (P<0.05) compared with arespective DMSO-treated control and bbetween empty vector transfected and Bcl-2 overexpressing cells by one-way ANOVA followed by Bonferroni's multiple comparison test. Each experiment was done at least twice and representative data from one such experiment are shown.

Article Snippet: Sources of antibodies were as follows: antibodies against Cdc25C, cleaved poly-(ADP-ribose)-polymerase (PARP), and p53 were from Cell Signaling Technology (Danvers, MA); anti-cyclin B1, anti-cyclin-dependent kinase 1 (Cdk1), anti-Bak, anti-Bax, and anti-p53 upregulated mediator of apoptosis (PUMA) antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA); antibodies against Cdc25B and active Bax (for immunofluorescence microscopy) were purchased from BD Biosciences (San Diego, CA); anti-Bcl-2 antibody was from Dako-Agilent Technologies (Houston, TX); an antibody specific for detection of active Bak (for immunofluorescence microscopy) was from Calbiochem (Billerica, MA); and anti-actin antibody was from Sigma-Aldrich.

Techniques: Over Expression, Western Blot, Control, Transfection, Plasmid Preparation, Quantitation Assay, Comparison

Journal: Breast cancer research and treatment

Article Title: Zerumbone causes Bax and Bak-mediated apoptosis in human breast cancer cells and inhibits orthotopic xenograft growth in vivo

doi: 10.1007/s10549-012-2280-5

Figure Lengend Snippet: Critical role for Bax and Bak in zerumbone (ZER)-induced apoptosis. a Fluorescence microscopy for analysis of active Bax and Bak in MDA-MB-231 and MCF-7 cells after 8 hour treatment with DMSO or 20 µM of ZER. Staining for mitochondria (MitoTracker Green) and activated Bak or Bax is indicated by green and red colors, respectively. b Representative flow histograms depicting apoptotic fraction quantitation in SV40 immortalized mouse embryonic fibroblasts (MEF) derived from wild-type mice (WT) and Bak and Bax double knockout (DKO) mice after 24 hour treatment with DMSO or indicated concentration of ZER. c Quantitation of apoptotic cells (Annexin V-FITC/PI method) in SV40 immortalized MEFs derived from wild type mice (WT) and Bak-Bax double knockout (DKO) mice. The MEF were treated for 24 or 48 hours with DMSO (control) or the indicated concentrations of ZER and processed for flow cytometry. Quantitation relative to DMSO-treated WT MEF is shown. Results shown are mean ± SD (n=3). Significantly different (P<0.05) compared with arespective DMSO-treated control and bbetween WT and DKO by one-way ANOVA followed by Bonferroni's multiple comparison test. Each experiment was done at least twice and representative data from one such experiment are shown.

Article Snippet: Sources of antibodies were as follows: antibodies against Cdc25C, cleaved poly-(ADP-ribose)-polymerase (PARP), and p53 were from Cell Signaling Technology (Danvers, MA); anti-cyclin B1, anti-cyclin-dependent kinase 1 (Cdk1), anti-Bak, anti-Bax, and anti-p53 upregulated mediator of apoptosis (PUMA) antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA); antibodies against Cdc25B and active Bax (for immunofluorescence microscopy) were purchased from BD Biosciences (San Diego, CA); anti-Bcl-2 antibody was from Dako-Agilent Technologies (Houston, TX); an antibody specific for detection of active Bak (for immunofluorescence microscopy) was from Calbiochem (Billerica, MA); and anti-actin antibody was from Sigma-Aldrich.

Techniques: Fluorescence, Microscopy, Staining, Quantitation Assay, Derivative Assay, Double Knockout, Concentration Assay, Control, Flow Cytometry, Comparison