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Biochem. Pharmacol. October 24, epub ahead of print. Ibandronate  increases the expression of the pro-apoptotic gene FAS by epigenetic mechanisms in tumor cells. 2012

Thaler, R., Spitzer, S., Karlic, H., Berger, C., Klaushofer, K. and Varga, F.

Notes: Caspase-Glo® 3/7 and Caspase-Glo® 8 Assays were used to assess activation of apoptosis pathways in MC3T3-E1 cells (clonal mouse), U-2 OS human osteoscarcoma cell line and CCL-51 cells (mouse mammary gland tumor cells). Although ibandronate reduced cell proliferation in all cell lines, its effect on activation of caspases was different in neoplastic versus non-neoplastic cells. Caspase-8 and caspase-3/7 activities were reduced in MC3T3-E1 cells after 72 hours treatment with ibandronate. In two tumor cell lines assayed, opposite results were seen: caspase-8 and caspase-3/7 activities increased in U-2 OS cells and in CCL-51 cells. Luminescence was detected using a GloMax® 96 Microplate Luminometer. (Figure 1 in the paper)

To analyze FAS promoter methylation levels, fragments of the targeted promoter regions were generated by digestion of genomic DNA using CpG methylation insensitive restriction enzymes MboII and PstI from cells cultured in the presence of ibandronate for varying lengths of time. The authors demonstrated that FAS promoter methylation is altered in tumor cells in the presence of ibandronate. (4253)

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J. Biol. Chem. 286, 21546–21554. TWEAK induces apoptosis through a death-signaling complex comprising Receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8. 2011

Ikner, A. and Ashkenazi, A.

Notes: The authors of this study set out to describe the mechanism of cell death through which TNF-like weak inducer of apoptosis (TWEAK) exerts its apoptotic effect on certain cancer cells. The used the CellTiter-Glo® Cell Viability Assay and the the Caspase-Glo® 3/7 Assay to investigate cell viability and mechanism of cell death in HSC3 cells treated with TWEAK. They looked at caspase-8 activity in cells treated with TWEAK in the presence or absence of a caspase-8 inhibitor using the Caspase-Glo® 8 Assay. They showed that TWEAK induces caspase-dependent apoptosis in these cells. (4170)

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Mol. Cancer Res. 8, 729–738. Bortezomib sensitizes human renal cell carcinomas to TRAIL apoptosis through increased activation of caspase-8 in the death-inducing signaling complex. 2010

Brooks, A.D., Jacobsen, K.M., Li, W., Shanker, A. and Sayers, T.J.

Notes: Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) tends to cause apoptosis in tumor cells over normal cells, and so the TRAIL ligand and signaling pathway is an attractive pathway for developing cancer therapeutics. Bortezomib is a proteasome inhbitor that is used for therapy in many cancers. Studies indicate that it can sensitize tumor cells to the apoptotic effects of TRAIL. In this study, the authors investigated the ability of bortezomib on renal cell carcinoma (RCC). Growth inhibition of RCC in response to treatment with bortezomib followed by TRAIL treatment in the presence or absence of caspase inhibitors was assessed using the CellTiter® 96 AQueous Non-Radioactive Cell Proliferation Assay. They assessed caspase activity in bortezomib/TRAI- treated RCC using the Caspase-Glo® 8 Assay. The effect of bortezomib on the proteasome of the RCCs was investigated using the Proteasome-Glo™ Chymotrypsin-Like Cell-Based Assay. Their studies suggest that bortezomib can sensitize some RCC to TRAIL signaling. (4169)

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Expert Opin. Drug Metab. Toxicol. 4, 103–120. Bioluminescent assays for ADMET 2008

Cali, J.J., Niles, A., Valley, M.P., O’Brien, M.A., Riss, T.L., and Shultz, J.

Notes: The authors of this review article highlight the use of bioluminescence as a readout for high-throughput ADME/Tox assays. They discuss three strategies for designing bioluminescent assays, using either luciferase, ATP or luciferin substrates as the limiting reagents for a luciferase-catalyzed reaction. Reporter gene assays limit the production of luciferase by tying it to a promoter or DNA regulatory region of interest. Such assays can be used to study genes that are regulated by drugs and other xenobiotics. Bioluminescent assays in which ATP is the limiting reagent of the luciferase reaction can be designed to monitor cell viability or the activity kinases. Bioluminescent assays in which the substrate is limiting can be designed so that the activity of a particular enzyme results in the production of a luciferin substrate that can, in turn, be acted upon by luciferase. (3926)

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Assay Drug Dev. Technol. 5, 127–136. Bioluminescent assays for high-throughput screening 2007

Fan, F. and Wood, K.V.

Notes: The authors of this paper review bioluminescent assay technologies, discussing HTS reporter, cell-based and luciferase biosensor assays. They divide luminescent assays into three basic categories: assays that measure ATP concentration (cell viability and kinase assays), assays that measure changes in luciferase levels (reporter assays, GPCR assays), and assays that measure changes in luciferin levels (protease [including caspase], P450 and MAO assays). (3737)

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Cancer Res. 66, 8172-81. Zebrafish as a "biosensor"? Effects of ionizing radiation and amifostine on embryonic viability and development. 2006

Geiger, G.A, Parker S.E., Beothy, A.P., Tucker, J.A., Mullins, M.C., and Kao, G.D.

Notes: In this study, the Caspase-Glo® 8 and Caspase-Glo® 9 Assays were used to assess caspase activation in Zebrafish embryos after radiation exposure. After irradiation, caspase activation, morphological abnormalities, and DNA fragmentation were observed, all three of which could be partially reversed by treatment with the radiomodifier amifostine. The Caspase-Glo® 9 Assay was shown to be sensitive enough to detect the effects of radiation on as few as 2 embryos. The authors concluded that the Caspase-Glo® Assays provided an effective and convenient means for rapidly assessing the lethal effects of radiation on Zebrafish embryos, and for assaying the ability of the radiomodifier to counteract these effects. The assay could be performed within hours of radiation exposure directly on the embryos in a 96-well plate format. (3571)

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Infect. Immun. 73, 5194–7. Intracellular survival of Campylobacter jejuni in human monocytic cells and induction of apoptotic death by cytholethal distending toxin. 2005

Hickey, T.E., Majam, G. and Guerry, P.

Notes: Bacterial cytolethal distending toxin (CDT) is known to induce apoptosis of immune cells, but little is known of the toxin from Campylobacter jejuni. In this study, the authors examined the effects of C. jejuni CDT on cultured monocytes. The human monocyte line 28SC was inoculated with 2µg Campylobacter membrane proteins per milliliter of culture. After 8 hours, the cells were harvested and assessed for caspase-8 or caspase-9 activity using the Caspase-Glo® 8 and Caspase-Glo® 9 Assays, respectively. The 28SC cells were pulsed with 6.2 µM camptothecin for 2 hours as a positive control for apoptosis. (3288)

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J. Biol. Chem. 280(19), 19401–9. Selective knockdown of the long variant of cellular FLICE inhibitory protein augments death receptor-mediated caspase-8 activation and apoptosis. 2005

Sharp, D.A., Lawrence, D.A. and Ashkenazi, A.

Notes: Researchers were interested in determining if knockdown of cellular FLICE inhibitory protein (c-FLIP) would affect caspase-8 activation. Instead of assaying cultured cells for the Caspase-Glo® 8 Assay, the authors used siRNAs targeting c-FLIPL, c-FLIPS or nontarget control to transfect A549 cells. Equal number of cells were harvested and treated with FLAG-tagged Apo2L/TRAIL + anti-FLAG M2 antibody at 37°C for various times prior to lysis. The lysate was immunoprecipitated overnight using protein A/G beads. After washing with lysis buffer, the beads were resuspended in phosphate buffer and the immobilized death-inducing signaling complex (DISC) was assayed for caspase-8 activity in 96-well plates using an equal volume of Caspase-Glo® 8 Reagent.

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J. Immunol. 173, 4286-4296. Divergent trophoblast responses to bacterial products mediated by TLRs 2004

Abrahams, V.M., Bole-Aldo, P., Kim, Y.M., Straszewski-Chavez, S.L., Chaiworapongsa, T., Romero, R. and Mor, G.

Notes: In this paper, researchers examined the effect of activating mammalian homologues of the Drosophila Toll receptor gene (TDR) on apoptosis in the trophoblast cell lines HTR8 and 3A. Bacterial peptidoglycan (PDG) was used to indirectly activate caspase-3/7, -8 and -9 through TDRs. Caspase activity was measured using the Capase-Glo™ 3/7, 8 and 9 Assays. Caspase-3/7, -8 and -9 activities decreased in both the HTR8 and 3A cell lines transiently transfected with a Fas Associated Death Domain (FADD-DN). Data were expressed as relative light units and were normalized to protein levels in lysates. (3171)

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J. Biol. Chem. 279, 48434–48442. Nuclear import of proinflammatory transcription factors is required for massive liver apoptosis induced by bacterial lipopolysaccharide. 2004

Liu, D., Li, C., Chen, Y., Burnett, C., Liu, X.Y., Downs, S., Collins, R.D., and Hawiger, J.

Notes: The Caspase-Glo® 3/7, -8 and -9 Assays were used to  measure Caspase-3, -8, and -9 activities in mouse liver homogenates. The authors describe a modified procedure for making liver homogenates in a hypotonic extraction buffer.  Homogenates were cleared with a 15 minute spin at 13,000 x g and normalized to a 1mg/ml concentration before use the assays. Data comparing control and cSN50 peptide-treated animals at various time points are presented.  (3213)

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