Defects in death-inducing signalling complex formation prevent JNK activation and Fas-mediated apoptosis in DU 145 prostate carcinoma cells

Curtin, James F.; Cotter, Thomas G.

doi:10.1038/sj.bjc.6601393

Cited by 5 publications

(6 citation statements)

References 33 publications

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“…Few anticancer reagents work on the hormone-refractory prostate cancer. It is well known that androgen-independent cancer cells are resistant to radiotherapy, chemotherapy, and Fas-mediated apoptosis (Suzuki et al, 2000;Curtin and Cotter, 2003). In this study, however, we observed that ASA in combination with TRAIL effectively induces cytotoxicity to androgen-dependent LNCaP and its derivative androgen-independent cells.…”

Section: Discussioncontrasting

confidence: 48%

Aspirin Enhances Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Mediated Apoptosis in Hormone-Refractory Prostate Cancer Cells through Survivin Down-Regulation

Yoo

2007

Mol Pharmacol

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Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a promising cancer therapeutic agent because of its tumor selectivity. TRAIL is known to induce apoptosis in cancer cells but spare most normal cells. In this study, we examined whether acetylsalicylic acid (ASA), so-called aspirin, enhances TRAIL-induced apoptosis in androgen-dependent LNCaP and androgenindependent LNCaP-derived prostate cancer cells. To evaluate the cell death effects of TRAIL in combination with ASA on tumor cells, we performed DNA fragmentation assay and immunoblot analysis for poly(ADP-ribose) polymerase-1, caspases, and antiapoptotic proteins. We observed that ASA promoted TRAILinduced apoptotic death in both LNCaP and its derived cells (C4, C4-2, and C4-2B). These enhancements of TRAIL's effect were related to the decrease in survivin protein expression by pretreatment with ASA. We also confirmed that knockdown in survivin expression by transfecting survivin small interfering RNA increased TRAIL-induced apoptosis. To study the mechanism of survivin down-regulation, we determined the levels of mRNA and the activities of survivin promoter in the ASA-treated and untreated cells. Reduction of the intracellular levels of survivin protein was due to a decrease in transcriptional activity. Data from electrophoretic mobility shift assay and chromatin immunoprecipitation analyses revealed that ASA inhibited the transcription factor E2F-1 binding activity to the survivin promoter region, which is known to regulate survivin gene transcription. Taken together, our studies suggested that ASA-promoted TRAIL cytotoxicity is mediated by down-regulating survivin, and the down-regulation of survivin is due to inhibition of E2F-1 binding activity to the survivin promoter region.

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Section: Discussioncontrasting

confidence: 48%

Aspirin Enhances Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Mediated Apoptosis in Hormone-Refractory Prostate Cancer Cells through Survivin Down-Regulation

Yoo

2007

Mol Pharmacol

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“…The failure of androgen ablation therapy leads to a hormone‐refractory state of the disease. It is well known that androgen‐independent cancer cells are resistant to radiotherapy, chemotherapy, and Fas‐mediated apoptosis [Suzuki et al, 2000; Curtin and Cotter, 2003]. Nonetheless, previous studies show that DTX is an effective anti‐cancer agent against HRPC [Chowdhury et al, 2007].…”

Section: Discussionmentioning

confidence: 99%

Pretreatment of docetaxel enhances TRAIL‐mediated apoptosis in prostate cancer cells

Yoo

2008

J of Cellular Biochemistry

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Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a promising cancer therapeutic agent because of its tumor selectivity. TRAIL is known to induce apoptosis in cancer cells but spare most normal cells. In this study, we examined whether treatment of docetaxel (DTX) can enhance apoptotic cell death by TRAIL against androgen-independent prostate cancer (AIPC). The cell death effect of combinations of TRAIL and docetaxel on prostate cancer cell lines (androgen-dependent LNCaP and its derived androgen-independent, metastatic C4-2B) was evaluated by synergisms of apoptosis. Western blot assay and DNA fragmentation assay were used to study the underlying mechanisms of cell death and search for any mechanisms of enhancement of TRAIL induced apoptosis in the presence of docetaxel. In addition, we investigated the in vitro anti-tumor effects of combined docetaxel and TRAIL using MAP kinase inhibitors. Docetaxel itself could not induce apoptotic cell death in 24 h even in high concentration. Apoptotic cell death, however, was drastically enhanced by pretreatment of docetaxel 20 h before TRAIL treatment. Docetaxel enhanced the PARP-1 cleavage and caspases activation by TRAIL especially in androgen-independent, metastatic C4-2B cell line, mainly by phosphorylation of Bcl-2 by JNK activation. It appears that apoptotic cell death was protected by the JNK inhibitor SP600125. The results of our study show that pretreatment of docetaxel is able to enhance the apoptosis produced by TRAIL in prostate cancer cells, especially in hormone-refractory prostate cancer (HRPC).

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“…Phosphorylated HSPB1 is supposed to interact with Daxx, preventing its translocation to the cytosol, and thus inhibits binding of Daxx to Fas receptor and Daxx-dependent apoptosis (51,52). This suggestion was not confirmed in a recently published paper (70), and one cannot exclude that HSPB1 somehow affects not only the Daxx-dependent pathway but can also affect the FADDdependent activation of caspase-8.…”

Section: H Hspb1 In Apoptosis and Carcinogenesismentioning

confidence: 93%

Large Potentials of Small Heat Shock Proteins

Mymrikov

Seit-Nebi

Gusev

2011

Physiological Reviews

373

414

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Modern classification of the family of human small heat shock proteins (the so-called HSPB) is presented, and the structure and properties of three members of this family are analyzed in detail. Ubiquitously expressed HSPB1 (HSP27) is involved in the control of protein folding and, when mutated, plays a significant role in the development of certain neurodegenerative disorders. HSPB1 directly or indirectly participates in the regulation of apoptosis, protects the cell against oxidative stress, and is involved in the regulation of the cytoskeleton. HSPB6 (HSP20) also possesses chaperone-like activity, is involved in regulation of smooth muscle contraction, has pronounced cardioprotective activity, and seems to participate in insulin-dependent regulation of muscle metabolism. HSPB8 (HSP22) prevents accumulation of aggregated proteins in the cell and participates in the regulation of proteolysis of unfolded proteins. HSPB8 also seems to be directly or indirectly involved in regulation of apoptosis and carcinogenesis, contributes to cardiac cell hypertrophy and survival and, when mutated, might be involved in development of neurodegenerative diseases. All small heat shock proteins play important "housekeeping" roles and regulate many vital processes; therefore, they are considered as attractive therapeutic targets.

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Defects in death-inducing signalling complex formation prevent JNK activation and Fas-mediated apoptosis in DU 145 prostate carcinoma cells

Cited by 5 publications

References 33 publications

Aspirin Enhances Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Mediated Apoptosis in Hormone-Refractory Prostate Cancer Cells through Survivin Down-Regulation

Aspirin Enhances Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Mediated Apoptosis in Hormone-Refractory Prostate Cancer Cells through Survivin Down-Regulation

Pretreatment of docetaxel enhances TRAIL‐mediated apoptosis in prostate cancer cells

Large Potentials of Small Heat Shock Proteins

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