Following a TRAIL: Update on a ligand and its five receptors

Kimberley, Fiona C.; Screaton, Gavin

doi:10.1038/sj.cr.7290236

Cited by 221 publications

(202 citation statements)

References 118 publications

(122 reference statements)

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“…27 We have demonstrated here that although CaP cells are resistant to TRAIL, the cytotoxicity can be significantly enhanced when combined with freezing. The combination was then applied to normal human prostate cells to evaluate potential therapeutic effects.…”

Section: Trail and Freezing Ablate Prostate Cancer Cells Dm Clarke Et Almentioning

confidence: 71%

“…25,26 Tumor necrosis factor related apoptosis-inducing ligand (TRAIL) is a member of the TNFR superfamily and induces apoptosis through engagement of death receptors. [27][28][29] TRAIL is a cytotoxic agent that preferentially induces apoptosis in a variety of human cancers both in vitro and in vivo, whereas normal cells remain less affected. 28 However, some tumor cell types including those of the prostate remain resistant to the apoptogenic effects of TRAIL.…”

Section: Introductionmentioning

confidence: 99%

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Targeted induction of apoptosis via TRAIL and cryoablation: a novel strategy for the treatment of prostate cancer

Clarke

Robilotto

VanBuskirk

et al. 2007

Prostate Cancer Prostatic Dis

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Adjuvant therapies contribute to the successful treatment of cancer. Our previous reports have shown that combining cryoablation with cytotoxic agents enhances cell death. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a cytotoxic agent that preferentially induces apoptosis in a variety of human cancer cells. Human prostate cancer cells (PC-3) are resistant to many cytodestructive agents, including cryoablation and TRAIL. Here, we evaluated the effects of TRAIL combined with cryoablation on PC-3 and normal prostate (RWPE-1) cell death. Exposure of PC-3 cells to freezing (À101C) or TRAIL (500ng/ml) results in minimal cell death, whereas a complete loss of viability is observed with the simultaneous combination. The synergistic effect was found to be due to a marked increase in apoptosis. Western blot analysis revealed a significant level of caspase-8 and -3 cleavage between 12 and 24 h post-exposure. Caspase activation assays provided similar results and also indicated a role for caspase-9. Inhibitors to caspase-8 and -9 along with a pan-caspase inhibitor were incorporated to determine which pathway was necessary for the combined efficacy. Inhibition of caspase-8 significantly blocked the combination-induced cell death compared to cells that did not receive the inhibitor (63% compared to 10% viable). The addition of the caspase-9 inhibitor resulted in only a minimal protection. Importantly, the combination was not effective when applied to normal prostate cells. The results describe a novel therapeutic model for the treatment of prostate cancer and provide support for future in vivo studies.

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Section: Trail and Freezing Ablate Prostate Cancer Cells Dm Clarke Et Almentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Targeted induction of apoptosis via TRAIL and cryoablation: a novel strategy for the treatment of prostate cancer

Clarke

Robilotto

VanBuskirk

et al. 2007

Prostate Cancer Prostatic Dis

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“…8C). Anyway, TNFRSF10A and TNFRSF10B can form a heterodimer (50). However, the role of their interaction has not been elucidated.…”

Section: Discussionmentioning

confidence: 99%

DDIT3 and KAT2A Proteins Regulate TNFRSF10A and TNFRSF10B Expression in Endoplasmic Reticulum Stress-mediated Apoptosis in Human Lung Cancer Cells

Lei

et al. 2015

Journal of Biological Chemistry

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Background:The mechanisms of transcriptional regulation of TNFRSF10A and TNFRSF10B are not well described. Results: DDIT3 and KAT2A cooperatively up-regulated TNFRSF10A and TNFRSF10B. Conclusion: DDIT3 and KAT2A promote the transcription of TNFRSF10A and TNFRSF10B via the AP-1 and DDIT3 binding sites, respectively. Significance: Our findings offer new insights on the mechanisms of ER stress-mediated apoptosis.

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“…It is a Type II transmembrane protein with an extracellular (C-terminus) domain, which can be cleaved, resulting in a soluble form. Unlike TNF-a which is cleaved by metalloproteinases, TRAIL is cleaved by a cysteine protease (Kimberley and Screaton, 2004). The soluble form, in addition to the membrane bound form, is biologically active.…”

mentioning

confidence: 99%

TRAIL resistance results in cancer progression: a TRAIL to perdition?

Malhi

Gores

2006

Oncogene

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Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL, APO-2L) is a mediator of cell death that preferentially targets cancer cells. The potential of TRAIL as a chemotherapeutic agent is limited, however, because of the emergence of TRAIL resistance. Furthermore, recent studies have demonstrated that alternative TRAIL signaling is unmasked in TRAIL resistant cells. In these cells, the predominant effect of TRAIL receptor activation is the activation of nuclear factor-jB (NF-jB), which promotes tumor metastases and invasion. TRAIL resistance can occur at the level of the death inducing signaling complex via upregulation of cFLIP or via an increase in antiapoptotic proteins of the Bcl-2 family. A paradigm emerges from this information, that chemotherapy, targeting NF-jB, cFLIP, or antiapoptotic proteins of the Bcl-2 family, in combination with TRAIL maybe more rational than TRAIL therapy alone.

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Following a TRAIL: Update on a ligand and its five receptors

Cited by 221 publications

References 118 publications

Targeted induction of apoptosis via TRAIL and cryoablation: a novel strategy for the treatment of prostate cancer

Targeted induction of apoptosis via TRAIL and cryoablation: a novel strategy for the treatment of prostate cancer

DDIT3 and KAT2A Proteins Regulate TNFRSF10A and TNFRSF10B Expression in Endoplasmic Reticulum Stress-mediated Apoptosis in Human Lung Cancer Cells

TRAIL resistance results in cancer progression: a TRAIL to perdition?

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