Cytotoxicity of Tumor Necrosis Factor related apoptosis-inducing ligand towards Ewing's sarcoma cell lines
Open Access
- 22 February 2001
- journal article
- research article
- Published by Springer Nature in Oncogene
- Vol. 20 (8) , 1010-1014
- https://doi.org/10.1038/sj.onc.1204154
Abstract
Death ligands of the Tumor Necrosis Factor (TNF) family are known to induce apoptosis upon binding to their cognate receptors. However, the clinical utility of these cytokines as anticancer agents has been limited due to unacceptable toxicity. TRAIL is a recently isolated death ligand that possesses selective anti-tumor activity against a number of cancer cell lines without significant systemic toxicity. In this report we present evidence that cell lines derived from Ewing's Sarcoma (ES) are uniformly sensitive to TRAIL-mediated apoptosis. Furthermore, unlike TNF-α, treatment with TRAIL fails to induce the anti-apoptotic and pro-inflammatory NF-κB pathway in the ES cell lines. Our results suggest that TRAIL may prove to be a useful agent for the treatment of Ewing's sarcoma and related peripheral neuroectodermal tumors.Keywords
This publication has 14 references indexed in Scilit:
- Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligandNature Medicine, 2000
- Molecular Biology of the Ewing’s Sarcoma/Primitive Neuroectodermal Tumor FamilyJournal of Clinical Oncology, 2000
- Modulation of the NF-κB pathway by virally encoded Death Effector Domains-containing proteinsOncogene, 1999
- Safety and antitumor activity of recombinant soluble Apo2 ligandJournal of Clinical Investigation, 1999
- The Novel Receptor TRAIL-R4 Induces NF-κB and Protects against TRAIL-Mediated Apoptosis, yet Retains an Incomplete Death DomainImmunity, 1997
- Death Receptor 5, a New Member of the TNFR Family, and DR4 Induce FADD-Dependent Apoptosis and Activate the NF-κB PathwayImmunity, 1997
- TUMOUR NECROSIS FACTOR-INDUCED NECROSIS VERSUS ANTI-Fas-INDUCED APOPTOSIS IN L929 CELLSCytokine, 1997
- Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmACurrent Biology, 1996
- Book NotesManuscripta, 1996
- Crystal structure of an isoleucine-zipper trimerNature, 1994