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Role of IG20 Splice Variants in TRAIL Resistance

Authors' Affiliation: Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois

Requests for reprints: Bellur S. Prabhakar, Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, 835 South Wolcott Street (MC 790), Chicago, IL 60612. Phone: 312-996-4945; Fax: 312-996-6415; E-mail: bprabhak{at}uic.edu.

Abstract

Tumor necrosis factor receptor–related apoptosis-inducing ligand (TRAIL) can induce apoptosis primarily in cancer cells with little or no effect on normal cells; therefore, it has the potential for use in cancer therapy. TRAIL binding to death receptors DR4 and DR5 triggers the death-inducing signal complex formation and activation of procaspase-8, which in turn activates caspase-3, leading to cell death. Like FasL, TRAIL can trigger type 1 (caspase-8 caspase-3) or type 2 (caspase-8 Bid cleavage capsase-9 caspase-3) apoptotic pathways depending on the cell type. Some cancers are resistant to TRAIL treatment because most molecules in the TRAIL signaling pathway, including FLIPs and IAPs, can contribute to resistance. In addition, we have identified an essential role for splice variants of the IG20 gene in TRAIL resistance.

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