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- W2212084842 abstract "Proc Amer Assoc Cancer Res, Volume 46, 20052261 We have previously demonstrated that two IgG3-avidin fusion proteins specific for the rat and human transferrin receptors (anti-rat TfR IgG3-Av and anti-hTfR IgG3-Av) formed strong non-covalent interactions with different biotinylated molecules and delivered them into cancer cells. In addition, we reported that these fusion proteins exhibited potent antiproliferative/proapoptotic activity against hematopoietic malignant cell lines (Ng et al., PNAS, 2002, 99:10706). We now report that anti-hTfR IgG3-Av down-regulates cell surface TfR and directs it to intracellular degradation. Studies using the malignant B lymphocytic cell line ARH-77 provide evidence that the internalized TfR is degraded into multiple fragments by serine and cysteine proteases. In addition, we demonstrated that following TfR degradation, ARH-77 cells exhibit mitochondrial membrane depolarization and activation of caspase 9, 3 and 8. Iron, but not zinc supplement effectively prevents mitochondrial damage and cell death, suggesting that anti-hTfR IgG3-Av induces apoptosis by causing iron deprivation. This hypothesis is further supported by data showing that ARH-77 cells treated with the iron chelator deferioxamine (DFO) or anti-hTfR IgG3-Av have similar profiles and kinetics of mitochondrial membrane depolarization and apoptosis. These events, however, cannot be fully blocked by co-incubation of anti-hTfR IgG3-Av with a pan-caspase inhibitor. This report provides important insights into the mechanism of apoptosis induced by anti-hTfR IgG3-Av. Further development of this fusion protein as a drug delivery system and as a tumoricidal agent may lead to effective therapeutics for hematopoietic malignancies such as multiple myeloma." @default.
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- W2212084842 date "2005-05-01" @default.
- W2212084842 modified "2023-09-28" @default.
- W2212084842 title "Mechanism of apoptosis induced by an IgG3-avidin fusion protein specific for the human transferrin receptor" @default.
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