TAILIEUCHUNG - Báo cáo khoa học: a-Fetoprotein positively regulates cytochrome c-mediated caspase activation and apoptosome complex formation

Previous results have shown that theoncoembryonicmarker a-fetoprotein (AFP) is able to induce apoptosis in tumor cells through activation of caspase 3, bypassing Fas-dependent and tumor necrosis factor receptor-dependent signaling. In this study we further investigate the molecular interactions involvedin the AFP-mediatedsignaling of apoptosis. We show that AFP treatment of tumor cells is accompaniedby cytosolic translocation of mitochondrial cytochromec. In a cell-free system, AFP mediates process-ing andactivation of caspases 3 and9 by synergistic enhancement of the low-dose cytochromec-mediated sig-nals | Eur. J. Biochem. 270 4388-4399 2003 FEBS 2003 doi a-Fetoprotein positively regulates cytochrome c-mediated caspase activation and apoptosome complex formation Lidia Semenkova1 I Elena Dudich1 I Igor Dudich1 Natalie Tokhtamisheva1 Edward Tatulov2 Yury Okruzhnov3 Jesus Garcia-Foncillas3 Juan-Antonio Palop-Cubillo4 and Timo Korpela5 Institute of Immunological Engineering Moscow Russia 2Anticancer Drug Research Center Moscow Russia Departments of 3Oncology and 4Organic Chemistry and Pharmacology University of Navarra Pamplona Spain 5Joint Finnish-Russian Biotechnology Laboratory Turku University Finland Previous results have shown that the oncoembryonic marker a-fetoprotein AFP is able to induce apoptosis in tumor cells through activation of caspase 3 bypassing Fas-dependent and tumor necrosis factor receptor-dependent signaling. In this study we further investigate the molecular interactions involvedin the AFP-meidatedsignaling of apoptosis. We show that AFP treatment of tumor cells is accompaniedby cytosolic translocation of mitochondrial cytochrome c. In a cell-free system AFP mediates processing and activation of C í sf í í e33 add b by synergistic enhancement of the low-dose cytochrome c-mediated signals. AFP was unable to regulate activity of caspase 3 in cell extracts depleted of cytochrome c or caspase d. Using high-resolution chromatography we show that AFP positively regulates cytochrome c dATP-mediated apoptosome complex formation enhances recruitment of caspases and Apaf-1 into the complex and I dease of the active caspases 3 and 9 from the apopiotome. By Liting a dí reel protein-protein interaction assay we show that pure human AFP almost completely disrupts the association between processed caspaees 3 11119 a and tire u-tiluOs inhibitor of apoptosis protein cIAP-2 demonstrating its release from the complex. Our data suggest that AFP may regulate cell death by displacing cIAP-2 from the apoptosome resulting tn .

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