The Journal of biological chemistry · 2002
Hepatocyte Fas-associating death domain protein/mediator of receptor-induced toxicity (FADD/MORT1) levels increase in response to pro-apoptotic stimuli.
СтатьяПоддержка исследования: вне правительства СШАПоддержка службы здравоохранения СШАНазвание и аннотация: Перевод в очереди
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Kim Peter K M, Wang Yinna, Gambotto Andrea, Kim Young-Myeong, Weller Richard, Zuckerbraun Brian S, Hua Yun, Watkins Simon C, Billiar Timothy R
Аннотация
We examined the regulation of Fas-associating death domain (FADD) protein as an important adaptor molecule in apoptosis signaling and hypothesized that the regulation of FADD could contribute to hepatocyte death. FADD/mediator of receptor-induced toxicity (MORT1) is required for activation of several signaling pathways of cell death. In this study we report the interesting and unexpected result that actinomycin D increased the expression of FADD protein, and we demonstrate that other cellular stresses like ultraviolet irradiation or heat shock could also increase FADD levels in hepatocytes. In cells treated with actinomycin D, FADD levels were elevated homogeneously in the cytoplasm. The increase in cytoplasmic FADD protein by actinomycin D or FADD overexpression alone both correlated with cell death, and specific antisense inhibition of FADD expression consistently diminished approximately 30% of the cell death induced by actinomycin D. These data indicate that FADD protein expression can increase rapidly in hepatocytes exposed to broadly cytotoxic agents.
Предметные рубрики MeSH
Adaptor Proteins, Signal TransducingAdenoviridaeAnimalsApoptosisCarrier ProteinsCaspase 8Caspase 9CaspasesCell SurvivalCells, CulturedCycloheximideDactinomycinDose-Response Relationship, DrugEnzyme ActivationFas-Associated Death Domain ProteinHSP70 Heat-Shock ProteinsHepatocytesHot TemperatureHumansMaleMiceMice, Inbred C57BLMolecular Sequence DataProtein Synthesis InhibitorsRatsRats, Sprague-DawleySignal TransductionTime FactorsUltraviolet Rays