Publication | Closed Access
Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
187
Citations
20
References
2002
Year
Lipid PeroxidationApoptosisImmunologyRed CellsCell DeathRedox BiologyCellular PhysiologyOxidative StressInflammationAutophagyCell SignalingRedox SignalingBiochemistryGranulocyteReactive Oxygen SpecieCell BiologyRegulates Phosphatidylserine ExternalizationPhagocyteSignal TransductionNatural SciencesPhysiologyCaspase 3Cellular BiochemistryMedicine
The appearance of phosphatidylserine (PS) on the outer surface of red cells is an important signal for their uptake by macrophages. We report for the first time that procaspase 3 present in the anucleated mature human erythrocyte is activated under oxidative stress induced by t-butylhydroperoxide leading to impairment of the aminophospholipid translocase, PS externalization and increased erythrophagocytosis. This is the first report linking caspase 3 activation to inhibition of flippase activity and uptake of red cells by macrophages.
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