Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
[摘要] 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.
[发布日期] [发布机构]
[效力级别] [学科分类] 生物化学/生物物理
[关键词] Caspase 3;Human erythrocyte;Phospholipid asymmetry;Phosphatidylserine;Aminophospholipid translocase;Phagocytosis;PS;phosphatidylserine;PE;phosphatidylethanolamine;PC;phosphatidylcholine;NBD-PS;1-palmitoyl-2-[6-[7(nitrobenz-2-oxa-1;3-diazol-4-yl)amino]-caproyl]-sn-glycerol-3-phosphoserine;t-BHP;t-butylhydroperoxide;Z-DEVD-FMK;benzyloxycarbonyl-Asp(OCH3)-Glu(OCH3)-Val-Asp(OCH3)-fluoromethylketone;Ac;acetyl;pNA;p-nitroanilide [时效性]
