4.5 Article

Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes

Journal

FEBS LETTERS
Volume 513, Issue 2-3, Pages 184-188

Publisher

WILEY
DOI: 10.1016/S0014-5793(02)02294-9

Keywords

caspase 3; human erythrocyte; phospholipid asymmetry; phosphatidylserine; aminophospholipid translocase; phagocytosis

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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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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