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. 2002 Feb 27;513(2-3):184-8.
doi: 10.1016/s0014-5793(02)02294-9.

Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes

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Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes

Debabrata Mandal et al. FEBS Lett. .
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Abstract

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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