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Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
Author(s) -
Mandal Debabrata,
Moitra Prasun K,
Saha Samiran,
Basu Joyoti
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02294-9
Subject(s) - phosphatidylserine , phagocytosis , translocase , microbiology and biotechnology , phospholipid scramblase , flippase , apoptosis , oxidative stress , biology , caspase , chemistry , biochemistry , biophysics , programmed cell death , chromosomal translocation , membrane , phospholipid , gene
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.