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Role of glycoprotein Ibα in phagocytosis of platelets by macrophages
Author(s) -
Badlou Bahram A.,
Spierenburg Gerrit,
Ulrichts Hans,
Deckmyn Hans,
Smid W. Martin,
Akkerman JanWillem N.
Publication year - 2006
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1111/j.1537-2995.2006.01034.x
Subject(s) - phagocytosis , platelet , macrophage , antibody , glycoprotein , population , chemistry , biology , microbiology and biotechnology , immunology , biochemistry , in vitro , medicine , environmental health
BACKGROUND: Platelet (PLT) storage at 0 to 4°C suppresses bacterial multiplication, but induces clusters of glycoprotein (GP) Ibα that trigger their phagocytosis by macrophages and reduce their survival after transfusion. A method was sought that detects cold‐induced changes in GPIbα involved in phagocytosis. STUDY DESIGN AND METHODS: Human PLTs were isolated and stored for up to 48 hours at 0°C. Binding of a phycoerythrin (PE)‐labeled antibody directed against amino acids (AA) 1‐35 on GPIbα (AN51‐PE) was compared with phagocytosis of PLTs by matured monocytic THP‐1 cells, analyzed by fluorescence‐activated cell sorting. RESULTS: Freshly isolated PLTs were detected as a single population of AN51‐PE–positive particles and showed less than 5 percent phagocytosis. Cold storage led to a decrease in AN51‐PE binding and an increase in phagocytosis. N ‐Acetylglucosamine, known to interfere with macrophage recognition of GPIbα clusters, restored normal AN51‐PE binding to cold‐stored PLTs and suppressed phagocytosis. CONCLUSIONS: It is concluded that binding of an antibody against AA 1‐35 on GPIbα reflects changes in GPIbα that make PLTs targets for phagocytosis by macrophages.