Abstract
Platelet storage at 04 C suppresses bacterial multiplication, but induces clusters of glycoprotein (GP) Ibalpha that trigger their phagocytosis by macrophages and reduce their survival after transfusion. We searched for a method that detects cold-induced changes in GPIbalpha involved in phagocytosis.STUDY DESIGN AND METHODS: Human platelets were isolated and stored for up to 48 hrs at 0C. Binding of a PE-labeled antibody directed against amino acids 1–35 on GPIbalpha (AN51-PE) was compared with phagocytosis of platelets by matured monocytic THP-1 cells, analyzed by FACS.RESULTS: Freshly isolated platelets were detected as a single population of AN51-PE positive particles and showed < 5% phagocytosis. Cold storage led to a decrease in AN51-PE binding and an increase in phagocytosis. N-acetylglucosamine (GlcNAc), known to interfere with macrophage recognition of GPIbalpha clusters, restored normal AN51-PE binding to cold-stored platelets and suppressed phagocytosis.CONCLUSIONS: We conclude that binding of an antibody against AA 1–35 on GPIbalpha reflects changes in GPIbalpha that make platelets targets for phagocytosis by macrophages.
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