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Title: Role of glycoprotein Ibalpha in phagocytosis of platelets by macrophages
Authors: Badlou, Bahram A ×
Spierenburg, Gerrit
Ulrichts, Hans
Deckmyn, Hans
Smid, W Martin
Akkerman, Jan-Willem N #
Issue Date: Nov-2006
Series Title: Transfusion vol:46 issue:12 pages:2090-2099
Abstract: BACKGROUND: Platelet (PLT) storage at 0 to 4 degrees C suppresses bacterial multiplication, but induces clusters of glycoprotein (GP) Ibalpha that trigger their phagocytosis by macrophages and reduce their survival after transfusion. A method was sought that detects cold-induced changes in GPIbalpha involved in phagocytosis. STUDY DESIGN AND METHODS: Human PLTs were isolated and stored for up to 48 hours at 0 degrees C. Binding of a phycoerythrin (PE)-labeled antibody directed against amino acids (AA) 1-35 on GPIbalpha (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 GPIbalpha 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 GPIbalpha reflects changes in GPIbalpha that make PLTs targets for phagocytosis by macrophages.
ISSN: 0041-1132
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Chemistry, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

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