Role of glycoprotein Ibalpha in phagocytosis of platelets by macrophages

Bahram A Badlou, Gerrit Spierenburg, Hans Ulrichts, Hans Deckmyn, W Martin Smid, Jan-Willem N Akkerman*

*Corresponding author for this work

    Research output: Contribution to journalArticleAcademicpeer-review

    20 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)2090-9
    Number of pages10
    Issue number12
    Publication statusPublished - Dec-2006


    • Acetylglucosamine/pharmacology
    • Antibodies, Monoclonal/metabolism
    • Blood Platelets/physiology
    • Filtration
    • Humans
    • Macrophages/immunology
    • Phagocytosis
    • Platelet Glycoprotein GPIb-IX Complex/physiology

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