Role of glycoprotein Ibalpha in phagocytosis of platelets by macrophages

Autor: W Martin Smid, Hans Deckmyn, Gerrit Spierenburg, Bahram A Badlou, Hans Ulrichts, Jan-Willem N. Akkerman
Jazyk: angličtina
Rok vydání: 2006
Předmět:
Zdroj: Transfusion, 46(12), 2090-9. Wiley
ISSN: 0041-1132
Popis: 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.
Databáze: OpenAIRE