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.
journal_name
Transfusionjournal_title
Transfusionauthors
Badlou BA,Spierenburg G,Ulrichts H,Deckmyn H,Smid WM,Akkerman JWdoi
10.1111/j.1537-2995.2006.01034.xsubject
Has Abstractpub_date
2006-12-01 00:00:00pages
2090-9issue
12eissn
0041-1132issn
1537-2995pii
TRF01034journal_volume
46pub_type
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