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Department of Immunology and Cell Biology, Research Center Borstel, Borstel, Germany
Platelet factor 4 (PF-4), a member of the 
-chemokine subfamily
of cytokines, activates human neutrophils independently of
intracellular free calcium mobilization or binding to IL-8R. In the
present study, we have identified and partially characterized a
receptor for PF-4 on human neutrophils, which displays weak
cross-reactivity with the IFN-
-inducible protein 10, but not with
other -chemokines such as IL-8, neutrophil-activating peptide 2, or
melanoma growth-stimulatory activity (GRO). Binding studies revealed
that human neutrophils express a high number of receptors
(Bmax 
7.6 x 106
sites/cell) of moderate affinity (Kd 
650
nM). The kinetics of PF-4-binding correlates with the proportion of
PF-4 tetramers in solution and with the activation of neutrophils for
exocytosis. Reduction of PF-4 binding and PF-4-induced exocytosis in
the presence of various glycosaminoglycans or following treatment of
cells with chondroitinase ABC (but not other
glycosaminoglycan-degrading enzymes) altogether demonstrates that the
PF-4 receptor is a proteoglycan of the chondroitin sulfate class.
Cross-linking experiments with radiolabeled PF-4 revealed a
receptor-ligand complex of 250 kDa. Taken together, our data show
that a distinct chondroitin sulfate proteoglycan represents specific
receptors for tetrameric PF-4 on human
neutrophils.
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