GLYCOSYLATION IMPROVES THE PRIMING EFFECT EXERTED BY RECOMBINANT HUMAN GRANULOCYTE-COLONY-STIMULATING FACTOR (LENOGRASTIM) ON HUMAN NEUTROPHIL SUPEROXIDE PRODUCTION

The role of glycosylation in modulating the activity of recombinant hu man granulocyte colony-stimulating factor (rHuG-CSF) on polymorphonucl ear leukocytes (PMNs) was investigated. We addressed this study by com paring the effects of lenograstim (glycosylated rHuG-CSF) and its degl ycosylated counterpart on superoxide production by PMNs on fibronectin . When the triggering activity of the cytokine was evaluated, no O-2(- ) release was elicited from neutrophils treated with either preparatio n of rHuG-CSF. Instead, a clear potentiation of both fMLP- and TNF-ind uced respiratory burst was produced by preincubating the cells with rH uG-CSF. Such effect was found to be significantly increased when glyco sylated versus deglycosylated preparation was used, leading to the con clusion that the sugar moiety of the molecule could be of importance i n improving the priming activity exerted by rHuG-CSF on PMN metabolic response.