Effect of tunicamycin C2 on the induction of crystal induced chemotactic factor in human neutrophils

We have investigated the effect of tunicamycin-C2, which specifically inhibits glycosylation of proteins but not their synthesis, in the induction of crystal-induced chemotactic factor (CCF) in human neutrophils by monosodium urate crystals. Tunicamycin C2 appears to impair transport of the CCF to the lysosomal fraction of the cell and its subsequent secretion into the extracellular fluid, resulting in accumulation of nonglycosylated chemotactic proteins in the cytosol. Based on the results of affinity chromatography studies with various lectins, the carbohydrate moiety(ies) of the glycosylated chemotactic peptide contain mannose, N-acetyl-D-galactosamine, galactose, and fucose.