Removal or oxidation of surface membrane sialic acid inhibits formyl-peptide-induced polymorphonuclear leukocyte chemotaxis.

Polymorphonuclear leukocyte (PMN) surface membrane glycoproteins are probably involved in the phenomenon of stimulus-response coupling. Consequently, we examined the effects of either removal or oxidation of surface membrane-associated sialic acid residues on some responses of human PMN to chemotactic factors. Treatment of human PMN with either neuraminidase or sodium metaperiodate did not affect the ability of these cells to migrate randomly, but did inhibit their ability to respond chemotactically to the synthetic peptide N-formyl-methionyl-leucyl-phenylalanine (FMLP). Treated PMN responded normally, however, to the complement-derived peptide C5a, and to the lipoxygenase product leukotriene B4. Enzymatic removal or oxidation of membrane sialic acid residues did not affect either FMLP-induced PMN degranulation or FMLP-induced generation by PMN of superoxide anion radicals. Removal of sialic acid did not significantly alter specific binding of [3H]FMLP to its receptor(s) on the PMN membrane. These findings indicate that sialic acid residues on the PMN surface membrane play an important role in modulating PMN responses to FMLP.