Characteristics of N-formyl-methionyl-leucyl-phenylalanine as an inducer of lysosomal enzyme release from human neutrophils.

N-formyl-methionyl-leucyl-phenylalanine (FMLP) stimulated a time- and concentration-dependent release of granule associated beta-glucuronidase and lysozyme but not cytoplasmic lactate dehydrogenase from human neutrophils. Maximum discharge of lysome activity released is insignificant when cells are not preincubated with cytochalasin B prior to being exposed to FMLP (10(-10)-10(-7) M); although 11.2 +/- 1.3 and 12.4 +/- 1.1% of total activity for beta-glucuronidase and lysozyme, respectively, is secreteer, had no effect on FMLP-elicited lysosomal enzyme extrusion. 8-(N,N-diethylamino)-octyl-3,4,5-trimethoxybenzoate hydrochloride (TMB-8), a purported antagonist of intracidating the role of calcium in the mechanism of lysosomal enzyme release.