Esterase dependence of human neutrophil functions: lysozyme secretion, spontaneous migration, and continuity of the respiratory burst.
To assess the esterase dependency of human neutrophil secretion of lysosomal enzyme, the influence of several aromatic amino acid esters on phorbol myristate acetate-induced release of lysozome was studied. This function was found to be esterase-dependent on the basis of the inhibitory influence of such esters. Of the esters tested, tryptophan octyl ester, tryptophan benzyl ester, benzoyl tyrosine ethyl ester, and tryosine methyl ester were the most potent inhibitors of this response, being effective in the order listed. All esters with inhibitory effects were active at concentrations of less than or equal to 100 muM. Other neutrophil functions found to be similarly sensitive to the presence of these esters were spontaneous and chemotactic migration an continuity of the respiratory burst. The common inhibition profile of these neutrophil activities by the esters used suggests the activity of a common enzyme in these various functions.
D000596:Amino Acids / Q000494:pharmacology; D002634:Chemotaxis, Leukocyte / Q000187:drug effects; D004950:Esterases / Q000037:antagonists & inhibitors / Q000502:physiology*; D006801:Humans; D009113:Muramidase / Q000378:metabolism*; D009504:Neutrophils / Q000201:enzymology*; D010101:Oxygen Consumption
D000596:Amino Acids; D004950:Esterases; D009113:Muramidase