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Abstract
We report here that the chemotactic peptide, N-formyl-methionyl-leucyl-phenylalanine (FMLP), and the mitogenic phorbol ester, phorbol myristate acetate (PMA) cause a time- and concentration-dependent, selective, extracellular release of N-acetyl-β-glucosaminidase and lysozyme from freshly isolated, adherent human peripheral blood monocytes. The inability of the protein synthesis inhibitor, cycloheximide, to influence enzyme release indicates that these enzymes are constitutive secretory products. 1- O-Hexadecyl-/octadecyl-2- O-acetyl-sn-glyceryl-3-phosphorylcholine demonstrated moderate secretory activity, whereas pepstatin A, concanavalin A, and leukotriene B 4 were essentially inactive. FMLP- and PMA-induced enzyme release were inhibited with the intracellular calcium antagonist, 8-( N,N-diethylamino)-octyl-(3,4,5-trimethoxy)benzoate hydrochloride and the anion channel blocker, 4,4′-diisothiocyano-2,2′-disulfonic acid stilbene. These results demonstrate the capacity of soluble, surface-active stimuli to activate the human monocyte secretory process.
Published Version
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