Characteristics of aggregated immunoglobulin G as an immunologic phagocytic stimulus for granule enzyme release from human neutrophils

Abstract

Aggregated immunoglobulin G (AggIgG) induced a time- and concentration-dependent phagocytic release of granule-associated lysozyme and myeloperoxidase (MPO) from human neutrophils. Degranulation was significantly enhanced in the presence of calcium or magnesium, and maximum granule exocytosis was observed when both divalent cations were present. AggIgG-stimulated enzyme release was inhibited with the intracellular calcium antagonist, TMB-8[8-(N, N-diethyl-amino)-octyl-(3,4,5-trimethoxy)benzoate] in the absence of extracellular calcium, DIDS (4,4′-diisothiocyano-2,2′-disulfonic acid stilbene), a permeant anion channel blocker, also suppressed AggIgG-induced degranulation. Cycloheximide, an inhibitor of protein synthesis, enhanced granule exocytosis from AggIgG-treated neutrophils. Two inhibitors of transmethylation reactions, 3-deazaadenosine (3-DZA) and homocysteine thiolactone (HCTL) in combination, suppressed AggIgG-elicited granule enzyme release. These data indicate that AggIgG is a useful probe for investigating the requirements for phagocytic enzyme release from human neutrophils.

DOI: 10.1007/BF00915995

8 Figures and Tables

Cite this paper

@article{Smith1986CharacteristicsOA, title={Characteristics of aggregated immunoglobulin G as an immunologic phagocytic stimulus for granule enzyme release from human neutrophils}, author={Robert J. Smith and Susan C. Speziale and Roger G. Ulrich and Barbara J. Bowman}, journal={Inflammation}, year={1986}, volume={10}, pages={131-143} }