A possible requirement for arachidonic acid lipoxygenation in the mechanism of phagocytic degranulation by human neutrophils stimulated with aggregated immunoglobulin G

Aggregated immunoglobulin G (AggIgG) caused a concentration-dependent extracellular release of granule-associated lysozyme and myeloperoxidase (MPO) from human neutrophils. Generation of the 5-lipoxygenase product of arachidonic acid (AA) metabolism, 5(S), 12(R)-dihydroxy-6,14-cis,8,10-trans-eicosat...

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Veröffentlicht in:Biochemical and biophysical research communications 1986-04, Vol.136 (1), p.310-315
Hauptverfasser: Smith, Robert J., Yein, Fred S., Speziale, Susan C., Bowman, Barbara J.
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Sprache:eng
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Zusammenfassung:Aggregated immunoglobulin G (AggIgG) caused a concentration-dependent extracellular release of granule-associated lysozyme and myeloperoxidase (MPO) from human neutrophils. Generation of the 5-lipoxygenase product of arachidonic acid (AA) metabolism, 5(S), 12(R)-dihydroxy-6,14-cis,8,10-trans-eicosatetraenoic acid [leukotriene B 4 (LTB 4)], by neutrophils exposed to AggIgG occurred in the presence but not absence of exogenous AA. U-60,257B (piriprost potassium), an inhibitor of leukotriene synthesis, caused a dose-related suppression of LTB 4 production and granule exocytosis by AggIgG-treated cells. These data suggest that a lipoxygenase product of AA metabolism may mediate AggIgG-induced phagocytic release of granule constituents from neutrophils.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(86)90911-3