Protein kinase C activation precedes XXXX release during IgG-mediated phagocytosis.

@entity1 @entity2366 @entity3348 @entity4515 @entity1426 @entity7131 @entity3900 @entity866 @entity460 @entity18398 @entity11616 @entity7098 @entity35844
Previous studies demonstrated that both @entity7131 ( @entity7131 ) and @entity1426 (AA) are required for IgG-mediated phagocytosis by @entity1 monocytes. We have characterized a @entity460 -independent "phagocytic" @entity3900 (designated pPL) that mediates @entity1426 release. The present studies were designed to order @entity7131 and pPL in the phagocytic signaling pathway. The @entity7131 inhibitors @entity866 and @entity11616 caused a coordinated decrease in phagocytosis of IgG-opsonized erythrocytes and @entity1426 release. The @entity7098 activators mastoparan and @entity3348 restored phagocytosis to @entity7131 -inhibited cells, but were ineffective in monocytes pretreated with the pPL inhibitor @entity35844 . Similarly, @entity7131 activation with @entity4515 and @entity2366 enhanced phagocytosis in the absence, but not in the presence, of @entity35844 . These results indicate that pPL may be regulated by an upstream phosphorylation event. Thus, we examined the effects of Ab-opsonized glass bead ingestion, @entity18398 -mediated inhibition of phosphatases, and @entity4515 treatment on the activity of pPL and on its distribution between the cytosolic and membrane-associated compartments. IgG-opsonized erythrocytes and okadaic acid caused an overall increase in pPL activity, with a twofold increase in membrane-associated pPL. @entity4515 treatment caused a 1.8-fold increase in membrane-associated pPL activity. @entity18398 and @entity4515 mimic IgG-opsonized erythrocytes with respect to membrane activation of pPL, suggesting that pPL activity may be regulated by @entity7131 . Collectively, these results indicate that pPL activity is modulated by @entity7131 during IgG-mediated phagocytosis, and that the @entity7131 requirement can be bypassed by direct activation of pPL.
