We have established that polymorphonuclear neutrophil (PMN)-binding anti-Fcgamma receptor IIIb (FcgammaRIIIb) autoantibodies (autoAb) inhibit the function of these cells but extend their survival. Here, we show that recombinant FcgammaRIIIb (rFcgammaRIIIb), as well as purified FcgammaRIIIb (pFcgammaRIIIb), deteriorated the PMN adherence and respiratory burst in a dose-dependent manner. Furthermore, rFcgammaRIIIb and pFcgammaRIIIb reduced the level of annexin V-binding PMN from 23.6 +/- 1.6 % to 6.3 +/- 1.0 and 11.0 +/- 1.0 %, respectively, while human serum albumin exerted no effects. Incubation of rFcgammaRIIIb with those autoAb binding to soluble FcgammaRIIIb resulted in the attachment of such immune complexes (IC) to the cells, thereby also delaying apoptosis (44.9 +/- 5.9 versus 18.0 +/- 2.0 % annexin V-binding PMN after 16 hours). Soluble FcgammaRIIIb, in concert with FcgammaRIIIb / anti-FcgammaRIIIb IC, produced similar effects in that the percentage of annexin V-binding PMN declined to 16.0 +/-1.9 %. It was thus suggested that FcgammaRIIIb / anti-FcgammaRIIIb IC inserted the Fc region of their IgG into the membrane FcgammaRIIIb. Such an interpretation is consistent with our finding that, whereas aggregated IgG and anti-FcgammaRIIIb monoclonal Ab prevented membrane FcgammaRIIIb / IC interaction, neither soluble FcgammaRIIIb, nor anti-cgammaRII did so. We conclude that the function and the life span of PMN are influenced synergistically by soluble FcgammaRIIIb and anti-FcgammaRIIIb autoAb.