The interaction of ethanol with human monocyte IgG-Fc receptors, characterized by monoclonal antibodies raised against two distinct receptor subpopulations.

Human blood monocytes (Mo) in medium containing 10% autologous serum were exposed to ethanol (160 mM) at 37 degrees C for 15 min. After being washed, the cells were incubated with murine monoclonal antibodies (MoAb), one binding to the 40 kDa Fc receptor (FcR) (MoAb IV3) and the other to the 72 kDa FcR (MoAb 32). The incubation was performed with and without excess of human or rabbit IgG. The amount of receptor-bound MoAb was evaluated by fluorescein isothiocyanate (FITC)-labelled anti-mouse IgG. Most control Mo bound MoAb IV3 (90 +/- 8% stained cells) while only 52 +/- 2% Mo were positively stained by MoAb 32. The staining increased in the presence of human IgG in the assay mixtures. Pre-incubation with 160 mM ethanol reduced the MoAb IV3 binding (61 +/- 2% stained cells), but had no significant effect on the binding of MoAb 32. Wash-out experiments indicated normalization of receptor function (MoAb IV3 binding) after 4 h. Treatment of medium or serum with ethanol before incubation of the Mo had no effect. It was concluded that a brief exposure of human Mo to ethanol leads to changes in a subpopulation of IgG FcR. Since these changes appeared when MoAb were used against the receptors, they probably represent a decrease in functional receptors and not changes in affinity.