Recombinant human leukocyte interferon modulates neutrophil function in vitro.

Recombinant human interferon-alpha 2 (rIFN-alpha A) was evaluated as a modulator of neutrophil functions. Neutrophils treated with rIFN-alpha A for 1 h in vitro showed reduced chemiluminescence (CL) and aggregation in response to phagocytosis. In contrast, when certain soluble stimuli [f-met-leu-phe (fMLP) or leukotriene B4] were used, rIFN-alpha A treatment conferred a doubling of CL. This was paralleled by a similar increase in superoxide anion production and a 56% increase of release of beta-glucuronidase and lysozyme. The NBT test showed that IFN treatment did not increase the number of responding neutrophils. However, there was a significant increase in the displaceable binding of fML[3H]P. Enzyme release, aggregation, and CL in response to other soluble stimuli, the ionophore A23187 and phorbol myristate acetate were unaffected by IFN treatment. Likewise, chemotaxis was not affected. Thus, phagocytosis-associated events and aggregation were hampered by rIFN-alpha A whereas secretory responses to receptor-dependent soluble stimuli were augmented. The mechanism for the latter is most likely dependent on the observed modulation of binding of fMLP to its receptor.