Recombinant interferons increase macrophage Fc receptor capacity.
We utilized recombinant interferon preparations to confirm and extend our previous findings that biochemically purified preparations of interferon augment Fc receptor (FcR)-mediated functions. Five different recombinant human alpha-interferons (IFN) were tested and increased Fc-mediated phagocytosis and binding of opsonized erythrocytes with varying efficiencies. We found, however, that when the different alpha-IFN species were ranked with respect to their FcR-enhancing activity, their hierarchy differed from those reported for antiviral, antiproliferative, and NK cell-inducing activities. Recombinant murine gamma-IFN was also found to increase Fc-mediated phagocytosis, but was significantly more potent than either beta-IFN or recombinant alpha-IFN when compared on the basis of antiviral activity. A comparison of the amino acid sequences of the recombinant IFN may help define functional domains of the molecule.
D000818:Animals; D005260:Female; D006801:Humans; D007370:Interferon Type I / Q000302:isolation & purification / Q000494:pharmacology* / Q000502:physiology; D007371:Interferon-gamma / Q000302:isolation & purification / Q000494:pharmacology* / Q000502:physiology; D008264:Macrophages / Q000378:metabolism*; D051379:Mice; D008809:Mice, Inbred C3H; D010587:Phagocytosis / Q000187:drug effects; D011961:Receptors, Fc / Q000032:analysis / Q000187:drug effects* / Q000502:physiology; D011995:Recombination, Genetic
D007370:Interferon Type I; D011961:Receptors, Fc; D007371:Interferon-gamma