title: Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis.
abstract: In a previous investigation, inhibition of complement-dependent rosette formation by alpha 1-antitrypsin (alpha 1-AT) was observed, and it was demonstrated that alpha 1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of alpha 1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined. Purified alpha 1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by alpha 1-AT. It was demonstrated that alpha 1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that alpha 1-AT may have an impact on various immune functions involving complement receptors.
mesh_terms: D001782:Blood Donors; D003176:Complement C3 / Q000378:metabolism*; D006801:Humans; D007938:Leukemia / Q000097:blood; D009000:Monocytes / Q000276:immunology; D009895:Opsonin Proteins; D010587:Phagocytosis; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D000515:alpha 1-Antitrypsin / Q000494:pharmacology*
chemical_list: D003176:Complement C3; D009895:Opsonin Proteins; D000515:alpha 1-Antitrypsin