6533b85dfe1ef96bd12be9f9

RESEARCH PRODUCT

Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis.

Anna MódManfred P. DierichJános GergelyGyorgy FüstSusan R. Hollán

subject

LeukemiaPhagocytosisImmunologyAlpha (ethology)Blood DonorsHematologyComplement receptorComplement C3Saccharomyces cerevisiaeCarbohydrateBiologyOpsonin ProteinsYeastPeripheral bloodMonocytesImmune systemBiochemistryPhagocytosisRosette formationalpha 1-AntitrypsinImmunology and AllergyHumans

description

Abstract In a previous investigation, inhibition of complement-dependent rosette formation by alpha1-antitrypsin (α1-AT) was observed, and it was demonstrated that α1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined. Purified α1-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 α1-AT. It was demonstrated that α1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α1-AT may have an impact on various immune functions involving complement receptors.

10.1016/s0171-2985(81)80005-8https://pubmed.ncbi.nlm.nih.gov/7016739