Involvement of hyposialylated immunoglobulins in the inactivation of alpha 1-proteinase inhibitor.
The elastase inhibitory capacity of alpha 1-proteinase inhibitor (alpha 1-PI) was measured, using a direct and reproducible method, with phagocytic cells maintained in the tissue culture plate through the assay. The oxidative inactivation of alpha 1-PI is known to be mediated by the action of myeloperoxidase (MPO). The fact that hyposialylated IgG (hs IgG) induce the release of MPO prompted us to investigate the effects of such hs IgG on the inhibitory capacity of alpha 1-PI. The results show that 1-PI inactivation was observed only when phagocytic cells were activated by aggregated hs IgG, and not by unaggregated hs IgG. These observations indicate that hyposialylation should be completed by aggregation to perpetuate the oxidative reactions characteristic of inflammatory diseases.
D001798:Blood Proteins / Q000494:pharmacology*; D002478:Cells, Cultured; D006801:Humans; D007074:Immunoglobulin G; D010084:Oxidation-Reduction; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D009195:Peroxidase / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010586:Phagocytes / Q000187:drug effects / Q000378:metabolism*; D012794:Sialic Acids; D013329:Structure-Activity Relationship; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D007074:Immunoglobulin G; D012794:Sialic Acids; D000515:alpha 1-Antitrypsin; D010544:Peroxidases; D009195:Peroxidase; D010196:Pancreatic Elastase; D013755:Tetradecanoylphorbol Acetate