Phagocytosis by human monocytes of particles activating the alternative pathway of complement.
The phagocytosis of particles activating the alternative pathway of complement by human monocytes cultured under serum-free conditions was studied. In contrast to native zymosan particles, which were easily ingested, rabbit erythrocytes and agarose beads had to be coated with C3b or C3bi to be engulfed by the monocytes. The binding and ingestion by monocytes of particles coated with C3bi were greater than for the same particles coated with the equivalent amount of C3b. The binding and uptake of rabbit erythrocytes and agarose beads were proportional to the amount of C3b or C3bi on the particles. In contrast to the complement activator particles, C3b- and C3bi-coated sheep erythrocytes, which are non-activators, were not ingested by the monocytes, although attachment to the monocytes took place. The presence of methylamine or cobra venom factor, which are complement inhibitors, strongly reduced the ingestion of native zymosan by the monocytes, whereas the uptake of C3b- or C3bi-coated zymosan particles were only weakly affected. This suggests that the binding of native zymosan to monocytes is sensitive to interference from a cell-derived alternative pathway C3 convertase (C3bBb). Binding and uptake of activators by human monocytes via complement receptor(s) are discussed.
D000818:Animals; D001665:Binding Sites; D003167:Complement Activation; D003179:Complement C3b / Q000378:metabolism; D003180:Complement C3b Inactivator Proteins / Q000378:metabolism; D003170:Complement Pathway, Alternative; D004912:Erythrocytes / Q000276:immunology / Q000378:metabolism; D006801:Humans; D009000:Monocytes / Q000276:immunology* / Q000378:metabolism; D010587:Phagocytosis; D011817:Rabbits; D012685:Sepharose / Q000276:immunology / Q000378:metabolism; D012756:Sheep; D015054:Zymosan / Q000276:immunology / Q000378:metabolism
D003180:Complement C3b Inactivator Proteins; D003179:Complement C3b; D015054:Zymosan; D012685:Sepharose