Platelet-activating factor enhances complement-dependent phagocytosis of diamide-treated erythrocytes by human monocytes through activation of protein kinase C and phosphorylation of complement receptor type one (CR1).

摘要: Abstract Oligomerization of band 3 protein has been recently indicated as an early event in senescent or damaged red cell membrane followed by specific deposition anti-band antibodies and binding complement C3 fragments. The 3-anti-band 3-C3b complex is recognized homologous monocytes, phagocytosis ensues. This study shows that recognition the monocyte C3b receptor type one (CR1) plays a crucial role process removal cells. Indeed, blocking CR1 with anti-CR1 monoclonal antibody abrogated diamide-treated Platelet-activating factor (PAF) phospholipid mediator involved inflammatory processes. Nanomolar (R)-PAF enhanced CR1-dependent human sheep cells coated C3b, induced fast translocation kinase C to compartment, stimulated phosphorylation CR1. biologically inert lyso-PAF enantiomer (S)-PAF were inactive. PAF antagonists inhibitors blocked enhancement PAF. Protein translocation, CR1, stimulation this active state capable mediating represent novel pathway which interferes homeostasis possibly modulates reactions host mechanisms against infections.