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The transcriptional nuclear factor binding to the Y box of human leukocyte antigen genes (NF-Y) for the  C5a receptor  ( C5aR ) gene is active in erythroblasts. However, the roles of the  C5aR  in erythropoiesis are unclear. We have previously demonstrated that apoptotic cell-derived ribosomal protein  S19  ( RP S19 ) oligomers exhibit extraribosomal functions in promoting monocyte chemotaxis and proapoptosis via the  C5aR  without receptor internalisation. In contrast to the extraribosomal functions of the  RP S19 , a proapoptotic signal in pro-EBs, which is caused by mutations in the  RP S19  gene, is associated with the inherited erythroblastopenia, Diamond-Blackfan anaemia. In this study, we detected  C5aR  expression and  RP S19  oligomer generation in human erythroleukemia K562 cells during haemin-induced erythropoiesis. Under monocell culture conditions, the differentiation into K562 erythrocyte-like cells was enhanced following the overexpression of Wild-type  RP S19 . Conversely, the differentiation was repressed following the overexpression of mutant  RP S19 . An  RP S19  oligomer inhibitor and a  C5aR  inhibitor blocked the association of the K562 basophilic EB-like cells and the THP-1 macrophage-like cells under coculture conditions. When bound to  RP S19  oligomers, the  C5aR  may exhibit dual functions as a connector for the EB-macrophage island and as a sensor for EB differentiation in the bone marrow.

clinical and developmental immunology/clinical and developmental immunology

Dual Functions of the C5a Receptor as a Connector for the K562 Erythroblast-Like Cell-THP-1 Macrophage-Like Cell Island and as a Sensor for the Differentiation of the K562 Erythroblast-Like Cell during Haemin-Induced Erythropoiesis